Full text data of CEACAM8
CEACAM8
(CGM6)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Carcinoembryonic antigen-related cell adhesion molecule 8 (CD67 antigen; Carcinoembryonic antigen CGM6; Non-specific cross-reacting antigen NCA-95; CD66b; Flags: Precursor)
Carcinoembryonic antigen-related cell adhesion molecule 8 (CD67 antigen; Carcinoembryonic antigen CGM6; Non-specific cross-reacting antigen NCA-95; CD66b; Flags: Precursor)
UniProt
P31997
ID CEAM8_HUMAN Reviewed; 349 AA.
AC P31997; O60399; Q16574;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JUL-1999, sequence version 2.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 8;
DE AltName: Full=CD67 antigen;
DE AltName: Full=Carcinoembryonic antigen CGM6;
DE AltName: Full=Non-specific cross-reacting antigen NCA-95;
DE AltName: CD_antigen=CD66b;
DE Flags: Precursor;
GN Name=CEACAM8; Synonyms=CGM6;
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].
RC TISSUE=Spleen;
RX PubMed=2208113;
RA Berling B., Kolbinger F., Grunert F., Thompson J.A., Brombacher F.,
RA Buchegger F., Vkleist S., Zimmermann W.;
RT "Cloning of a carcinoembryonic antigen gene family member expressed in
RT leukocytes of chronic myeloid leukemia patients and bone marrow.";
RL Cancer Res. 50:6534-6539(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-322.
RX PubMed=2306228; DOI=10.1016/0006-291X(90)90975-S;
RA Arakawa F., Kuroki M., Misumi Y., Oikawa S., Nakazato H., Matsuoka Y.;
RT "Characterization of a cDNA clone encoding a new species of the
RT nonspecific cross-reacting antigen (NCA), a member of the CEA gene
RT family.";
RL Biochem. Biophys. Res. Commun. 166:1063-1071(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1427854; DOI=10.1016/S0888-7543(05)80230-7;
RA Khan W.N., Fraengsmyr L., Teglund S., Israelsson A., Bremer K.,
RA Hammarstroem S.;
RT "Identification of three new genes and estimation of the size of the
RT carcinoembryonic antigen family.";
RL Genomics 14:384-390(1992).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=9427723;
RA Eades-Perner A., Thompson J., van der Putten H., Zimmermann W.;
RT "Mice transgenic for the human CGM6 gene express its product, the
RT granulocyte marker CD66b, exclusively in granulocytes.";
RL Blood 91:663-672(1998).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-288, AND MASS
RP SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [8]
RP STRUCTURE BY NMR OF 33-154.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first Ig-like domain of human
RT carcinoembryonic antigen related cell adhesion molecule 8.";
RL Submitted (MAY-2007) to the PDB data bank.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Expressed in leukocytes of chronic myeloid
CC Leukemia patients and bone marrow.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X52378; CAA36604.1; -; mRNA.
DR EMBL; M33326; AAA59914.1; -; mRNA.
DR EMBL; D90064; BAA14108.1; -; mRNA.
DR EMBL; AC004558; AAC13659.1; -; Genomic_DNA.
DR EMBL; BC026263; AAH26263.1; -; mRNA.
DR EMBL; Z95119; CAB08298.1; -; Genomic_DNA.
DR PIR; S13524; A34815.
DR RefSeq; NP_001807.2; NM_001816.3.
DR UniGene; Hs.41; -.
DR PDB; 2DKS; NMR; -; A=33-149.
DR PDBsum; 2DKS; -.
DR ProteinModelPortal; P31997; -.
DR SMR; P31997; 33-316.
DR IntAct; P31997; 3.
DR STRING; 9606.ENSP00000244336; -.
DR PhosphoSite; P31997; -.
DR DMDM; 6166048; -.
DR PaxDb; P31997; -.
DR PeptideAtlas; P31997; -.
DR PRIDE; P31997; -.
DR DNASU; 1088; -.
DR Ensembl; ENST00000244336; ENSP00000244336; ENSG00000124469.
DR GeneID; 1088; -.
DR KEGG; hsa:1088; -.
DR UCSC; uc002oud.2; human.
DR CTD; 1088; -.
DR GeneCards; GC19M043084; -.
DR HGNC; HGNC:1820; CEACAM8.
DR HPA; CAB033676; -.
DR MIM; 114890; gene.
DR neXtProt; NX_P31997; -.
DR PharmGKB; PA26364; -.
DR eggNOG; NOG149650; -.
DR HOGENOM; HOG000233417; -.
DR HOVERGEN; HBG007922; -.
DR InParanoid; P31997; -.
DR KO; K06499; -.
DR OMA; VRMITVS; -.
DR OrthoDB; EOG74BJS7; -.
DR PhylomeDB; P31997; -.
DR EvolutionaryTrace; P31997; -.
DR GeneWiki; CEACAM8; -.
DR GenomeRNAi; 1088; -.
DR NextBio; 4526; -.
DR PRO; PR:P31997; -.
DR ArrayExpress; P31997; -.
DR Bgee; P31997; -.
DR CleanEx; HS_CEACAM8; -.
DR Genevestigator; P31997; -.
DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein;
KW Membrane; Polymorphism; Reference proteome; Repeat; Signal.
FT SIGNAL 1 34
FT CHAIN 35 320 Carcinoembryonic antigen-related cell
FT adhesion molecule 8.
FT /FTId=PRO_0000014572.
FT PROPEP 321 349 Removed in mature form.
FT /FTId=PRO_0000014573.
FT DOMAIN 35 142 Ig-like V-type.
FT DOMAIN 145 232 Ig-like C2-type 1.
FT DOMAIN 237 319 Ig-like C2-type 2.
FT LIPID 320 320 GPI-anchor amidated aspartate.
FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 111 111 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 115 115 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 152 152 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 173 173 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 197 197 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 224 224 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 256 256 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 274 274 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 288 288 N-linked (GlcNAc...).
FT CARBOHYD 309 309 N-linked (GlcNAc...) (Potential).
FT DISULFID 167 215 Probable.
FT DISULFID 259 299 Probable.
FT VARIANT 17 17 G -> V (in dbSNP:rs28367882).
FT /FTId=VAR_049849.
FT VARIANT 45 45 A -> V (in dbSNP:rs35221575).
FT /FTId=VAR_049850.
FT VARIANT 114 114 R -> K (in dbSNP:rs1041997).
FT /FTId=VAR_011721.
FT VARIANT 322 322 L -> V (in dbSNP:rs45476198).
FT /FTId=VAR_049851.
FT VARIANT 340 340 I -> M (in dbSNP:rs8103051).
FT /FTId=VAR_049852.
FT STRAND 37 46
FT STRAND 51 57
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 TURN 114 116
FT STRAND 120 126
FT TURN 127 129
FT STRAND 139 141
SQ SEQUENCE 349 AA; 38154 MW; AACF74DA1AC839D8 CRC64;
MGPISAPSCR WRIPWQGLLL TASLFTFWNP PTTAQLTIEA VPSNAAEGKE VLLLVHNLPQ
DPRGYNWYKG ETVDANRRII GYVISNQQIT PGPAYSNRET IYPNASLLMR NVTRNDTGSY
TLQVIKLNLM SEEVTGQFSV HPETPKPSIS SNNSNPVEDK DAVAFTCEPE TQNTTYLWWV
NGQSLPVSPR LQLSNGNRTL TLLSVTRNDV GPYECEIQNP ASANFSDPVT LNVLYGPDAP
TISPSDTYYH AGVNLNLSCH AASNPPSQYS WSVNGTFQQY TQKLFIPNIT TKNSGSYACH
TTNSATGRNR TTVRMITVSD ALVQGSSPGL SARATVSIMI GVLARVALI
//
ID CEAM8_HUMAN Reviewed; 349 AA.
AC P31997; O60399; Q16574;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JUL-1999, sequence version 2.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 8;
DE AltName: Full=CD67 antigen;
DE AltName: Full=Carcinoembryonic antigen CGM6;
DE AltName: Full=Non-specific cross-reacting antigen NCA-95;
DE AltName: CD_antigen=CD66b;
DE Flags: Precursor;
GN Name=CEACAM8; Synonyms=CGM6;
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].
RC TISSUE=Spleen;
RX PubMed=2208113;
RA Berling B., Kolbinger F., Grunert F., Thompson J.A., Brombacher F.,
RA Buchegger F., Vkleist S., Zimmermann W.;
RT "Cloning of a carcinoembryonic antigen gene family member expressed in
RT leukocytes of chronic myeloid leukemia patients and bone marrow.";
RL Cancer Res. 50:6534-6539(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-322.
RX PubMed=2306228; DOI=10.1016/0006-291X(90)90975-S;
RA Arakawa F., Kuroki M., Misumi Y., Oikawa S., Nakazato H., Matsuoka Y.;
RT "Characterization of a cDNA clone encoding a new species of the
RT nonspecific cross-reacting antigen (NCA), a member of the CEA gene
RT family.";
RL Biochem. Biophys. Res. Commun. 166:1063-1071(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1427854; DOI=10.1016/S0888-7543(05)80230-7;
RA Khan W.N., Fraengsmyr L., Teglund S., Israelsson A., Bremer K.,
RA Hammarstroem S.;
RT "Identification of three new genes and estimation of the size of the
RT carcinoembryonic antigen family.";
RL Genomics 14:384-390(1992).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=9427723;
RA Eades-Perner A., Thompson J., van der Putten H., Zimmermann W.;
RT "Mice transgenic for the human CGM6 gene express its product, the
RT granulocyte marker CD66b, exclusively in granulocytes.";
RL Blood 91:663-672(1998).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-288, AND MASS
RP SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [8]
RP STRUCTURE BY NMR OF 33-154.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first Ig-like domain of human
RT carcinoembryonic antigen related cell adhesion molecule 8.";
RL Submitted (MAY-2007) to the PDB data bank.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Expressed in leukocytes of chronic myeloid
CC Leukemia patients and bone marrow.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X52378; CAA36604.1; -; mRNA.
DR EMBL; M33326; AAA59914.1; -; mRNA.
DR EMBL; D90064; BAA14108.1; -; mRNA.
DR EMBL; AC004558; AAC13659.1; -; Genomic_DNA.
DR EMBL; BC026263; AAH26263.1; -; mRNA.
DR EMBL; Z95119; CAB08298.1; -; Genomic_DNA.
DR PIR; S13524; A34815.
DR RefSeq; NP_001807.2; NM_001816.3.
DR UniGene; Hs.41; -.
DR PDB; 2DKS; NMR; -; A=33-149.
DR PDBsum; 2DKS; -.
DR ProteinModelPortal; P31997; -.
DR SMR; P31997; 33-316.
DR IntAct; P31997; 3.
DR STRING; 9606.ENSP00000244336; -.
DR PhosphoSite; P31997; -.
DR DMDM; 6166048; -.
DR PaxDb; P31997; -.
DR PeptideAtlas; P31997; -.
DR PRIDE; P31997; -.
DR DNASU; 1088; -.
DR Ensembl; ENST00000244336; ENSP00000244336; ENSG00000124469.
DR GeneID; 1088; -.
DR KEGG; hsa:1088; -.
DR UCSC; uc002oud.2; human.
DR CTD; 1088; -.
DR GeneCards; GC19M043084; -.
DR HGNC; HGNC:1820; CEACAM8.
DR HPA; CAB033676; -.
DR MIM; 114890; gene.
DR neXtProt; NX_P31997; -.
DR PharmGKB; PA26364; -.
DR eggNOG; NOG149650; -.
DR HOGENOM; HOG000233417; -.
DR HOVERGEN; HBG007922; -.
DR InParanoid; P31997; -.
DR KO; K06499; -.
DR OMA; VRMITVS; -.
DR OrthoDB; EOG74BJS7; -.
DR PhylomeDB; P31997; -.
DR EvolutionaryTrace; P31997; -.
DR GeneWiki; CEACAM8; -.
DR GenomeRNAi; 1088; -.
DR NextBio; 4526; -.
DR PRO; PR:P31997; -.
DR ArrayExpress; P31997; -.
DR Bgee; P31997; -.
DR CleanEx; HS_CEACAM8; -.
DR Genevestigator; P31997; -.
DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein;
KW Membrane; Polymorphism; Reference proteome; Repeat; Signal.
FT SIGNAL 1 34
FT CHAIN 35 320 Carcinoembryonic antigen-related cell
FT adhesion molecule 8.
FT /FTId=PRO_0000014572.
FT PROPEP 321 349 Removed in mature form.
FT /FTId=PRO_0000014573.
FT DOMAIN 35 142 Ig-like V-type.
FT DOMAIN 145 232 Ig-like C2-type 1.
FT DOMAIN 237 319 Ig-like C2-type 2.
FT LIPID 320 320 GPI-anchor amidated aspartate.
FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 111 111 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 115 115 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 152 152 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 173 173 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 197 197 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 224 224 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 256 256 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 274 274 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 288 288 N-linked (GlcNAc...).
FT CARBOHYD 309 309 N-linked (GlcNAc...) (Potential).
FT DISULFID 167 215 Probable.
FT DISULFID 259 299 Probable.
FT VARIANT 17 17 G -> V (in dbSNP:rs28367882).
FT /FTId=VAR_049849.
FT VARIANT 45 45 A -> V (in dbSNP:rs35221575).
FT /FTId=VAR_049850.
FT VARIANT 114 114 R -> K (in dbSNP:rs1041997).
FT /FTId=VAR_011721.
FT VARIANT 322 322 L -> V (in dbSNP:rs45476198).
FT /FTId=VAR_049851.
FT VARIANT 340 340 I -> M (in dbSNP:rs8103051).
FT /FTId=VAR_049852.
FT STRAND 37 46
FT STRAND 51 57
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 TURN 114 116
FT STRAND 120 126
FT TURN 127 129
FT STRAND 139 141
SQ SEQUENCE 349 AA; 38154 MW; AACF74DA1AC839D8 CRC64;
MGPISAPSCR WRIPWQGLLL TASLFTFWNP PTTAQLTIEA VPSNAAEGKE VLLLVHNLPQ
DPRGYNWYKG ETVDANRRII GYVISNQQIT PGPAYSNRET IYPNASLLMR NVTRNDTGSY
TLQVIKLNLM SEEVTGQFSV HPETPKPSIS SNNSNPVEDK DAVAFTCEPE TQNTTYLWWV
NGQSLPVSPR LQLSNGNRTL TLLSVTRNDV GPYECEIQNP ASANFSDPVT LNVLYGPDAP
TISPSDTYYH AGVNLNLSCH AASNPPSQYS WSVNGTFQQY TQKLFIPNIT TKNSGSYACH
TTNSATGRNR TTVRMITVSD ALVQGSSPGL SARATVSIMI GVLARVALI
//
MIM
114890
*RECORD*
*FIELD* NO
114890
*FIELD* TI
*114890 CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE 5; CEACAM5
;;CARCINOEMBRYONIC ANTIGEN; CEA
read more*FIELD* TX
DESCRIPTION
Members of the CEACAM subfamily, including CEACAM5, belong to the CEA
gene family. For general information on the CEA gene family, see CEACAM1
(109770).
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 (see 176390); the CEACAM subfamily, which includes
CEACAM1 (BGP), CEACAM3 (CGM1; 609142), 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 (see 109770). The CEA gene was
renamed CEACAM5.
CLONING
Carcinoembryonic antigen was first described by Gold and Freedman (1965)
as a complex immunoreactive glycoprotein. Oikawa et al. (1987) cloned
cDNAs corresponding to the mRNA encoding a polypeptide that is
immunoreactive with the antisera specific to CEA. The amino acid
sequence deduced from the nucleotide sequence of the cDNA showed that
CEA is synthesized as a precursor with a signal peptide followed by 668
amino acids of the putative mature CEA peptide.
Zimmermann et al. (1987) isolated and characterized cDNA clones for
human CEA. They found no CEA mRNA in HeLa cells or in normal human
fibroblasts.
Kamarck et al. (1987) prepared a cDNA for CEA from an adenocarcinoma
cell line. They confirmed its identity by specific hybridization to DNA
transfected into L cells, which then expressed CEA. Hybridization of the
cDNA insert to genomic DNA from colon carcinoma cells showed no
rearrangement in the tumors.
MAPPING
By analysis of somatic cell hybrids, Kamarck et al. (1987) mapped the
CEA gene to chromosome 19.
By genomic clones used in somatic cell hybrids and by in situ
hybridization, Willcocks et al. (1987, 1989) assigned the CEA locus to
19q13.1-q13.3. Zimmermann et al. (1988) used a DNA fragment from the NCA
gene to localize the gene(s) by in situ hybridization to chromosome 19.
Two specific hybridization sites were found, 1 on the long arm,
19q31-q32, and a minor accumulation on the short arm, 19p13.2-p13.3.
Zimmermann et al. (1988) also used a fragment from the repeat region of
the CEA cDNA clone to map the gene to 19q31-q32 by in situ
hybridization. No accumulation of grains was observed over the short
arm. Nishi et al. (1991) assigned the CEA gene to 19q13.2 by in situ
hybridization. Thompson and Zimmermann (1988) stated that the CEA gene
family, consisting of approximately 10 genes, is localized in 2 clusters
on chromosome 19. By the time of their report, mRNA species for 5 of the
genes had been identified and found to show tissue variability in their
transcriptional activity. Willcocks and Craig (1990) found that the CEA
gene comprises 9 exons encoding amino acids and 1 encoding a 3-prime
untranslated fragment. Thompson et al. (1992) stated that various
methods, including hybridization analysis of large DNA fragments
separated by pulsed field gel electrophoresis, yielded similar results,
indicating that the entire CEA gene family is contained in a region
located at 19q13.1-q13.2 between the CYP2A (122720) and D19S15/D19S8
markers. They found that the CEA subgroup has 9 members, including CEA,
nonspecific crossreacting antigen, biliary glycoprotein (BGP), and 6
genes referred to as CEA gene family members: CGM1, CGM2, CGM6, CGM7,
CGM8, and CGM9. From large groups of ordered cosmid clones, Thompson et
al. (1992) confirmed the identity of all known CEA subgroup genes,
either by hybridization using gene-specific probes or by DNA sequencing.
These studies identified a new member of the CEA subgroup, CGM8, which
they concluded probably represents a pseudogene due to the existence of
2 stop codons, one in the leader exon and one in the N-terminal domain
exon. The gene order and orientation, which were determined with
hybridization with probes from the 5-prime and 3-prime regions of the
genes, were determined to be as follows: cen/3-prime CGM7/3-prime
CGM2/5-prime CEA/5-prime NCA/5-prime CGM1/3-prime BGP/3-prime
CGM9/3-prime CGM6/5-prime CGM8///PSG cluster/qter. By fluorescence in
situ hybridization, Brandriff et al. (1992) concluded that the gene
order is cen--CGM7--CEA--NCA--CGM1--BGP--CGM9--CGM8--PSG--tel. The order
agreed completely with that obtained by Thompson et al. (1992).
GENE FUNCTION
CEA injected into experimental animals accumulates in the liver and is
largely confined to macrophages (Kupffer cells) (Toth et al., 1982). The
binding domain of the protein was narrowed to the hinge region between
its N domain and its first (A1) immunoglobulin loop domain. Furthermore,
the binding domain was narrowed to amino acids 108-112 (PELPK) (Thomas
et al., 1992; Gangopadhyay and Thomas, 1996).
Zimmer and Thomas (2001) noted that CEA expression is used clinically to
monitor patients with colorectal and other cancers and that a subset of
these patients have extraordinarily high CEA levels that cannot be
attributed solely to tumor load. In addition, elevated levels of serum
CEA are found in patients with benign liver disease including cirrhosis,
biliary obstruction, and hepatitis. In tumor cells of 3 of 8 colorectal
cancer patients with high CEA levels, Zimmer and Thomas (2001)
identified heterozygous mutations in the region of CEA (PELPK motif)
responsible for its hepatic clearance. CEA with mutations in the PELPK
motif showed remarkably reduced circulatory clearance rates in an animal
model. A patient without mutation in the region showed normal clearance
rates. Zimmer and Thomas (2001) concluded that mutations in PELPK may
affect structural stability and binding affinity to the Kupffer receptor
in the liver. They suggested that CEA may have a role as a facilitator
of hepatic metastasis.
By generating a chimeric protein of CEACAM5 and NCAM1 (116930),
Nicholson and Stanners (2007) identified a novel specificity signal of 6
amino acids (PGLSAG) within the glycophosphatidylinositol (GPI) anchor
attachment signal of CEACAM5 that was necessary and sufficient to
specify the addition of a particular functional GPI.
Muenzner et al. (2010) found that CEA-binding bacteria colonized the
urogenital tract of CEA transgenic mice, but not of wildtype mice, by
suppressing exfoliation of mucosal cells. CEA binding triggered de novo
expression of the transforming growth factor receptor CD105 (131195),
changing focal adhesion composition and activating beta-1 integrins
(135630). Muenzner et al. (2010) concluded that this manipulation of
integrin inside-out signaling promotes efficient mucosal colonization
and represents a potential target to prevent or cure bacterial
infections.
*FIELD* SA
Thompson et al. (1987)
*FIELD* RF
1. 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.
2. 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.
3. Gangopadhyay, A.; Thomas, P.: Processing of carcinoembryonic antigen
by Kupffer cells: recognition of a penta-peptide sequence. Arch.
Biochem. Biophys. 334: 151-157, 1996.
4. Gold, P.; Freedman, S. O.: Demonstration of tumor-specific antigens
in human colonic carcinomata by immunological tolerance and absorption
techniques. J. Exp. Med. 121: 439-462, 1965.
5. Kamarck, M. E.; Elting, J. J.; Hart, J. T.; Goebel, S. J.; Rae,
P. M. M.; Nothdurft, M. A.; Nedwin, J. J.; Barnett, T. R.: Carcinoembryonic
antigen family: expression in a mouse L-cell transfectant and characterization
of a partial cDNA in bacteriophage lambda-gt11. Proc. Nat. Acad.
Sci. 84: 5350-5354, 1987.
6. Muenzner, P.; Bachmann, V.; Zimmermann, W.; Hentschel, J.; Hauck,
C. R.: Human-restricted bacterial pathogens block shedding of epithelial
cells by stimulating integrin activation. Science 329: 1197-1201,
2010.
7. Nicholson, T. B.; Stanners, C. P.: Identification of a novel functional
specificity signal within the GPI anchor signal sequence of carcinoembryonic
antigen. J. Cell Biol. 177: 211-218, 2007.
8. Nishi, M.; Inazawa, J.; Inoue, K.; Nakagawa, H.; Taniwaki, M.;
Misawa, S.; Oikawa, S.; Nakazato, H.; Abe, T.: Regional chromosomal
assignment of carcinoembryonic antigen gene (CEA) to chromosome 19
at band q13.2. Cancer Genet. Cytogenet. 54: 77-81, 1991.
9. Oikawa, S.; Nakazato, H.; Kosaki, G.: Primary structure of human
carcinoembryonic antigen (CEA) deduced from cDNA sequence. Biochem.
Biophys. Res. Commun. 142: 511-528, 1987.
10. Thomas, P.; Petrick, A. T.; Toth, C. A.; Fox, E. S.; Elting, J.
J.; Steele, G., Jr.: A peptide sequence on carcinoembryonic antigen
binds to a 80 kD protein on Kupffer cells. Biochem. Biophys. Res.
Commun. 188: 671-677, 1992.
11. Thompson, J.; Zimmermann, W.: The carcinoembryonic antigen gene
family: structure, expression and evolution. Tumour Biol. 9: 63-83,
1988.
12. 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.
13. 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.
14. Toth, C. A.; Thomas, P.; Broitman, S. A.; Zamcheck, N.: A new
Kupffer cell receptor mediating plasma clearance of carcinoembryonic
antigen by the rat. Biochem. J. 204: 377-381, 1982.
15. Willcocks, T. C.; Craig, I. W.: Characterization of the genomic
organization of human carcinoembryonic antigen (CEA): comparison with
other family members and sequence analysis of 5-prime controlling
region. Genomics 8: 492-500, 1990.
16. Willcocks, T. C.; Craig, S. P.; Coates, D.; Craig, I. W.: Coding
sequences for carcinoembryonic antigen (CEA) assigned to human chromosome
19q13. (Abstract) Cytogenet. Cell Genet. 46: 716 only, 1987.
17. Willcocks, T. C.; Craig, S. P.; Craig, I. W.: Assignment of the
coding sequence for carcinoembryonic antigen (CEA) and normal cross-reacting
antigen (NCA) to human chromosome 19q13. Ann. Hum. Genet. 53: 141-148,
1989.
18. Zimmer, R.; Thomas, P.: Mutations in the carcinoembryonic antigen
gene in colorectal cancer patients: implications on liver metastasis. Cancer
Res. 61: 2822-2826, 2001.
19. Zimmermann, W.; Ortlieb, B.; Friedrich, R.; von Kleist, S.: Isolation
and characterization of cDNA clones encoding the human carcinoembryonic
antigen reveal a highly conserved repeating structure. Proc. Nat.
Acad. Sci. 84: 2960-2964, 1987.
20. Zimmermann, W.; Weber, B.; Ortlieb, B.; Rudert, F.; Schempp, W.;
Fiebig, H.-H.; Shively, J. E.; von Kleist, S.; Thompson, J. A.: Chromosomal
localization of the carcinoembryonic antigen gene family and differential
expression in various tumors. Cancer Res. 48: 2550-2554, 1988.
*FIELD* CN
Ada Hamosh - updated: 10/27/2010
Paul J. Converse - updated: 11/9/2009
Victor A. McKusick - updated: 8/12/2002
Victor A. McKusick - updated: 1/21/2000
*FIELD* CD
Victor A. McKusick: 4/14/1987
*FIELD* ED
alopez: 10/27/2010
carol: 9/17/2010
terry: 12/1/2009
mgross: 11/11/2009
terry: 11/9/2009
carol: 10/29/2009
mgross: 1/5/2005
mgross: 8/20/2003
cwells: 8/12/2002
mgross: 2/17/2000
mcapotos: 2/3/2000
terry: 1/21/2000
terry: 5/13/1994
mimadm: 4/9/1994
carol: 4/5/1993
carol: 6/9/1992
carol: 6/2/1992
supermim: 3/16/1992
*RECORD*
*FIELD* NO
114890
*FIELD* TI
*114890 CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE 5; CEACAM5
;;CARCINOEMBRYONIC ANTIGEN; CEA
read more*FIELD* TX
DESCRIPTION
Members of the CEACAM subfamily, including CEACAM5, belong to the CEA
gene family. For general information on the CEA gene family, see CEACAM1
(109770).
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 (see 176390); the CEACAM subfamily, which includes
CEACAM1 (BGP), CEACAM3 (CGM1; 609142), 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 (see 109770). The CEA gene was
renamed CEACAM5.
CLONING
Carcinoembryonic antigen was first described by Gold and Freedman (1965)
as a complex immunoreactive glycoprotein. Oikawa et al. (1987) cloned
cDNAs corresponding to the mRNA encoding a polypeptide that is
immunoreactive with the antisera specific to CEA. The amino acid
sequence deduced from the nucleotide sequence of the cDNA showed that
CEA is synthesized as a precursor with a signal peptide followed by 668
amino acids of the putative mature CEA peptide.
Zimmermann et al. (1987) isolated and characterized cDNA clones for
human CEA. They found no CEA mRNA in HeLa cells or in normal human
fibroblasts.
Kamarck et al. (1987) prepared a cDNA for CEA from an adenocarcinoma
cell line. They confirmed its identity by specific hybridization to DNA
transfected into L cells, which then expressed CEA. Hybridization of the
cDNA insert to genomic DNA from colon carcinoma cells showed no
rearrangement in the tumors.
MAPPING
By analysis of somatic cell hybrids, Kamarck et al. (1987) mapped the
CEA gene to chromosome 19.
By genomic clones used in somatic cell hybrids and by in situ
hybridization, Willcocks et al. (1987, 1989) assigned the CEA locus to
19q13.1-q13.3. Zimmermann et al. (1988) used a DNA fragment from the NCA
gene to localize the gene(s) by in situ hybridization to chromosome 19.
Two specific hybridization sites were found, 1 on the long arm,
19q31-q32, and a minor accumulation on the short arm, 19p13.2-p13.3.
Zimmermann et al. (1988) also used a fragment from the repeat region of
the CEA cDNA clone to map the gene to 19q31-q32 by in situ
hybridization. No accumulation of grains was observed over the short
arm. Nishi et al. (1991) assigned the CEA gene to 19q13.2 by in situ
hybridization. Thompson and Zimmermann (1988) stated that the CEA gene
family, consisting of approximately 10 genes, is localized in 2 clusters
on chromosome 19. By the time of their report, mRNA species for 5 of the
genes had been identified and found to show tissue variability in their
transcriptional activity. Willcocks and Craig (1990) found that the CEA
gene comprises 9 exons encoding amino acids and 1 encoding a 3-prime
untranslated fragment. Thompson et al. (1992) stated that various
methods, including hybridization analysis of large DNA fragments
separated by pulsed field gel electrophoresis, yielded similar results,
indicating that the entire CEA gene family is contained in a region
located at 19q13.1-q13.2 between the CYP2A (122720) and D19S15/D19S8
markers. They found that the CEA subgroup has 9 members, including CEA,
nonspecific crossreacting antigen, biliary glycoprotein (BGP), and 6
genes referred to as CEA gene family members: CGM1, CGM2, CGM6, CGM7,
CGM8, and CGM9. From large groups of ordered cosmid clones, Thompson et
al. (1992) confirmed the identity of all known CEA subgroup genes,
either by hybridization using gene-specific probes or by DNA sequencing.
These studies identified a new member of the CEA subgroup, CGM8, which
they concluded probably represents a pseudogene due to the existence of
2 stop codons, one in the leader exon and one in the N-terminal domain
exon. The gene order and orientation, which were determined with
hybridization with probes from the 5-prime and 3-prime regions of the
genes, were determined to be as follows: cen/3-prime CGM7/3-prime
CGM2/5-prime CEA/5-prime NCA/5-prime CGM1/3-prime BGP/3-prime
CGM9/3-prime CGM6/5-prime CGM8///PSG cluster/qter. By fluorescence in
situ hybridization, Brandriff et al. (1992) concluded that the gene
order is cen--CGM7--CEA--NCA--CGM1--BGP--CGM9--CGM8--PSG--tel. The order
agreed completely with that obtained by Thompson et al. (1992).
GENE FUNCTION
CEA injected into experimental animals accumulates in the liver and is
largely confined to macrophages (Kupffer cells) (Toth et al., 1982). The
binding domain of the protein was narrowed to the hinge region between
its N domain and its first (A1) immunoglobulin loop domain. Furthermore,
the binding domain was narrowed to amino acids 108-112 (PELPK) (Thomas
et al., 1992; Gangopadhyay and Thomas, 1996).
Zimmer and Thomas (2001) noted that CEA expression is used clinically to
monitor patients with colorectal and other cancers and that a subset of
these patients have extraordinarily high CEA levels that cannot be
attributed solely to tumor load. In addition, elevated levels of serum
CEA are found in patients with benign liver disease including cirrhosis,
biliary obstruction, and hepatitis. In tumor cells of 3 of 8 colorectal
cancer patients with high CEA levels, Zimmer and Thomas (2001)
identified heterozygous mutations in the region of CEA (PELPK motif)
responsible for its hepatic clearance. CEA with mutations in the PELPK
motif showed remarkably reduced circulatory clearance rates in an animal
model. A patient without mutation in the region showed normal clearance
rates. Zimmer and Thomas (2001) concluded that mutations in PELPK may
affect structural stability and binding affinity to the Kupffer receptor
in the liver. They suggested that CEA may have a role as a facilitator
of hepatic metastasis.
By generating a chimeric protein of CEACAM5 and NCAM1 (116930),
Nicholson and Stanners (2007) identified a novel specificity signal of 6
amino acids (PGLSAG) within the glycophosphatidylinositol (GPI) anchor
attachment signal of CEACAM5 that was necessary and sufficient to
specify the addition of a particular functional GPI.
Muenzner et al. (2010) found that CEA-binding bacteria colonized the
urogenital tract of CEA transgenic mice, but not of wildtype mice, by
suppressing exfoliation of mucosal cells. CEA binding triggered de novo
expression of the transforming growth factor receptor CD105 (131195),
changing focal adhesion composition and activating beta-1 integrins
(135630). Muenzner et al. (2010) concluded that this manipulation of
integrin inside-out signaling promotes efficient mucosal colonization
and represents a potential target to prevent or cure bacterial
infections.
*FIELD* SA
Thompson et al. (1987)
*FIELD* RF
1. 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.
2. 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.
3. Gangopadhyay, A.; Thomas, P.: Processing of carcinoembryonic antigen
by Kupffer cells: recognition of a penta-peptide sequence. Arch.
Biochem. Biophys. 334: 151-157, 1996.
4. Gold, P.; Freedman, S. O.: Demonstration of tumor-specific antigens
in human colonic carcinomata by immunological tolerance and absorption
techniques. J. Exp. Med. 121: 439-462, 1965.
5. Kamarck, M. E.; Elting, J. J.; Hart, J. T.; Goebel, S. J.; Rae,
P. M. M.; Nothdurft, M. A.; Nedwin, J. J.; Barnett, T. R.: Carcinoembryonic
antigen family: expression in a mouse L-cell transfectant and characterization
of a partial cDNA in bacteriophage lambda-gt11. Proc. Nat. Acad.
Sci. 84: 5350-5354, 1987.
6. Muenzner, P.; Bachmann, V.; Zimmermann, W.; Hentschel, J.; Hauck,
C. R.: Human-restricted bacterial pathogens block shedding of epithelial
cells by stimulating integrin activation. Science 329: 1197-1201,
2010.
7. Nicholson, T. B.; Stanners, C. P.: Identification of a novel functional
specificity signal within the GPI anchor signal sequence of carcinoembryonic
antigen. J. Cell Biol. 177: 211-218, 2007.
8. Nishi, M.; Inazawa, J.; Inoue, K.; Nakagawa, H.; Taniwaki, M.;
Misawa, S.; Oikawa, S.; Nakazato, H.; Abe, T.: Regional chromosomal
assignment of carcinoembryonic antigen gene (CEA) to chromosome 19
at band q13.2. Cancer Genet. Cytogenet. 54: 77-81, 1991.
9. Oikawa, S.; Nakazato, H.; Kosaki, G.: Primary structure of human
carcinoembryonic antigen (CEA) deduced from cDNA sequence. Biochem.
Biophys. Res. Commun. 142: 511-528, 1987.
10. Thomas, P.; Petrick, A. T.; Toth, C. A.; Fox, E. S.; Elting, J.
J.; Steele, G., Jr.: A peptide sequence on carcinoembryonic antigen
binds to a 80 kD protein on Kupffer cells. Biochem. Biophys. Res.
Commun. 188: 671-677, 1992.
11. Thompson, J.; Zimmermann, W.: The carcinoembryonic antigen gene
family: structure, expression and evolution. Tumour Biol. 9: 63-83,
1988.
12. 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.
13. 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.
14. Toth, C. A.; Thomas, P.; Broitman, S. A.; Zamcheck, N.: A new
Kupffer cell receptor mediating plasma clearance of carcinoembryonic
antigen by the rat. Biochem. J. 204: 377-381, 1982.
15. Willcocks, T. C.; Craig, I. W.: Characterization of the genomic
organization of human carcinoembryonic antigen (CEA): comparison with
other family members and sequence analysis of 5-prime controlling
region. Genomics 8: 492-500, 1990.
16. Willcocks, T. C.; Craig, S. P.; Coates, D.; Craig, I. W.: Coding
sequences for carcinoembryonic antigen (CEA) assigned to human chromosome
19q13. (Abstract) Cytogenet. Cell Genet. 46: 716 only, 1987.
17. Willcocks, T. C.; Craig, S. P.; Craig, I. W.: Assignment of the
coding sequence for carcinoembryonic antigen (CEA) and normal cross-reacting
antigen (NCA) to human chromosome 19q13. Ann. Hum. Genet. 53: 141-148,
1989.
18. Zimmer, R.; Thomas, P.: Mutations in the carcinoembryonic antigen
gene in colorectal cancer patients: implications on liver metastasis. Cancer
Res. 61: 2822-2826, 2001.
19. Zimmermann, W.; Ortlieb, B.; Friedrich, R.; von Kleist, S.: Isolation
and characterization of cDNA clones encoding the human carcinoembryonic
antigen reveal a highly conserved repeating structure. Proc. Nat.
Acad. Sci. 84: 2960-2964, 1987.
20. Zimmermann, W.; Weber, B.; Ortlieb, B.; Rudert, F.; Schempp, W.;
Fiebig, H.-H.; Shively, J. E.; von Kleist, S.; Thompson, J. A.: Chromosomal
localization of the carcinoembryonic antigen gene family and differential
expression in various tumors. Cancer Res. 48: 2550-2554, 1988.
*FIELD* CN
Ada Hamosh - updated: 10/27/2010
Paul J. Converse - updated: 11/9/2009
Victor A. McKusick - updated: 8/12/2002
Victor A. McKusick - updated: 1/21/2000
*FIELD* CD
Victor A. McKusick: 4/14/1987
*FIELD* ED
alopez: 10/27/2010
carol: 9/17/2010
terry: 12/1/2009
mgross: 11/11/2009
terry: 11/9/2009
carol: 10/29/2009
mgross: 1/5/2005
mgross: 8/20/2003
cwells: 8/12/2002
mgross: 2/17/2000
mcapotos: 2/3/2000
terry: 1/21/2000
terry: 5/13/1994
mimadm: 4/9/1994
carol: 4/5/1993
carol: 6/9/1992
carol: 6/2/1992
supermim: 3/16/1992