Full text data of CEACAM1
CEACAM1
(BGP, BGP1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1; BGP-1; CD66a; Flags: Precursor)
Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1; BGP-1; CD66a; Flags: Precursor)
Comments
Isoform P13688-10 was detected.
Isoform P13688-10 was detected.
UniProt
P13688
ID CEAM1_HUMAN Reviewed; 526 AA.
AC P13688; A6NE38; A8MY49; O60430; Q069I7; Q13854; Q13857; Q13858;
read moreAC Q13859; Q13860; Q15600; Q15601; Q16170; Q5UB49; Q7KYP5; Q96CA7;
AC Q9UQV9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 22-JAN-2014, entry version 153.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 1;
DE AltName: Full=Biliary glycoprotein 1;
DE Short=BGP-1;
DE AltName: CD_antigen=CD66a;
DE Flags: Precursor;
GN Name=CEACAM1; Synonyms=BGP, BGP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2457922; DOI=10.1073/pnas.85.18.6959;
RA Hinoda Y., Neumaier M., Hefta S.A., Drzeniek Z., Wagener C.,
RA Shively L., Hefta L.J.F., Shively J.E., Paxton R.J.;
RT "Molecular cloning of a cDNA coding biliary glycoprotein I: primary
RT structure of a glycoprotein immunologically crossreactive with
RT carcinoembryonic antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6959-6963(1988).
RN [2]
RP ERRATUM, AND SEQUENCE REVISION.
RA Hinoda Y., Neumaier M., Hefta S.A., Drzeniek Z., Wagener C.,
RA Shively L., Hefta L.J.F., Shively J.E., Paxton R.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 86:1668-1668(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6 AND 8).
RX PubMed=2537311; DOI=10.1083/jcb.108.2.267;
RA Barnett T.R., Kretschmer A., Austen D.A., Goebel S.J., Hart J.T.,
RA Elting J.J., Kamarck M.E.;
RT "Carcinoembryonic antigens: alternative splicing accounts for the
RT multiple mRNAs that code for novel members of the carcinoembryonic
RT antigen family.";
RL J. Cell Biol. 108:267-276(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION.
RC TISSUE=Leukocyte;
RX PubMed=2025273; DOI=10.1016/S0006-291X(05)80223-2;
RA Kuroki M., Arakawa F., Matsuo Y., Oikawa S., Nakazato H., Matsuoka Y.;
RT "Three novel molecular forms of biliary glycoprotein deduced from cDNA
RT clones from a human leukocyte library.";
RL Biochem. Biophys. Res. Commun. 176:578-585(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 293-494 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 293-458 (ISOFORM
RP 9), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 293-458, AND GLYCOSYLATION.
RX PubMed=8423792;
RA Barnett T.R., Drake L., Pickle W. II;
RT "Human biliary glycoprotein gene: characterization of a family of
RT novel alternatively spliced RNAs and their expressed proteins.";
RL Mol. Cell. Biol. 13:1273-1282(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), AND SUBCELLULAR LOCATION.
RC TISSUE=Colon adenocarcinoma;
RX PubMed=8018919;
RA Watt S.M., Fawcett J., Murdoch S.J., Teixeira A.M., Gschmeissner S.E.,
RA Hajibagheri N.M., Simmons D.L.;
RT "CD66 identifies the biliary glycoprotein (BGP) adhesion molecule:
RT cloning, expression, and adhesion functions of the BGPc splice
RT variant.";
RL Blood 84:200-210(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC TISSUE=Monocyte;
RA Kuroki M., Matsuo Y., Misumi Y., Oikawa S., Matsuoka Y.;
RT "A new isoform of human biliary glycoprotein (BGP) containing a domain
RT encoded by an Alu-like sequence.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11).
RA Long S., Phillips A., Ma H., Paoni N.F., Wong-Staal F., Fan W.;
RT "Isolation of the cDNA encoding a putative carcinoembryonic antigen-
RT related cell adhesion molecule 1 short form 3 (CEACAM1-3S).";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-35; VAL-83;
RP HIS-123 AND ARG-376.
RG SeattleSNPs variation discovery resource;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21, AND DISEASE.
RX PubMed=8055923; DOI=10.1111/j.1432-1033.1994.tb19022.x;
RA Hauck W., Nedellec P., Turbide C., Stanners C.P., Barnett T.R.,
RA Beauchemin N.;
RT "Transcriptional control of the human biliary glycoprotein gene, a CEA
RT gene family member down-regulated in colorectal carcinomas.";
RL Eur. J. Biochem. 223:529-541(1994).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=7628460; DOI=10.1111/j.1432-1033.1995.tb20676.x;
RA Nedellec P., Turbide C., Beauchemin N.;
RT "Characterization and transcriptional activity of the mouse biliary
RT glycoprotein 1 gene, a carcinoembryonic antigen-related gene.";
RL Eur. J. Biochem. 231:104-114(1995).
RN [15]
RP NOMENCLATURE OF ALTERNATIVE SPLICING ISOFORMS.
RX PubMed=11501563; DOI=10.1006/excr.1999.4610;
RA Beauchemin N., Draber P., Dveksler G., Gold P., Gray-Owen S.,
RA Grunert F., Hammarstrom S., Holmes K.V., Karlsson A., Kuroki M.,
RA Lin S.H., Lucka L., Najjar S.M., Neumaier M., Obrink B., Shively J.E.,
RA Skubitz K.M., Stanners C.P., Thomas P., Thompson J.A., Virji M.,
RA von Kleist S., Wagener C., Watt S., Zimmermann W.;
RT "Redefined nomenclature for members of the carcinoembryonic antigen
RT family.";
RL Exp. Cell Res. 252:243-249(1999).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104 AND ASN-111, AND MASS
RP SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-152; ASN-208; ASN-224;
RP ASN-363; ASN-378 AND ASN-405, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 34-141.
RX PubMed=16929097; DOI=10.1107/S0907444906020737;
RA Fedarovich A., Tomberg J., Nicholas R.A., Davies C.;
RT "Structure of the N-terminal domain of human CEACAM1: binding target
RT of the opacity proteins during invasion of Neisseria meningitidis and
RT N. gonorrhoeae.";
RL Acta Crystallogr. D 62:971-979(2006).
CC -!- INTERACTION:
CC Q16568:CARTPT; NbExp=3; IntAct=EBI-4314481, EBI-4314526;
CC P40199:CEACAM6; NbExp=2; IntAct=EBI-4314481, EBI-4314501;
CC Q8GH87:uspa1 (xeno); NbExp=12; IntAct=EBI-4314481, EBI-7936357;
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
CC -!- SUBCELLULAR LOCATION: Isoform 3: Secreted.
CC -!- SUBCELLULAR LOCATION: Isoform 4: Secreted.
CC -!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: Isoform 6: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: Isoform 7: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: Isoform 8: Cell membrane; Single-pass type I
CC membrane protein. Note=Localizes to sites of cell-cell contact.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=1; Synonyms=BGPa, CEACAM1-4L, TM1-CEA;
CC IsoId=P13688-1; Sequence=Displayed;
CC Name=2; Synonyms=BGPg, CEACAM1-4C1;
CC IsoId=P13688-2; Sequence=VSP_002482, VSP_002483;
CC Name=3; Synonyms=BGPh, CEACAM1-3;
CC IsoId=P13688-3; Sequence=VSP_002478, VSP_002479;
CC Name=4; Synonyms=BGPi, CEACAM1-3C2;
CC IsoId=P13688-4; Sequence=VSP_002480, VSP_002481;
CC Name=5; Synonyms=BGPy, CEACAM1-3AL;
CC IsoId=P13688-5; Sequence=VSP_009227;
CC Note=Ref.5 (AAA57143) sequence is in conflict in positions:
CC 323:N->L, 337:Q->E. Ref.7 (BAA02063) sequence is in conflict in
CC position: 329:R->G;
CC Name=6; Synonyms=BGPb, CEACAM1-3L, TM2-CEA;
CC IsoId=P13688-6; Sequence=VSP_010938;
CC Name=7; Synonyms=BGPx, CEACAM1-1L;
CC IsoId=P13688-7; Sequence=VSP_012222;
CC Name=8; Synonyms=BGPc, CEACAM1-4S, TM3-CEA;
CC IsoId=P13688-8; Sequence=VSP_040572, VSP_040574;
CC Name=9; Synonyms=BGPz, CEACAM1-3AS;
CC IsoId=P13688-9; Sequence=VSP_040571, VSP_040572, VSP_040574;
CC Name=10;
CC IsoId=P13688-10; Sequence=VSP_040573, VSP_040575;
CC Note=No experimental confirmation available;
CC Name=11; Synonyms=BGPd, CEACAM1-3S;
CC IsoId=P13688-11; Sequence=VSP_010938, VSP_040572, VSP_040574;
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57141.1; Type=Erroneous gene model prediction;
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/ceacam1/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CEACAM1ID40044ch19q13.html";
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DR EMBL; J03858; AAA51826.1; -; mRNA.
DR EMBL; X14831; CAA32940.1; -; mRNA.
DR EMBL; X16354; CAA34404.1; -; mRNA.
DR EMBL; X16356; CAA34405.1; -; mRNA.
DR EMBL; D90311; BAA14341.1; -; mRNA.
DR EMBL; D90312; BAA14342.1; -; mRNA.
DR EMBL; D90313; BAA14343.1; -; mRNA.
DR EMBL; M69176; AAA51825.1; -; mRNA.
DR EMBL; M72238; AAA58393.1; -; mRNA.
DR EMBL; M72238; AAA58394.1; -; mRNA.
DR EMBL; M76741; AAA57141.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M76742; AAA57142.1; -; mRNA.
DR EMBL; M76743; AAA57143.1; -; mRNA.
DR EMBL; M76744; AAA57144.1; -; mRNA.
DR EMBL; S71326; AAB31183.1; -; mRNA.
DR EMBL; D12502; BAA02063.1; -; mRNA.
DR EMBL; AY766113; AAV34600.1; -; mRNA.
DR EMBL; DQ989182; ABI75349.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18433.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18434.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18435.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18436.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18437.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18438.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18439.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57137.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57140.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57141.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57143.1; -; Genomic_DNA.
DR EMBL; BC014473; AAH14473.1; -; mRNA.
DR EMBL; X67277; CAA47694.1; -; Genomic_DNA.
DR PIR; A32164; A32164.
DR PIR; B48078; B48078.
DR PIR; JH0394; JH0394.
DR PIR; JH0395; JH0395.
DR PIR; JH0396; JH0396.
DR RefSeq; NP_001020083.1; NM_001024912.2.
DR RefSeq; NP_001171742.1; NM_001184813.1.
DR RefSeq; NP_001171744.1; NM_001184815.1.
DR RefSeq; NP_001171745.1; NM_001184816.1.
DR RefSeq; NP_001192273.1; NM_001205344.1.
DR RefSeq; NP_001703.2; NM_001712.4.
DR UniGene; Hs.512682; -.
DR PDB; 2GK2; X-ray; 2.20 A; A/B=34-141.
DR PDBsum; 2GK2; -.
DR ProteinModelPortal; P13688; -.
DR SMR; P13688; 34-414.
DR IntAct; P13688; 6.
DR MINT; MINT-5002435; -.
DR STRING; 9606.ENSP00000161559; -.
DR DrugBank; DB00113; Arcitumomab.
DR PhosphoSite; P13688; -.
DR DMDM; 399116; -.
DR PaxDb; P13688; -.
DR PRIDE; P13688; -.
DR DNASU; 634; -.
DR Ensembl; ENST00000161559; ENSP00000161559; ENSG00000079385.
DR Ensembl; ENST00000351134; ENSP00000325946; ENSG00000079385.
DR Ensembl; ENST00000352591; ENSP00000244291; ENSG00000079385.
DR Ensembl; ENST00000358394; ENSP00000351165; ENSG00000079385.
DR Ensembl; ENST00000403444; ENSP00000384709; ENSG00000079385.
DR Ensembl; ENST00000403461; ENSP00000384083; ENSG00000079385.
DR Ensembl; ENST00000599389; ENSP00000471918; ENSG00000079385.
DR GeneID; 634; -.
DR KEGG; hsa:634; -.
DR UCSC; uc002otv.3; human.
DR CTD; 634; -.
DR GeneCards; GC19M043009; -.
DR H-InvDB; HIX0017795; -.
DR HGNC; HGNC:1814; CEACAM1.
DR HPA; CAB002146; -.
DR HPA; HPA011041; -.
DR MIM; 109770; gene.
DR neXtProt; NX_P13688; -.
DR PharmGKB; PA26358; -.
DR eggNOG; NOG149650; -.
DR HOVERGEN; HBG007922; -.
DR KO; K06499; -.
DR OMA; NTSYLWS; -.
DR OrthoDB; EOG74BJS7; -.
DR EvolutionaryTrace; P13688; -.
DR GeneWiki; CEACAM1; -.
DR GenomeRNAi; 634; -.
DR NextBio; 2562; -.
DR PRO; PR:P13688; -.
DR ArrayExpress; P13688; -.
DR Bgee; P13688; -.
DR CleanEx; HS_CEACAM1; -.
DR Genevestigator; P13688; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; NAS:UniProtKB.
DR GO; GO:0016477; P:cell migration; NAS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion; NAS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Polymorphism;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 34
FT CHAIN 35 526 Carcinoembryonic antigen-related cell
FT adhesion molecule 1.
FT /FTId=PRO_0000014562.
FT TOPO_DOM 35 428 Extracellular (Potential).
FT TRANSMEM 429 452 Helical; (Potential).
FT TOPO_DOM 453 526 Cytoplasmic (Potential).
FT DOMAIN 35 142 Ig-like V-type.
FT DOMAIN 145 232 Ig-like C2-type 1.
FT DOMAIN 237 317 Ig-like C2-type 2.
FT DOMAIN 323 413 Ig-like C2-type 3.
FT MOD_RES 35 35 Pyrrolidone carboxylic acid.
FT CARBOHYD 104 104 N-linked (GlcNAc...).
FT CARBOHYD 111 111 N-linked (GlcNAc...).
FT CARBOHYD 115 115 N-linked (GlcNAc...).
FT CARBOHYD 152 152 N-linked (GlcNAc...).
FT CARBOHYD 182 182 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 197 197 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 208 208 N-linked (GlcNAc...).
FT CARBOHYD 224 224 N-linked (GlcNAc...).
FT CARBOHYD 232 232 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 254 254 N-linked (GlcNAc...).
FT CARBOHYD 274 274 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 288 288 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 292 292 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 302 302 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 309 309 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 345 345 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 351 351 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 363 363 N-linked (GlcNAc...).
FT CARBOHYD 378 378 N-linked (GlcNAc...).
FT CARBOHYD 405 405 N-linked (GlcNAc...).
FT DISULFID 167 215 Probable.
FT DISULFID 259 299 Probable.
FT DISULFID 348 396 Probable.
FT VAR_SEQ 143 416 Missing (in isoform 7).
FT /FTId=VSP_012222.
FT VAR_SEQ 320 416 ELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWF
FT FKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNP
FT ISKNQSDPIMLNVNY -> D (in isoform 6 and
FT isoform 11).
FT /FTId=VSP_010938.
FT VAR_SEQ 320 321 EL -> GK (in isoform 3).
FT /FTId=VSP_002478.
FT VAR_SEQ 321 416 LSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFF
FT KNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPI
FT SKNQSDPIMLNVNY -> RQNLTMLPRLDSNSWAQAILPSV
FT SQSAEITD (in isoform 5).
FT /FTId=VSP_009227.
FT VAR_SEQ 321 416 LSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFF
FT KNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPI
FT SKNQSDPIMLNVNY -> MAFHHVAKAGLKLLSSSNPPAST
FT SQSAKITD (in isoform 9).
FT /FTId=VSP_040571.
FT VAR_SEQ 321 351 LSPVVAKPQIKASKTTVTGDKDSVNLTCSTN -> SPVLGE
FT DEAVPGQHHPQHKPCQEGGCWDVLV (in isoform 4).
FT /FTId=VSP_002480.
FT VAR_SEQ 322 526 Missing (in isoform 3).
FT /FTId=VSP_002479.
FT VAR_SEQ 352 526 Missing (in isoform 4).
FT /FTId=VSP_002481.
FT VAR_SEQ 416 417 YN -> CK (in isoform 2).
FT /FTId=VSP_002482.
FT VAR_SEQ 418 526 Missing (in isoform 2).
FT /FTId=VSP_002483.
FT VAR_SEQ 459 464 RASDQR -> SSGPLQ (in isoform 8, isoform 9
FT and isoform 11).
FT /FTId=VSP_040572.
FT VAR_SEQ 460 468 ASDQRDLTE -> TTPMTHLTR (in isoform 10).
FT /FTId=VSP_040573.
FT VAR_SEQ 465 526 Missing (in isoform 8, isoform 9 and
FT isoform 11).
FT /FTId=VSP_040574.
FT VAR_SEQ 469 526 Missing (in isoform 10).
FT /FTId=VSP_040575.
FT VARIANT 35 35 Q -> K (in dbSNP:rs8111171).
FT /FTId=VAR_049844.
FT VARIANT 83 83 A -> V (in dbSNP:rs8110904).
FT /FTId=VAR_049845.
FT VARIANT 123 123 Q -> H (in dbSNP:rs8111468).
FT /FTId=VAR_049846.
FT VARIANT 376 376 Q -> R (in dbSNP:rs41355544).
FT /FTId=VAR_049847.
FT CONFLICT 142 142 P -> H (in Ref. 5; AAA57142).
FT CONFLICT 246 246 D -> Y (in Ref. 7; BAA02063).
FT STRAND 37 45
FT STRAND 51 56
FT STRAND 60 72
FT HELIX 75 77
FT STRAND 78 83
FT TURN 84 87
FT STRAND 88 91
FT STRAND 99 101
FT STRAND 107 109
FT HELIX 114 116
FT STRAND 118 126
FT STRAND 132 140
SQ SEQUENCE 526 AA; 57560 MW; CAD1B2328D069AF8 CRC64;
MGHLSAPLHR VRVPWQGLLL TASLLTFWNP PTTAQLTTES MPFNVAEGKE VLLLVHNLPQ
QLFGYSWYKG ERVDGNRQIV GYAIGTQQAT PGPANSGRET IYPNASLLIQ NVTQNDTGFY
TLQVIKSDLV NEEATGQFHV YPELPKPSIS SNNSNPVEDK DAVAFTCEPE TQDTTYLWWI
NNQSLPVSPR LQLSNGNRTL TLLSVTRNDT GPYECEIQNP VSANRSDPVT LNVTYGPDTP
TISPSDTYYR PGANLSLSCY AASNPPAQYS WLINGTFQQS TQELFIPNIT VNNSGSYTCH
ANNSVTGCNR TTVKTIIVTE LSPVVAKPQI KASKTTVTGD KDSVNLTCST NDTGISIRWF
FKNQSLPSSE RMKLSQGNTT LSINPVKRED AGTYWCEVFN PISKNQSDPI MLNVNYNALP
QENGLSPGAI AGIVIGVVAL VALIAVALAC FLHFGKTGRA SDQRDLTEHK PSVSNHTQDH
SNDPPNKMNE VTYSTLNFEA QQPTQPTSAS PSLTATEIIY SEVKKQ
//
ID CEAM1_HUMAN Reviewed; 526 AA.
AC P13688; A6NE38; A8MY49; O60430; Q069I7; Q13854; Q13857; Q13858;
read moreAC Q13859; Q13860; Q15600; Q15601; Q16170; Q5UB49; Q7KYP5; Q96CA7;
AC Q9UQV9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 22-JAN-2014, entry version 153.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 1;
DE AltName: Full=Biliary glycoprotein 1;
DE Short=BGP-1;
DE AltName: CD_antigen=CD66a;
DE Flags: Precursor;
GN Name=CEACAM1; Synonyms=BGP, BGP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2457922; DOI=10.1073/pnas.85.18.6959;
RA Hinoda Y., Neumaier M., Hefta S.A., Drzeniek Z., Wagener C.,
RA Shively L., Hefta L.J.F., Shively J.E., Paxton R.J.;
RT "Molecular cloning of a cDNA coding biliary glycoprotein I: primary
RT structure of a glycoprotein immunologically crossreactive with
RT carcinoembryonic antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6959-6963(1988).
RN [2]
RP ERRATUM, AND SEQUENCE REVISION.
RA Hinoda Y., Neumaier M., Hefta S.A., Drzeniek Z., Wagener C.,
RA Shively L., Hefta L.J.F., Shively J.E., Paxton R.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 86:1668-1668(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6 AND 8).
RX PubMed=2537311; DOI=10.1083/jcb.108.2.267;
RA Barnett T.R., Kretschmer A., Austen D.A., Goebel S.J., Hart J.T.,
RA Elting J.J., Kamarck M.E.;
RT "Carcinoembryonic antigens: alternative splicing accounts for the
RT multiple mRNAs that code for novel members of the carcinoembryonic
RT antigen family.";
RL J. Cell Biol. 108:267-276(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION.
RC TISSUE=Leukocyte;
RX PubMed=2025273; DOI=10.1016/S0006-291X(05)80223-2;
RA Kuroki M., Arakawa F., Matsuo Y., Oikawa S., Nakazato H., Matsuoka Y.;
RT "Three novel molecular forms of biliary glycoprotein deduced from cDNA
RT clones from a human leukocyte library.";
RL Biochem. Biophys. Res. Commun. 176:578-585(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 293-494 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 293-458 (ISOFORM
RP 9), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 293-458, AND GLYCOSYLATION.
RX PubMed=8423792;
RA Barnett T.R., Drake L., Pickle W. II;
RT "Human biliary glycoprotein gene: characterization of a family of
RT novel alternatively spliced RNAs and their expressed proteins.";
RL Mol. Cell. Biol. 13:1273-1282(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), AND SUBCELLULAR LOCATION.
RC TISSUE=Colon adenocarcinoma;
RX PubMed=8018919;
RA Watt S.M., Fawcett J., Murdoch S.J., Teixeira A.M., Gschmeissner S.E.,
RA Hajibagheri N.M., Simmons D.L.;
RT "CD66 identifies the biliary glycoprotein (BGP) adhesion molecule:
RT cloning, expression, and adhesion functions of the BGPc splice
RT variant.";
RL Blood 84:200-210(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC TISSUE=Monocyte;
RA Kuroki M., Matsuo Y., Misumi Y., Oikawa S., Matsuoka Y.;
RT "A new isoform of human biliary glycoprotein (BGP) containing a domain
RT encoded by an Alu-like sequence.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11).
RA Long S., Phillips A., Ma H., Paoni N.F., Wong-Staal F., Fan W.;
RT "Isolation of the cDNA encoding a putative carcinoembryonic antigen-
RT related cell adhesion molecule 1 short form 3 (CEACAM1-3S).";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-35; VAL-83;
RP HIS-123 AND ARG-376.
RG SeattleSNPs variation discovery resource;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21, AND DISEASE.
RX PubMed=8055923; DOI=10.1111/j.1432-1033.1994.tb19022.x;
RA Hauck W., Nedellec P., Turbide C., Stanners C.P., Barnett T.R.,
RA Beauchemin N.;
RT "Transcriptional control of the human biliary glycoprotein gene, a CEA
RT gene family member down-regulated in colorectal carcinomas.";
RL Eur. J. Biochem. 223:529-541(1994).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=7628460; DOI=10.1111/j.1432-1033.1995.tb20676.x;
RA Nedellec P., Turbide C., Beauchemin N.;
RT "Characterization and transcriptional activity of the mouse biliary
RT glycoprotein 1 gene, a carcinoembryonic antigen-related gene.";
RL Eur. J. Biochem. 231:104-114(1995).
RN [15]
RP NOMENCLATURE OF ALTERNATIVE SPLICING ISOFORMS.
RX PubMed=11501563; DOI=10.1006/excr.1999.4610;
RA Beauchemin N., Draber P., Dveksler G., Gold P., Gray-Owen S.,
RA Grunert F., Hammarstrom S., Holmes K.V., Karlsson A., Kuroki M.,
RA Lin S.H., Lucka L., Najjar S.M., Neumaier M., Obrink B., Shively J.E.,
RA Skubitz K.M., Stanners C.P., Thomas P., Thompson J.A., Virji M.,
RA von Kleist S., Wagener C., Watt S., Zimmermann W.;
RT "Redefined nomenclature for members of the carcinoembryonic antigen
RT family.";
RL Exp. Cell Res. 252:243-249(1999).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104 AND ASN-111, AND MASS
RP SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-152; ASN-208; ASN-224;
RP ASN-363; ASN-378 AND ASN-405, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 34-141.
RX PubMed=16929097; DOI=10.1107/S0907444906020737;
RA Fedarovich A., Tomberg J., Nicholas R.A., Davies C.;
RT "Structure of the N-terminal domain of human CEACAM1: binding target
RT of the opacity proteins during invasion of Neisseria meningitidis and
RT N. gonorrhoeae.";
RL Acta Crystallogr. D 62:971-979(2006).
CC -!- INTERACTION:
CC Q16568:CARTPT; NbExp=3; IntAct=EBI-4314481, EBI-4314526;
CC P40199:CEACAM6; NbExp=2; IntAct=EBI-4314481, EBI-4314501;
CC Q8GH87:uspa1 (xeno); NbExp=12; IntAct=EBI-4314481, EBI-7936357;
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
CC -!- SUBCELLULAR LOCATION: Isoform 3: Secreted.
CC -!- SUBCELLULAR LOCATION: Isoform 4: Secreted.
CC -!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: Isoform 6: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: Isoform 7: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: Isoform 8: Cell membrane; Single-pass type I
CC membrane protein. Note=Localizes to sites of cell-cell contact.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=1; Synonyms=BGPa, CEACAM1-4L, TM1-CEA;
CC IsoId=P13688-1; Sequence=Displayed;
CC Name=2; Synonyms=BGPg, CEACAM1-4C1;
CC IsoId=P13688-2; Sequence=VSP_002482, VSP_002483;
CC Name=3; Synonyms=BGPh, CEACAM1-3;
CC IsoId=P13688-3; Sequence=VSP_002478, VSP_002479;
CC Name=4; Synonyms=BGPi, CEACAM1-3C2;
CC IsoId=P13688-4; Sequence=VSP_002480, VSP_002481;
CC Name=5; Synonyms=BGPy, CEACAM1-3AL;
CC IsoId=P13688-5; Sequence=VSP_009227;
CC Note=Ref.5 (AAA57143) sequence is in conflict in positions:
CC 323:N->L, 337:Q->E. Ref.7 (BAA02063) sequence is in conflict in
CC position: 329:R->G;
CC Name=6; Synonyms=BGPb, CEACAM1-3L, TM2-CEA;
CC IsoId=P13688-6; Sequence=VSP_010938;
CC Name=7; Synonyms=BGPx, CEACAM1-1L;
CC IsoId=P13688-7; Sequence=VSP_012222;
CC Name=8; Synonyms=BGPc, CEACAM1-4S, TM3-CEA;
CC IsoId=P13688-8; Sequence=VSP_040572, VSP_040574;
CC Name=9; Synonyms=BGPz, CEACAM1-3AS;
CC IsoId=P13688-9; Sequence=VSP_040571, VSP_040572, VSP_040574;
CC Name=10;
CC IsoId=P13688-10; Sequence=VSP_040573, VSP_040575;
CC Note=No experimental confirmation available;
CC Name=11; Synonyms=BGPd, CEACAM1-3S;
CC IsoId=P13688-11; Sequence=VSP_010938, VSP_040572, VSP_040574;
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57141.1; Type=Erroneous gene model prediction;
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/ceacam1/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CEACAM1ID40044ch19q13.html";
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DR EMBL; J03858; AAA51826.1; -; mRNA.
DR EMBL; X14831; CAA32940.1; -; mRNA.
DR EMBL; X16354; CAA34404.1; -; mRNA.
DR EMBL; X16356; CAA34405.1; -; mRNA.
DR EMBL; D90311; BAA14341.1; -; mRNA.
DR EMBL; D90312; BAA14342.1; -; mRNA.
DR EMBL; D90313; BAA14343.1; -; mRNA.
DR EMBL; M69176; AAA51825.1; -; mRNA.
DR EMBL; M72238; AAA58393.1; -; mRNA.
DR EMBL; M72238; AAA58394.1; -; mRNA.
DR EMBL; M76741; AAA57141.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M76742; AAA57142.1; -; mRNA.
DR EMBL; M76743; AAA57143.1; -; mRNA.
DR EMBL; M76744; AAA57144.1; -; mRNA.
DR EMBL; S71326; AAB31183.1; -; mRNA.
DR EMBL; D12502; BAA02063.1; -; mRNA.
DR EMBL; AY766113; AAV34600.1; -; mRNA.
DR EMBL; DQ989182; ABI75349.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18433.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18434.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18435.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18436.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18437.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18438.1; -; Genomic_DNA.
DR EMBL; AC004785; AAC18439.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57137.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57140.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57141.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57143.1; -; Genomic_DNA.
DR EMBL; BC014473; AAH14473.1; -; mRNA.
DR EMBL; X67277; CAA47694.1; -; Genomic_DNA.
DR PIR; A32164; A32164.
DR PIR; B48078; B48078.
DR PIR; JH0394; JH0394.
DR PIR; JH0395; JH0395.
DR PIR; JH0396; JH0396.
DR RefSeq; NP_001020083.1; NM_001024912.2.
DR RefSeq; NP_001171742.1; NM_001184813.1.
DR RefSeq; NP_001171744.1; NM_001184815.1.
DR RefSeq; NP_001171745.1; NM_001184816.1.
DR RefSeq; NP_001192273.1; NM_001205344.1.
DR RefSeq; NP_001703.2; NM_001712.4.
DR UniGene; Hs.512682; -.
DR PDB; 2GK2; X-ray; 2.20 A; A/B=34-141.
DR PDBsum; 2GK2; -.
DR ProteinModelPortal; P13688; -.
DR SMR; P13688; 34-414.
DR IntAct; P13688; 6.
DR MINT; MINT-5002435; -.
DR STRING; 9606.ENSP00000161559; -.
DR DrugBank; DB00113; Arcitumomab.
DR PhosphoSite; P13688; -.
DR DMDM; 399116; -.
DR PaxDb; P13688; -.
DR PRIDE; P13688; -.
DR DNASU; 634; -.
DR Ensembl; ENST00000161559; ENSP00000161559; ENSG00000079385.
DR Ensembl; ENST00000351134; ENSP00000325946; ENSG00000079385.
DR Ensembl; ENST00000352591; ENSP00000244291; ENSG00000079385.
DR Ensembl; ENST00000358394; ENSP00000351165; ENSG00000079385.
DR Ensembl; ENST00000403444; ENSP00000384709; ENSG00000079385.
DR Ensembl; ENST00000403461; ENSP00000384083; ENSG00000079385.
DR Ensembl; ENST00000599389; ENSP00000471918; ENSG00000079385.
DR GeneID; 634; -.
DR KEGG; hsa:634; -.
DR UCSC; uc002otv.3; human.
DR CTD; 634; -.
DR GeneCards; GC19M043009; -.
DR H-InvDB; HIX0017795; -.
DR HGNC; HGNC:1814; CEACAM1.
DR HPA; CAB002146; -.
DR HPA; HPA011041; -.
DR MIM; 109770; gene.
DR neXtProt; NX_P13688; -.
DR PharmGKB; PA26358; -.
DR eggNOG; NOG149650; -.
DR HOVERGEN; HBG007922; -.
DR KO; K06499; -.
DR OMA; NTSYLWS; -.
DR OrthoDB; EOG74BJS7; -.
DR EvolutionaryTrace; P13688; -.
DR GeneWiki; CEACAM1; -.
DR GenomeRNAi; 634; -.
DR NextBio; 2562; -.
DR PRO; PR:P13688; -.
DR ArrayExpress; P13688; -.
DR Bgee; P13688; -.
DR CleanEx; HS_CEACAM1; -.
DR Genevestigator; P13688; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; NAS:UniProtKB.
DR GO; GO:0016477; P:cell migration; NAS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion; NAS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Polymorphism;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 34
FT CHAIN 35 526 Carcinoembryonic antigen-related cell
FT adhesion molecule 1.
FT /FTId=PRO_0000014562.
FT TOPO_DOM 35 428 Extracellular (Potential).
FT TRANSMEM 429 452 Helical; (Potential).
FT TOPO_DOM 453 526 Cytoplasmic (Potential).
FT DOMAIN 35 142 Ig-like V-type.
FT DOMAIN 145 232 Ig-like C2-type 1.
FT DOMAIN 237 317 Ig-like C2-type 2.
FT DOMAIN 323 413 Ig-like C2-type 3.
FT MOD_RES 35 35 Pyrrolidone carboxylic acid.
FT CARBOHYD 104 104 N-linked (GlcNAc...).
FT CARBOHYD 111 111 N-linked (GlcNAc...).
FT CARBOHYD 115 115 N-linked (GlcNAc...).
FT CARBOHYD 152 152 N-linked (GlcNAc...).
FT CARBOHYD 182 182 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 197 197 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 208 208 N-linked (GlcNAc...).
FT CARBOHYD 224 224 N-linked (GlcNAc...).
FT CARBOHYD 232 232 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 254 254 N-linked (GlcNAc...).
FT CARBOHYD 274 274 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 288 288 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 292 292 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 302 302 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 309 309 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 345 345 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 351 351 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 363 363 N-linked (GlcNAc...).
FT CARBOHYD 378 378 N-linked (GlcNAc...).
FT CARBOHYD 405 405 N-linked (GlcNAc...).
FT DISULFID 167 215 Probable.
FT DISULFID 259 299 Probable.
FT DISULFID 348 396 Probable.
FT VAR_SEQ 143 416 Missing (in isoform 7).
FT /FTId=VSP_012222.
FT VAR_SEQ 320 416 ELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWF
FT FKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNP
FT ISKNQSDPIMLNVNY -> D (in isoform 6 and
FT isoform 11).
FT /FTId=VSP_010938.
FT VAR_SEQ 320 321 EL -> GK (in isoform 3).
FT /FTId=VSP_002478.
FT VAR_SEQ 321 416 LSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFF
FT KNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPI
FT SKNQSDPIMLNVNY -> RQNLTMLPRLDSNSWAQAILPSV
FT SQSAEITD (in isoform 5).
FT /FTId=VSP_009227.
FT VAR_SEQ 321 416 LSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFF
FT KNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPI
FT SKNQSDPIMLNVNY -> MAFHHVAKAGLKLLSSSNPPAST
FT SQSAKITD (in isoform 9).
FT /FTId=VSP_040571.
FT VAR_SEQ 321 351 LSPVVAKPQIKASKTTVTGDKDSVNLTCSTN -> SPVLGE
FT DEAVPGQHHPQHKPCQEGGCWDVLV (in isoform 4).
FT /FTId=VSP_002480.
FT VAR_SEQ 322 526 Missing (in isoform 3).
FT /FTId=VSP_002479.
FT VAR_SEQ 352 526 Missing (in isoform 4).
FT /FTId=VSP_002481.
FT VAR_SEQ 416 417 YN -> CK (in isoform 2).
FT /FTId=VSP_002482.
FT VAR_SEQ 418 526 Missing (in isoform 2).
FT /FTId=VSP_002483.
FT VAR_SEQ 459 464 RASDQR -> SSGPLQ (in isoform 8, isoform 9
FT and isoform 11).
FT /FTId=VSP_040572.
FT VAR_SEQ 460 468 ASDQRDLTE -> TTPMTHLTR (in isoform 10).
FT /FTId=VSP_040573.
FT VAR_SEQ 465 526 Missing (in isoform 8, isoform 9 and
FT isoform 11).
FT /FTId=VSP_040574.
FT VAR_SEQ 469 526 Missing (in isoform 10).
FT /FTId=VSP_040575.
FT VARIANT 35 35 Q -> K (in dbSNP:rs8111171).
FT /FTId=VAR_049844.
FT VARIANT 83 83 A -> V (in dbSNP:rs8110904).
FT /FTId=VAR_049845.
FT VARIANT 123 123 Q -> H (in dbSNP:rs8111468).
FT /FTId=VAR_049846.
FT VARIANT 376 376 Q -> R (in dbSNP:rs41355544).
FT /FTId=VAR_049847.
FT CONFLICT 142 142 P -> H (in Ref. 5; AAA57142).
FT CONFLICT 246 246 D -> Y (in Ref. 7; BAA02063).
FT STRAND 37 45
FT STRAND 51 56
FT STRAND 60 72
FT HELIX 75 77
FT STRAND 78 83
FT TURN 84 87
FT STRAND 88 91
FT STRAND 99 101
FT STRAND 107 109
FT HELIX 114 116
FT STRAND 118 126
FT STRAND 132 140
SQ SEQUENCE 526 AA; 57560 MW; CAD1B2328D069AF8 CRC64;
MGHLSAPLHR VRVPWQGLLL TASLLTFWNP PTTAQLTTES MPFNVAEGKE VLLLVHNLPQ
QLFGYSWYKG ERVDGNRQIV GYAIGTQQAT PGPANSGRET IYPNASLLIQ NVTQNDTGFY
TLQVIKSDLV NEEATGQFHV YPELPKPSIS SNNSNPVEDK DAVAFTCEPE TQDTTYLWWI
NNQSLPVSPR LQLSNGNRTL TLLSVTRNDT GPYECEIQNP VSANRSDPVT LNVTYGPDTP
TISPSDTYYR PGANLSLSCY AASNPPAQYS WLINGTFQQS TQELFIPNIT VNNSGSYTCH
ANNSVTGCNR TTVKTIIVTE LSPVVAKPQI KASKTTVTGD KDSVNLTCST NDTGISIRWF
FKNQSLPSSE RMKLSQGNTT LSINPVKRED AGTYWCEVFN PISKNQSDPI MLNVNYNALP
QENGLSPGAI AGIVIGVVAL VALIAVALAC FLHFGKTGRA SDQRDLTEHK PSVSNHTQDH
SNDPPNKMNE VTYSTLNFEA QQPTQPTSAS PSLTATEIIY SEVKKQ
//
MIM
109770
*RECORD*
*FIELD* NO
109770
*FIELD* TI
*109770 CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE 1; CEACAM1
;;BILIARY GLYCOPROTEIN; BGP;;
read moreBILIARY GLYCOPROTEIN 1; BGP1;;
CD66 ANTIGEN; CD66
CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE PSEUDOGENES,
INCLUDED;;
CEACAMPS, INCLUDED
*FIELD* TX
GENE FAMILY
The carcinoembryonic antigen (CEA) gene family belongs to the
immunoglobulin superfamily of genes. Members of the CEA family consist
of a single N domain, with structural homology to the immunoglobulin
variable domains, followed by a variable number of immunoglobulin
constant-like A and/or B domains. Based on sequence similarity and
functional characteristics, the CEA family has been subdivided into the
CEA subgroup and the pregnancy-specific glycoprotein (PSG) subgroup (for
review see Thompson et al. (1991)). Members of the CEA subgroup are
anchored in the cell membrane, whereas all of the PSGs appear to be
secreted. Genes in the CEA and PSG subgroups have a similar gene
structure and organization. The first exon, denoted L, encodes the
5-prime untranslated region and part of the signal peptide. Exon 2,
denoted L/N, encodes the rest of the signal peptide and the N domain.
Depending on the gene, exon 2 is followed by zero to 6 exons, each
encoding an A or B domain. For more information on the PSG subgroup, see
PSG1 (176390).
CLONING
Biliary glycoprotein I (CEACAM1), an antigen cross-reactive with
carcinoembryonic antigen (CEA; 114890), has a molecular mass of 85,000
Da and consists of a single polypeptide chain containing approximately
40% carbohydrate by weight. Hinoda et al. (1988) isolated and sequenced
4 overlapping cDNA clones from a normal adult human colon library. BGP1
is a member of the CEA subgroup.
- Review
Schlossman et al. (1994) provided a table of all known CD antigens, with
a list of the common names, the size in kilodaltons, and the nature of
the protein (adhesion, myeloid, platelet, B cell, T cell, etc.).
EVOLUTION
Thompson et al. (1987) suggested that the CEA gene family, which
includes CEA-related antigens such as nonspecific cross-reacting antigen
(NCA; 163980) and biliary glycoprotein, evolved from a common ancestor
shared with neural cell adhesion molecule (116930) and
alpha-1-B-glycoprotein (138670) and is perhaps a subfamily of the
immunoglobulin superfamily. A subfamily of about 10 genes appears to
exist (Thompson et al., 1987).
GENE FUNCTION
Biliary glycoprotein is the human homolog of a cell adhesion molecule
(CAM) of the rat designated Cell-CAM. BGP is expressed in cells of
epithelial and myeloid origin. In granulocytes, BGP is a main antigen of
the CD66 cluster of differentiation antigens that mediate the binding to
endothelial E-selectin. Neumaier et al. (1993) reported findings
suggesting that loss or reduced expression of the BGP adhesion molecule
is a major event in colorectal carcinogenesis.
Ergun et al. (2000) showed that CEACAM1 exhibits angiogenic properties
in in vitro and in vivo angiogenesis assays. CEACAM1 purified from
granulocytes and endothelial cell media as well as recombinant CEACAM1
expressed in HEK293 cells stimulated proliferation, chemotaxis, and
capillary-like tube formation of human microvascular endothelial cells.
They increased vascularization of chick chorioallantoic membrane and
potentiated the effects of VEGF165 (192240). VEGF165 increased CEACAM1
expression at both the mRNA and the protein level. VEGF165-induced
endothelial tube formation was blocked by a monoclonal CEACAM1 antibody.
These data suggested that CEACAM1 is a major effector of VEGF in the
early microvessel formation. Since CEACAM1 is expressed in tumor
microvessels but not in large blood vessels, CEACAM1 may be a target for
the inhibition of tumor angiogenesis.
Following infection with Neisseria gonorrhea, there is a transient
decline in circulating CD4 (186940)-positive T lymphocytes that resolves
after bacterial clearance. The gonococcus adheres to and is taken up by
host cells through opacity-associated (Opa) proteins. Some Opa variants
bind to heparan sulfate proteoglycans (HSPGs, e.g., SDC2; 142460), while
others are specific for members of the CEACAM1/CD66 receptor family.
CEACAM1 is the only member of this family that is expressed by
lymphocytes and that contains a cytoplasmic ITIM (immunoreceptor
tyrosine-based inhibitory motif). Using flow cytometry, Boulton and
Gray-Owen (2002) demonstrated that CEACAM1 expression is upregulated
after lymphocyte activation. Exposure to gonococci expressing the
HSPG-specific Opa50 protein increased and exposure to CEACAM1-specific
Opa52 gonococci or to anti-CEACAM1 antibody inhibited expression of the
CD69 (107273) activation marker on and proliferation by lymphocytes
stimulated in vitro. The reduction in lymphocyte proliferation was not
due to an increase in cell death. CEACAM1 associated with Opa52 also
interacted with SHP1 (176883) and SHP2 (176876), presumably through its
cytoplasmic ITIM. Boulton and Gray-Owen (2002) suggested that Opa52
engagement of the CEACAM1 coinhibitory receptor induces
immunosuppression and may explain the failure of the host to develop a
memory humoral response to N. gonorrhea infection due to a lack of
T-cell help for B-cell activation.
Zalzali et al. (2008) found that expression of epitope-tagged SOX9
(608160) in human colonic carcinoma cells upregulated the expression of
CEACAM1. Conversely, Sox9-deficient mice showed reduced Ceacam1
expression in colon. The promoter regions of mouse, rat, and human
CEACAM1 contain SOX9-binding motifs despite no other significant
sequence homology. Chromatin immunoprecipitation analysis confirmed that
SOX9 bound the human CEACAM1 promoter. In addition, the histone
acetyltransferase p300 (EP300; 602700) enhanced transactivation of
CEACAM1 by the rat and human CEACAM1 promoters. Zalzali et al. (2008)
concluded that SOX9 regulates CEACAM1 expression in colon epithelium.
Mouse neutrophils do not bind the human-restricted pathogen Neisseria
gonorrhoeae. Sarantis and Gray-Owen (2012) showed that introducing any
of the gonorrheal Opa-binding human neutrophil CEACAMs into a murine
neutrophil cell line allowed binding and entry of Neisseria. CEACAM1 and
CEACAM6 (163980) both bound and allowed entry of the bacterium, but they
mediated little neutrophil activation. In contrast, uptake via CEACAM3
(609142) induced an oxidative burst and intracellular granule release
comparable to that seen during human neutrophil infection. Coexpression
of CEACAM3 with either CEACAM1 or CEACAM6 potentiated CEACAM3-dependent
responses. Sarantis and Gray-Owen (2012) concluded that, although
CEACAMs have different functions in neutrophils, they cooperate during
gonorrheal infection. Their findings implicated CEACAM3 in the
neutrophil innate response to neisserial infection.
MAPPING
By analysis of somatic cell hybrids, Robbins et al. (1991) mapped the
Bgp1 gene of the mouse to chromosome 7. They considered it likely that
the gene is located in the region of conservation of synteny in
chromosome 7 of the mouse and chromosome 19 of man. Location of the BPG1
gene in the CEA cluster of genes on 19q13.2 was established by Thompson
et al. (1992), who determined the order and orientation of the genes in
the cluster by hybridization with probes from the 5-prime and 3-prime
regions of the genes to large groups of ordered cosmid clones.
Studies by several groups resulted in the mapping of the CEA gene family
to 19q13.1-q13.2 (Thompson et al., 1990; Thompson et al., 1992; Tynan et
al., 1992; Trask et al., 1993). The CEA subgroup is located centromeric
of the PSG subgroup, and together they span approximately 1.1 to 1.2 Mb
(Brandriff et al., 1992; Tynan et al., 1992). Nine CEA subgroup genes
were mapped within 2 cosmid contigs of 270 and 160 kb (Tynan et al.,
1992). The order of these 9 CEA subgroup genes is cen--CGM7
(CEACAM4)--CGM2 (CEACAM7)--CEA (CEACAM5)--NCA (CEACAM6; 163980)--CGM1
(CEACAM3; 609142)--gap--BGP (CEACAM1)--CGM9 (CEACAMP2)--CGM6
(CEACAM8)--CGM8 (CEACAMP1)--tel (Thompson et al., 1992; Brandriff et
al., 1992). The CEA, NCA, CGM1, and CGM8 genes are oriented in a 5-prime
to 3-prime direction from centromere to telomere, whereas the CGM7,
CGM2, BGP, CGM9, and CGM6 genes are oriented in a 3-prime to 5-prime
direction from centromere to telomere.
- PSEUDOGENES
Using a high-resolution restriction fragment fingerprinting technique,
Olsen et al. (1994) assembled 256 cosmids spanning the PSG region on
19q13.2 into a single 700-kb contig. FISH to sperm pronuclei and cosmid
walking experiments indicated that this PSG contig is telomeric of CGM8.
Olsen et al. (1994) and Teglund et al. (1994) analyzed the PSG contig
and identified 7 novel members of the CEA gene family, which they named
CGM12 to CGM18 according to the proposal by Barnett and Zimmermann
(1990). CGM12 is a putative pseudogene belonging to the CEA subgroup.
CGM13 to CGM18 form a new subgroup within the CEA gene family. By
detailed restriction mapping and hybridization with gene-specific
probes, Olsen et al. (1994) determined that the CGM13 to CGM18 genes are
interspersed among the PSG genes. They found that the order of the genes
is cen--CGM8 (CEACAMP1)--CGM12 (CEACAMP5)--PSG3--PSG8 (176397)--CGM13
(CEACAMP6)--PSG12 (PSG10; 176399)--PSG1 (176390)--PSG6 (176395)--PSG7
(176396)--CGM14 (CEACAMP7)--PSG13 (PSG11; 176401)--CGM15
(CEACAMP8)--PSG2 (176391)--CGM16 (CEACAMP9)--PSG5 (176394)--PSG4
(176393)--CGM17 (CEACAMP10)--PSG11 (PSG9; 176398)--CGM18
(CEACAMP11)--CGM11 (CEACAMP4)--tel. From centromere to telomere, the
CGM12 gene is oriented in a 5-prime to 3-prime direction, and the CGM13
to CGM18 genes are oriented in a 3-prime to 5-prime direction.
Teglund et al. (1994) characterized the CEA family subgroup containing
CGM13 to CGM18; these were later stated to be pseudogenes (Beauchemin et
al., 1999).
NOMENCLATURE
Beauchemin et al. (1999) provided a revised nomenclature for the CEA
gene family. Based on this nomenclature, the CEA family is composed of
the PSG subfamily; the CEACAM subfamily, which includes CEACAM1 (BGP),
CEACAM3 (CGM1), CEACAM4 (CGM7), CEACAM5 (CEA), CEACAM6 (NCA), CEACAM7
(CGM2), and CEACAM8 (CGM6); and the CEACAM pseudogene (CEACAMP)
subfamily, CEACAMP1 through CEACAMP11, which had originally been named
CGM8 through CGM18. Because of its high degree of conservation across
species, the BGP gene was renamed CEACAM1.
ANIMAL MODEL
Poy et al. (2002) hypothesized that insulin stimulates phosphorylation
of CEACAM1, which in turn leads to upregulation of receptor-mediated
insulin endocytosis and degradation in the hepatocyte. To test the
hypothesis, they generated transgenic mice overexpressing in liver a
dominant-negative phosphorylation-defective CEACAM1 mutant, S503A.
Supporting their hypothesis, they found that S503A-CEACAM1 (L-SACC1)
transgenic mice developed hyperinsulinemia resulting from impaired
insulin clearance. The hyperinsulinemia caused secondary insulin
resistance with impaired glucose tolerance and random, but not fasting,
hyperglycemia. Transgenic mice developed visceral adiposity with
increased amounts of plasma free fatty acids and plasma and hepatic
triglycerides. These findings suggested a mechanism through which
insulin signaling regulates insulin sensitivity by modulating hepatic
insulin clearance.
Using S503A-CEACAM1 transgenic mice, Abou-Rjaily et al. (2004)
demonstrated that the effect of CEACAM1 on EGF-dependent cell
proliferation is mediated by its ability to bind to and sequester Shc
(600560), thus uncoupling EGFR (131550) signaling from the ras/MAPK
pathway. Impaired CEACAM1 phosphorylation led to a ligand-independent
increase of EGFR-mediated cell proliferation; this increase appeared to
be secondary to visceral obesity and the metabolic syndrome, with
increased levels of output of free fatty acids and heparin-binding
EGF-like growth factor from the adipose tissue of the mice. Abou-Rjaily
et al. (2004) concluded that S503A-CEACAM1 mice provide a model for the
mechanistic link between increased cell proliferation in states of
impaired metabolism and visceral obesity.
*FIELD* RF
1. Abou-Rjaily, G. A.; Lee, S. J.; May, D.; Al-Share, Q. Y.; DeAngelis,
A. M.; Ruch, R. J.; Neumaier, M.; Kalthoff, H.; Lin, S.-H.; Najjar,
S. M.: CEACAM1 modulates epidermal growth factor receptor-mediated
cell proliferation. J. Clin. Invest. 114: 944-952, 2004.
2. Barnett, T.; Zimmermann, W.: Workshop report: proposed nomenclature
for the carcinoembryonic antigen (CEA) gene family. Tumour Biol. 11:
59-63, 1990.
3. Beauchemin, N.; Draber, P.; Dveksler, G.; Gold, P.; Gray-Owen,
S.; Grunert, F.; Hammarstrom, S.; Holmes, K. V.; Karlsson, A.; Kuroki,
M.; Lin, S.-H.; Lucka, L.; and 13 others: Redefined nomenclature
for members of the carcinoembryonic antigen family. Exp. Cell Res. 252:
243-249, 1999.
4. Boulton, I. C.; Gray-Owen, S. D.: Neisserial binding to CEACAM1
arrests the activation and proliferation of CD4+ T lymphocytes. Nature
Immun. 3: 229-236, 2002.
5. Brandriff, B. F.; Gordon, L. A.; Tynan, K. T.; Olsen, A. S.; Mohrenweiser,
H. W.; Fertitta, A.; Carrano, A. V.; Trask, B. J.: Order and genomic
distances among members of the carcinoembryonic antigen (CEA) gene
family determined by fluorescence in situ hybridization. Genomics 12:
773-779, 1992.
6. Ergun, S.; Kilic, N.; Ziegeler, G.; Hansen, A.; Nollau, P.; Gotze,
J.; Wurmbach, J.-H.; Horst, A.; Weil, J.; Fernando, M.; Wagener, C.
: CEA-related cell adhesion molecule 1: a potent angiogenic factor
and a major effector of vascular endothelial growth factor. Molec.
Cell 5: 311-320, 2000.
7. Hinoda, Y.; Neumaier, M.; Hefta, S. A.; Drzeniek, Z.; Wagener,
C.; Shively, L.; Hefta, L. J. F.; Shively, J. E.; Paxton, R. J.:
Molecular cloning of a cDNA coding biliary glycoprotein I: primary
structure of a glycoprotein immunologically crossreactive with carcinoembryonic
antigen. Proc. Nat. Acad. Sci. 85: 6959-6963, 1988. Note: Erratum:
Proc. Nat. Acad. Sci. 86: 1668 only, 1989.
8. Neumaier, M.; Paululat, S.; Chan, A.; Matthaes, P.; Wagener, C.
: Biliary glycoprotein, a potential human cell adhesion molecule,
is down-regulated in colorectal carcinomas. Proc. Nat. Acad. Sci. 90:
10744-10748, 1993.
9. Olsen, A.; Teglund, S.; Nelson, D.; Gordon, L.; Copeland, A.; Georgescu,
A.; Carrano, A.; Hammarstrom, S.: Gene organization of the pregnancy-specific
glycoprotein region on human chromosome 19: assembly and analysis
of a 700-kb cosmid contig spanning the region. Genomics 23: 659-668,
1994.
10. Poy, M. N.; Yang, Y.; Rezaei, K.; Fernstrom, M. A.; Lee, A. D.;
Kido, Y.; Erickson, S. K.; Najjar, S. M.: CEACAM1 regulates insulin
clearance in liver. Nature Genet. 30: 270-276, 2002.
11. Robbins, J.; Robbins, P. F.; Kozak, C. A.; Callahan, R.: The
mouse biliary glycoprotein gene (Bgp): partial nucleotide sequence,
expression, and chromosomal assignment. Genomics 10: 583-587, 1991.
12. Sarantis, H.; Gray-Owen, S. D.: Defining the roles of human carcinoembryonic
antigen-related cellular adhesion molecules during neutrophil responses
to Neisseria gonorrhoeae. Infect. Immun. 80: 345-358, 2012.
13. Schlossman, S. F.; Boumsell, L.; Gilks, W.; Harlan, J. M.; Kishimoto,
T.; Morimoto, C.; Ritz, J.; Shaw, S.; Silverstein, R. L.; Springer,
T. A.; Tedder, T. F.; Todd, R. F.: CD antigens 1993. Immun. Today 15:
98-99, 1994.
14. Teglund, S.; Olsen, A.; Khan, W. N.; Frangsmyr, L.; Hammarstrom,
S.: The pregnancy-specific glycoprotein (PSG) gene cluster on human
chromosome 19: fine structure of the 11 PSG genes and identification
of 6 new genes forming a third subgroup within the carcinoembryonic
antigen (CEA) family. Genomics 23: 669-684, 1994.
15. Thompson, J.; Koumari, R.; Wagner, K.; Barnert, S.; Schleussner,
C.; Schrewe, H.; Zimmermann, W.; Muller, G.; Schempp, W.; Zaninetta,
D.; Ammaturo, D.; Hardman, N.: The human pregnancy-specific glycoprotein
genes are tightly linked on the long arm of chromosome 19 and are
coordinately expressed. Biochem. Biophys. Res. Commun. 167: 848-859,
1990. Note: Erratum: Biochem. Biophys. Res. Commun. 168: 1325 only,
1990.
16. Thompson, J.; Zimmermann, W.; Osthus-Bugat, P.; Schleussner, C.;
Eades-Perner, A.-M.; Barnert, S.; Von Kleist, S.; Willcocks, T.; Craig,
I.; Tynan, K.; Olsen, A.; Mohrenweiser, H.: Long-range chromosomal
mapping of the carcinoembryonic antigen (CEA) gene family cluster. Genomics 12:
761-772, 1992.
17. Thompson, J. A.; Grunert, F.; Zimmermann, W.: Carcinoembryonic
antigen gene family: molecular biology and clinical perspectives. J.
Clin. Lab. Anal. 5: 344-366, 1991.
18. Thompson, J. A.; Pande, H.; Paxton, R. J.; Shively, L.; Padma,
A.; Simmer, R. L.; Todd, C. W.; Riggs, A. D.; Shively, J. E.: Molecular
cloning of a gene belonging to the carcinoembryonic antigen gene family
and discussion of a domain model. Proc. Nat. Acad. Sci. 84: 2965-2969,
1987.
19. Trask, B.; Fertitta, A.; Christensen, M.; Youngblom, J.; Bergmann,
A.; Copeland, A.; de Jong, P.; Mohrenweiser, H.; Olsen, A.; Carrano,
A.; Tynan, K.: Fluorescence in situ hybridization mapping of human
chromosome 19: cytogenetic band location of 540 cosmids and 70 genes
or DNA markers. Genomics 15: 133-145, 1993.
20. Tynan, K.; Olsen, A.; Trask, B.; de Jong, P.; Thompson, J.; Zimmermann,
W.; Carrano, A.; Mohrenweiser, H.: Assembly and analysis of cosmid
contigs in the CEA-gene family region of human chromosome 19. Nucleic
Acids Res. 20: 1629-1636, 1992.
21. Zalzali, H.; Naudin, C.; Bastide, P.; Quittau-Prevostel, C.; Yaghi,
C.; Poulat, F.; Jay, P.; Blache, P.: CEACAM1, a SOX9 direct transcriptional
target identified in the colon epithelium. Oncogene 27: 7131-7138,
2008.
*FIELD* CN
Paul J. Converse - updated: 5/1/2012
Patricia A. Hartz - updated: 9/21/2009
Marla J. F. O'Neill - updated: 12/2/2004
Paul J. Converse - updated: 4/18/2002
Victor A. McKusick - updated: 2/19/2002
Stylianos E. Antonarakis - updated: 3/30/2000
Patti M. Sherman - updated: 2/17/2000
*FIELD* CD
Victor A. McKusick: 10/10/1988
*FIELD* ED
carol: 01/10/2014
terry: 12/21/2012
terry: 8/31/2012
mgross: 5/3/2012
terry: 5/1/2012
terry: 4/21/2011
carol: 9/17/2010
carol: 10/29/2009
carol: 9/22/2009
terry: 9/21/2009
mgross: 1/5/2005
carol: 12/2/2004
mgross: 4/18/2002
alopez: 2/22/2002
terry: 2/19/2002
mgross: 2/16/2001
mgross: 3/30/2000
mgross: 2/21/2000
mgross: 2/18/2000
mgross: 2/17/2000
alopez: 12/4/1998
carol: 9/22/1994
jason: 6/28/1994
carol: 12/9/1993
carol: 6/9/1992
carol: 6/2/1992
supermim: 3/16/1992
*RECORD*
*FIELD* NO
109770
*FIELD* TI
*109770 CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE 1; CEACAM1
;;BILIARY GLYCOPROTEIN; BGP;;
read moreBILIARY GLYCOPROTEIN 1; BGP1;;
CD66 ANTIGEN; CD66
CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE PSEUDOGENES,
INCLUDED;;
CEACAMPS, INCLUDED
*FIELD* TX
GENE FAMILY
The carcinoembryonic antigen (CEA) gene family belongs to the
immunoglobulin superfamily of genes. Members of the CEA family consist
of a single N domain, with structural homology to the immunoglobulin
variable domains, followed by a variable number of immunoglobulin
constant-like A and/or B domains. Based on sequence similarity and
functional characteristics, the CEA family has been subdivided into the
CEA subgroup and the pregnancy-specific glycoprotein (PSG) subgroup (for
review see Thompson et al. (1991)). Members of the CEA subgroup are
anchored in the cell membrane, whereas all of the PSGs appear to be
secreted. Genes in the CEA and PSG subgroups have a similar gene
structure and organization. The first exon, denoted L, encodes the
5-prime untranslated region and part of the signal peptide. Exon 2,
denoted L/N, encodes the rest of the signal peptide and the N domain.
Depending on the gene, exon 2 is followed by zero to 6 exons, each
encoding an A or B domain. For more information on the PSG subgroup, see
PSG1 (176390).
CLONING
Biliary glycoprotein I (CEACAM1), an antigen cross-reactive with
carcinoembryonic antigen (CEA; 114890), has a molecular mass of 85,000
Da and consists of a single polypeptide chain containing approximately
40% carbohydrate by weight. Hinoda et al. (1988) isolated and sequenced
4 overlapping cDNA clones from a normal adult human colon library. BGP1
is a member of the CEA subgroup.
- Review
Schlossman et al. (1994) provided a table of all known CD antigens, with
a list of the common names, the size in kilodaltons, and the nature of
the protein (adhesion, myeloid, platelet, B cell, T cell, etc.).
EVOLUTION
Thompson et al. (1987) suggested that the CEA gene family, which
includes CEA-related antigens such as nonspecific cross-reacting antigen
(NCA; 163980) and biliary glycoprotein, evolved from a common ancestor
shared with neural cell adhesion molecule (116930) and
alpha-1-B-glycoprotein (138670) and is perhaps a subfamily of the
immunoglobulin superfamily. A subfamily of about 10 genes appears to
exist (Thompson et al., 1987).
GENE FUNCTION
Biliary glycoprotein is the human homolog of a cell adhesion molecule
(CAM) of the rat designated Cell-CAM. BGP is expressed in cells of
epithelial and myeloid origin. In granulocytes, BGP is a main antigen of
the CD66 cluster of differentiation antigens that mediate the binding to
endothelial E-selectin. Neumaier et al. (1993) reported findings
suggesting that loss or reduced expression of the BGP adhesion molecule
is a major event in colorectal carcinogenesis.
Ergun et al. (2000) showed that CEACAM1 exhibits angiogenic properties
in in vitro and in vivo angiogenesis assays. CEACAM1 purified from
granulocytes and endothelial cell media as well as recombinant CEACAM1
expressed in HEK293 cells stimulated proliferation, chemotaxis, and
capillary-like tube formation of human microvascular endothelial cells.
They increased vascularization of chick chorioallantoic membrane and
potentiated the effects of VEGF165 (192240). VEGF165 increased CEACAM1
expression at both the mRNA and the protein level. VEGF165-induced
endothelial tube formation was blocked by a monoclonal CEACAM1 antibody.
These data suggested that CEACAM1 is a major effector of VEGF in the
early microvessel formation. Since CEACAM1 is expressed in tumor
microvessels but not in large blood vessels, CEACAM1 may be a target for
the inhibition of tumor angiogenesis.
Following infection with Neisseria gonorrhea, there is a transient
decline in circulating CD4 (186940)-positive T lymphocytes that resolves
after bacterial clearance. The gonococcus adheres to and is taken up by
host cells through opacity-associated (Opa) proteins. Some Opa variants
bind to heparan sulfate proteoglycans (HSPGs, e.g., SDC2; 142460), while
others are specific for members of the CEACAM1/CD66 receptor family.
CEACAM1 is the only member of this family that is expressed by
lymphocytes and that contains a cytoplasmic ITIM (immunoreceptor
tyrosine-based inhibitory motif). Using flow cytometry, Boulton and
Gray-Owen (2002) demonstrated that CEACAM1 expression is upregulated
after lymphocyte activation. Exposure to gonococci expressing the
HSPG-specific Opa50 protein increased and exposure to CEACAM1-specific
Opa52 gonococci or to anti-CEACAM1 antibody inhibited expression of the
CD69 (107273) activation marker on and proliferation by lymphocytes
stimulated in vitro. The reduction in lymphocyte proliferation was not
due to an increase in cell death. CEACAM1 associated with Opa52 also
interacted with SHP1 (176883) and SHP2 (176876), presumably through its
cytoplasmic ITIM. Boulton and Gray-Owen (2002) suggested that Opa52
engagement of the CEACAM1 coinhibitory receptor induces
immunosuppression and may explain the failure of the host to develop a
memory humoral response to N. gonorrhea infection due to a lack of
T-cell help for B-cell activation.
Zalzali et al. (2008) found that expression of epitope-tagged SOX9
(608160) in human colonic carcinoma cells upregulated the expression of
CEACAM1. Conversely, Sox9-deficient mice showed reduced Ceacam1
expression in colon. The promoter regions of mouse, rat, and human
CEACAM1 contain SOX9-binding motifs despite no other significant
sequence homology. Chromatin immunoprecipitation analysis confirmed that
SOX9 bound the human CEACAM1 promoter. In addition, the histone
acetyltransferase p300 (EP300; 602700) enhanced transactivation of
CEACAM1 by the rat and human CEACAM1 promoters. Zalzali et al. (2008)
concluded that SOX9 regulates CEACAM1 expression in colon epithelium.
Mouse neutrophils do not bind the human-restricted pathogen Neisseria
gonorrhoeae. Sarantis and Gray-Owen (2012) showed that introducing any
of the gonorrheal Opa-binding human neutrophil CEACAMs into a murine
neutrophil cell line allowed binding and entry of Neisseria. CEACAM1 and
CEACAM6 (163980) both bound and allowed entry of the bacterium, but they
mediated little neutrophil activation. In contrast, uptake via CEACAM3
(609142) induced an oxidative burst and intracellular granule release
comparable to that seen during human neutrophil infection. Coexpression
of CEACAM3 with either CEACAM1 or CEACAM6 potentiated CEACAM3-dependent
responses. Sarantis and Gray-Owen (2012) concluded that, although
CEACAMs have different functions in neutrophils, they cooperate during
gonorrheal infection. Their findings implicated CEACAM3 in the
neutrophil innate response to neisserial infection.
MAPPING
By analysis of somatic cell hybrids, Robbins et al. (1991) mapped the
Bgp1 gene of the mouse to chromosome 7. They considered it likely that
the gene is located in the region of conservation of synteny in
chromosome 7 of the mouse and chromosome 19 of man. Location of the BPG1
gene in the CEA cluster of genes on 19q13.2 was established by Thompson
et al. (1992), who determined the order and orientation of the genes in
the cluster by hybridization with probes from the 5-prime and 3-prime
regions of the genes to large groups of ordered cosmid clones.
Studies by several groups resulted in the mapping of the CEA gene family
to 19q13.1-q13.2 (Thompson et al., 1990; Thompson et al., 1992; Tynan et
al., 1992; Trask et al., 1993). The CEA subgroup is located centromeric
of the PSG subgroup, and together they span approximately 1.1 to 1.2 Mb
(Brandriff et al., 1992; Tynan et al., 1992). Nine CEA subgroup genes
were mapped within 2 cosmid contigs of 270 and 160 kb (Tynan et al.,
1992). The order of these 9 CEA subgroup genes is cen--CGM7
(CEACAM4)--CGM2 (CEACAM7)--CEA (CEACAM5)--NCA (CEACAM6; 163980)--CGM1
(CEACAM3; 609142)--gap--BGP (CEACAM1)--CGM9 (CEACAMP2)--CGM6
(CEACAM8)--CGM8 (CEACAMP1)--tel (Thompson et al., 1992; Brandriff et
al., 1992). The CEA, NCA, CGM1, and CGM8 genes are oriented in a 5-prime
to 3-prime direction from centromere to telomere, whereas the CGM7,
CGM2, BGP, CGM9, and CGM6 genes are oriented in a 3-prime to 5-prime
direction from centromere to telomere.
- PSEUDOGENES
Using a high-resolution restriction fragment fingerprinting technique,
Olsen et al. (1994) assembled 256 cosmids spanning the PSG region on
19q13.2 into a single 700-kb contig. FISH to sperm pronuclei and cosmid
walking experiments indicated that this PSG contig is telomeric of CGM8.
Olsen et al. (1994) and Teglund et al. (1994) analyzed the PSG contig
and identified 7 novel members of the CEA gene family, which they named
CGM12 to CGM18 according to the proposal by Barnett and Zimmermann
(1990). CGM12 is a putative pseudogene belonging to the CEA subgroup.
CGM13 to CGM18 form a new subgroup within the CEA gene family. By
detailed restriction mapping and hybridization with gene-specific
probes, Olsen et al. (1994) determined that the CGM13 to CGM18 genes are
interspersed among the PSG genes. They found that the order of the genes
is cen--CGM8 (CEACAMP1)--CGM12 (CEACAMP5)--PSG3--PSG8 (176397)--CGM13
(CEACAMP6)--PSG12 (PSG10; 176399)--PSG1 (176390)--PSG6 (176395)--PSG7
(176396)--CGM14 (CEACAMP7)--PSG13 (PSG11; 176401)--CGM15
(CEACAMP8)--PSG2 (176391)--CGM16 (CEACAMP9)--PSG5 (176394)--PSG4
(176393)--CGM17 (CEACAMP10)--PSG11 (PSG9; 176398)--CGM18
(CEACAMP11)--CGM11 (CEACAMP4)--tel. From centromere to telomere, the
CGM12 gene is oriented in a 5-prime to 3-prime direction, and the CGM13
to CGM18 genes are oriented in a 3-prime to 5-prime direction.
Teglund et al. (1994) characterized the CEA family subgroup containing
CGM13 to CGM18; these were later stated to be pseudogenes (Beauchemin et
al., 1999).
NOMENCLATURE
Beauchemin et al. (1999) provided a revised nomenclature for the CEA
gene family. Based on this nomenclature, the CEA family is composed of
the PSG subfamily; the CEACAM subfamily, which includes CEACAM1 (BGP),
CEACAM3 (CGM1), CEACAM4 (CGM7), CEACAM5 (CEA), CEACAM6 (NCA), CEACAM7
(CGM2), and CEACAM8 (CGM6); and the CEACAM pseudogene (CEACAMP)
subfamily, CEACAMP1 through CEACAMP11, which had originally been named
CGM8 through CGM18. Because of its high degree of conservation across
species, the BGP gene was renamed CEACAM1.
ANIMAL MODEL
Poy et al. (2002) hypothesized that insulin stimulates phosphorylation
of CEACAM1, which in turn leads to upregulation of receptor-mediated
insulin endocytosis and degradation in the hepatocyte. To test the
hypothesis, they generated transgenic mice overexpressing in liver a
dominant-negative phosphorylation-defective CEACAM1 mutant, S503A.
Supporting their hypothesis, they found that S503A-CEACAM1 (L-SACC1)
transgenic mice developed hyperinsulinemia resulting from impaired
insulin clearance. The hyperinsulinemia caused secondary insulin
resistance with impaired glucose tolerance and random, but not fasting,
hyperglycemia. Transgenic mice developed visceral adiposity with
increased amounts of plasma free fatty acids and plasma and hepatic
triglycerides. These findings suggested a mechanism through which
insulin signaling regulates insulin sensitivity by modulating hepatic
insulin clearance.
Using S503A-CEACAM1 transgenic mice, Abou-Rjaily et al. (2004)
demonstrated that the effect of CEACAM1 on EGF-dependent cell
proliferation is mediated by its ability to bind to and sequester Shc
(600560), thus uncoupling EGFR (131550) signaling from the ras/MAPK
pathway. Impaired CEACAM1 phosphorylation led to a ligand-independent
increase of EGFR-mediated cell proliferation; this increase appeared to
be secondary to visceral obesity and the metabolic syndrome, with
increased levels of output of free fatty acids and heparin-binding
EGF-like growth factor from the adipose tissue of the mice. Abou-Rjaily
et al. (2004) concluded that S503A-CEACAM1 mice provide a model for the
mechanistic link between increased cell proliferation in states of
impaired metabolism and visceral obesity.
*FIELD* RF
1. Abou-Rjaily, G. A.; Lee, S. J.; May, D.; Al-Share, Q. Y.; DeAngelis,
A. M.; Ruch, R. J.; Neumaier, M.; Kalthoff, H.; Lin, S.-H.; Najjar,
S. M.: CEACAM1 modulates epidermal growth factor receptor-mediated
cell proliferation. J. Clin. Invest. 114: 944-952, 2004.
2. Barnett, T.; Zimmermann, W.: Workshop report: proposed nomenclature
for the carcinoembryonic antigen (CEA) gene family. Tumour Biol. 11:
59-63, 1990.
3. Beauchemin, N.; Draber, P.; Dveksler, G.; Gold, P.; Gray-Owen,
S.; Grunert, F.; Hammarstrom, S.; Holmes, K. V.; Karlsson, A.; Kuroki,
M.; Lin, S.-H.; Lucka, L.; and 13 others: Redefined nomenclature
for members of the carcinoembryonic antigen family. Exp. Cell Res. 252:
243-249, 1999.
4. Boulton, I. C.; Gray-Owen, S. D.: Neisserial binding to CEACAM1
arrests the activation and proliferation of CD4+ T lymphocytes. Nature
Immun. 3: 229-236, 2002.
5. Brandriff, B. F.; Gordon, L. A.; Tynan, K. T.; Olsen, A. S.; Mohrenweiser,
H. W.; Fertitta, A.; Carrano, A. V.; Trask, B. J.: Order and genomic
distances among members of the carcinoembryonic antigen (CEA) gene
family determined by fluorescence in situ hybridization. Genomics 12:
773-779, 1992.
6. Ergun, S.; Kilic, N.; Ziegeler, G.; Hansen, A.; Nollau, P.; Gotze,
J.; Wurmbach, J.-H.; Horst, A.; Weil, J.; Fernando, M.; Wagener, C.
: CEA-related cell adhesion molecule 1: a potent angiogenic factor
and a major effector of vascular endothelial growth factor. Molec.
Cell 5: 311-320, 2000.
7. Hinoda, Y.; Neumaier, M.; Hefta, S. A.; Drzeniek, Z.; Wagener,
C.; Shively, L.; Hefta, L. J. F.; Shively, J. E.; Paxton, R. J.:
Molecular cloning of a cDNA coding biliary glycoprotein I: primary
structure of a glycoprotein immunologically crossreactive with carcinoembryonic
antigen. Proc. Nat. Acad. Sci. 85: 6959-6963, 1988. Note: Erratum:
Proc. Nat. Acad. Sci. 86: 1668 only, 1989.
8. Neumaier, M.; Paululat, S.; Chan, A.; Matthaes, P.; Wagener, C.
: Biliary glycoprotein, a potential human cell adhesion molecule,
is down-regulated in colorectal carcinomas. Proc. Nat. Acad. Sci. 90:
10744-10748, 1993.
9. Olsen, A.; Teglund, S.; Nelson, D.; Gordon, L.; Copeland, A.; Georgescu,
A.; Carrano, A.; Hammarstrom, S.: Gene organization of the pregnancy-specific
glycoprotein region on human chromosome 19: assembly and analysis
of a 700-kb cosmid contig spanning the region. Genomics 23: 659-668,
1994.
10. Poy, M. N.; Yang, Y.; Rezaei, K.; Fernstrom, M. A.; Lee, A. D.;
Kido, Y.; Erickson, S. K.; Najjar, S. M.: CEACAM1 regulates insulin
clearance in liver. Nature Genet. 30: 270-276, 2002.
11. Robbins, J.; Robbins, P. F.; Kozak, C. A.; Callahan, R.: The
mouse biliary glycoprotein gene (Bgp): partial nucleotide sequence,
expression, and chromosomal assignment. Genomics 10: 583-587, 1991.
12. Sarantis, H.; Gray-Owen, S. D.: Defining the roles of human carcinoembryonic
antigen-related cellular adhesion molecules during neutrophil responses
to Neisseria gonorrhoeae. Infect. Immun. 80: 345-358, 2012.
13. Schlossman, S. F.; Boumsell, L.; Gilks, W.; Harlan, J. M.; Kishimoto,
T.; Morimoto, C.; Ritz, J.; Shaw, S.; Silverstein, R. L.; Springer,
T. A.; Tedder, T. F.; Todd, R. F.: CD antigens 1993. Immun. Today 15:
98-99, 1994.
14. Teglund, S.; Olsen, A.; Khan, W. N.; Frangsmyr, L.; Hammarstrom,
S.: The pregnancy-specific glycoprotein (PSG) gene cluster on human
chromosome 19: fine structure of the 11 PSG genes and identification
of 6 new genes forming a third subgroup within the carcinoembryonic
antigen (CEA) family. Genomics 23: 669-684, 1994.
15. Thompson, J.; Koumari, R.; Wagner, K.; Barnert, S.; Schleussner,
C.; Schrewe, H.; Zimmermann, W.; Muller, G.; Schempp, W.; Zaninetta,
D.; Ammaturo, D.; Hardman, N.: The human pregnancy-specific glycoprotein
genes are tightly linked on the long arm of chromosome 19 and are
coordinately expressed. Biochem. Biophys. Res. Commun. 167: 848-859,
1990. Note: Erratum: Biochem. Biophys. Res. Commun. 168: 1325 only,
1990.
16. Thompson, J.; Zimmermann, W.; Osthus-Bugat, P.; Schleussner, C.;
Eades-Perner, A.-M.; Barnert, S.; Von Kleist, S.; Willcocks, T.; Craig,
I.; Tynan, K.; Olsen, A.; Mohrenweiser, H.: Long-range chromosomal
mapping of the carcinoembryonic antigen (CEA) gene family cluster. Genomics 12:
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17. Thompson, J. A.; Grunert, F.; Zimmermann, W.: Carcinoembryonic
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18. Thompson, J. A.; Pande, H.; Paxton, R. J.; Shively, L.; Padma,
A.; Simmer, R. L.; Todd, C. W.; Riggs, A. D.; Shively, J. E.: Molecular
cloning of a gene belonging to the carcinoembryonic antigen gene family
and discussion of a domain model. Proc. Nat. Acad. Sci. 84: 2965-2969,
1987.
19. Trask, B.; Fertitta, A.; Christensen, M.; Youngblom, J.; Bergmann,
A.; Copeland, A.; de Jong, P.; Mohrenweiser, H.; Olsen, A.; Carrano,
A.; Tynan, K.: Fluorescence in situ hybridization mapping of human
chromosome 19: cytogenetic band location of 540 cosmids and 70 genes
or DNA markers. Genomics 15: 133-145, 1993.
20. Tynan, K.; Olsen, A.; Trask, B.; de Jong, P.; Thompson, J.; Zimmermann,
W.; Carrano, A.; Mohrenweiser, H.: Assembly and analysis of cosmid
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21. Zalzali, H.; Naudin, C.; Bastide, P.; Quittau-Prevostel, C.; Yaghi,
C.; Poulat, F.; Jay, P.; Blache, P.: CEACAM1, a SOX9 direct transcriptional
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*FIELD* CN
Paul J. Converse - updated: 5/1/2012
Patricia A. Hartz - updated: 9/21/2009
Marla J. F. O'Neill - updated: 12/2/2004
Paul J. Converse - updated: 4/18/2002
Victor A. McKusick - updated: 2/19/2002
Stylianos E. Antonarakis - updated: 3/30/2000
Patti M. Sherman - updated: 2/17/2000
*FIELD* CD
Victor A. McKusick: 10/10/1988
*FIELD* ED
carol: 01/10/2014
terry: 12/21/2012
terry: 8/31/2012
mgross: 5/3/2012
terry: 5/1/2012
terry: 4/21/2011
carol: 9/17/2010
carol: 10/29/2009
carol: 9/22/2009
terry: 9/21/2009
mgross: 1/5/2005
carol: 12/2/2004
mgross: 4/18/2002
alopez: 2/22/2002
terry: 2/19/2002
mgross: 2/16/2001
mgross: 3/30/2000
mgross: 2/21/2000
mgross: 2/18/2000
mgross: 2/17/2000
alopez: 12/4/1998
carol: 9/22/1994
jason: 6/28/1994
carol: 12/9/1993
carol: 6/9/1992
carol: 6/2/1992
supermim: 3/16/1992