Full text data of ICAM3
ICAM3
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Intercellular adhesion molecule 3; ICAM-3 (CDw50; ICAM-R; CD50; Flags: Precursor)
Intercellular adhesion molecule 3; ICAM-3 (CDw50; ICAM-R; CD50; Flags: Precursor)
UniProt
P32942
ID ICAM3_HUMAN Reviewed; 547 AA.
AC P32942; Q6PD68;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 147.
DE RecName: Full=Intercellular adhesion molecule 3;
DE Short=ICAM-3;
DE AltName: Full=CDw50;
DE AltName: Full=ICAM-R;
DE AltName: CD_antigen=CD50;
DE Flags: Precursor;
GN Name=ICAM3;
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], AND VARIANTS AND GLY-115 GLY-143.
RX PubMed=1448173; DOI=10.1038/360481a0;
RA Fawcett J., Holness C.L., Needham L.A., Turley H., Gatter K.C.,
RA Mason D.Y., Simmons D.L.;
RT "Molecular cloning of ICAM-3, a third ligand for LFA-1, constitutively
RT expressed on resting leukocytes.";
RL Nature 360:481-484(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-115 AND GLY-143.
RX PubMed=1448174; DOI=10.1038/360485a0;
RA Vazeux R., Hoffman P.A., Tomita J.K., Dickinson E.S., Jasman R.L.,
RA St John T., Gallatin W.M.;
RT "Cloning and characterization of a new intercellular adhesion molecule
RT ICAM-R.";
RL Nature 360:485-488(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-115 AND GLY-143.
RX PubMed=8459213; DOI=10.1084/jem.177.4.1187;
RA de Fougerolles A.R., Kilckstein L.B., Springer T.A.;
RT "Cloning and expression of intercellular adhesion molecule 3 reveals
RT strong homology to other immunoglobulin family counter-receptors for
RT lymphocyte function-associated antigen 1.";
RL J. Exp. Med. 177:1187-1192(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tan J., Ong R., Hibberd M.L., Seielstad M.;
RT "Genetic variation in immune response genes.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 197-217; 269-293 AND 338-365.
RX PubMed=8325327; DOI=10.1002/eji.1830230717;
RA Juan M., Vilella R., Mila J., Yague J., Miralles A., Campbell K.S.,
RA Friedrich R.J., Cambier J., Vives J., de Fougerolles A.R.,
RA Springer T.A.;
RT "CDw50 and ICAM-3: two names for the same molecule.";
RL Eur. J. Immunol. 23:1508-1512(1993).
RN [8]
RP STRUCTURE OF N-LINKED CARBOHYDRATES.
RX PubMed=11179968; DOI=10.1046/j.1432-1327.2001.01960.x;
RA Funatsu O., Sato T., Kotovuori P., Gahmberg C.G., Ikekita M.,
RA Furukawa K.;
RT "Structural study of N-linked oligosaccharides of human intercellular
RT adhesion molecule-3 (CD50).";
RL Eur. J. Biochem. 268:1020-1029(2001).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363, 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 [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363, AND MASS
RP 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 [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-87; ASN-91;
RP ASN-134; ASN-206; ASN-295 AND ASN-363, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
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 [14]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 30-115 IN COMPLEX WITH
RP INTEGRIN ALPHALBETA2, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-52 AND
RP ASN-110.
RX PubMed=15728350; DOI=10.1073/pnas.0500200102;
RA Song G., Yang Y., Liu J.-H., Casasnovas J.M., Shimaoka M.,
RA Springer T.A., Wang J.-H.;
RT "An atomic resolution view of ICAM recognition in a complex between
RT the binding domains of ICAM-3 and integrin alphaLbeta2.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3366-3371(2005).
CC -!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion
CC protein LFA-1 (integrin alpha-L/beta-2). ICAM3 is also a ligand
CC for integrin alpha-D/beta-2.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein.
CC -!- PTM: Upon stimulation by a physiologic stimuli becomes rapidly and
CC transiently phosphorylated on serine residues.
CC -!- PTM: N-glycosylated; glycans consist of a mixture of tri- and
CC tetra-antennary complex-type chains and high-mannose chains.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM
CC family.
CC -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- WEB RESOURCE: Name=R&D; Systems' cytokine source book: ICAM-3;
CC URL="http://www.rndsystems.com/molecule_detail.aspx?m=1589";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=ICAM-3;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType;=view&cbpId;=cbp_hum_Itlect_263";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; S50015; AAB24331.2; ALT_SEQ; mRNA.
DR EMBL; X69711; CAA49369.1; -; mRNA.
DR EMBL; X69819; CAA49473.1; -; mRNA.
DR EMBL; DQ217937; ABB01007.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84092.1; -; Genomic_DNA.
DR EMBL; BC058903; AAH58903.1; -; mRNA.
DR PIR; S28904; S28904.
DR RefSeq; NP_002153.2; NM_002162.3.
DR UniGene; Hs.654563; -.
DR PDB; 1T0P; X-ray; 1.66 A; B=30-114.
DR PDBsum; 1T0P; -.
DR ProteinModelPortal; P32942; -.
DR SMR; P32942; 30-479.
DR IntAct; P32942; 3.
DR MINT; MINT-1391707; -.
DR STRING; 9606.ENSP00000160262; -.
DR PhosphoSite; P32942; -.
DR UniCarbKB; P32942; -.
DR DMDM; 206729872; -.
DR PaxDb; P32942; -.
DR PRIDE; P32942; -.
DR DNASU; 3385; -.
DR Ensembl; ENST00000160262; ENSP00000160262; ENSG00000076662.
DR GeneID; 3385; -.
DR KEGG; hsa:3385; -.
DR UCSC; uc002mob.2; human.
DR CTD; 3385; -.
DR GeneCards; GC19M010444; -.
DR H-InvDB; HIX0014743; -.
DR HGNC; HGNC:5346; ICAM3.
DR HPA; CAB002498; -.
DR MIM; 146631; gene.
DR neXtProt; NX_P32942; -.
DR PharmGKB; PA29594; -.
DR eggNOG; NOG146347; -.
DR HOGENOM; HOG000059554; -.
DR HOVERGEN; HBG052074; -.
DR InParanoid; P32942; -.
DR KO; K06486; -.
DR OMA; YGPKIDR; -.
DR OrthoDB; EOG7QG43X; -.
DR PhylomeDB; P32942; -.
DR Reactome; REACT_118779; Extracellular matrix organization.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; P32942; -.
DR GeneWiki; ICAM3; -.
DR GenomeRNAi; 3385; -.
DR NextBio; 13392; -.
DR PRO; PR:P32942; -.
DR ArrayExpress; P32942; -.
DR Bgee; P32942; -.
DR CleanEx; HS_ICAM3; -.
DR Genevestigator; P32942; -.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005178; F:integrin binding; TAS:ProtInc.
DR GO; GO:0016337; P:cell-cell adhesion; IEA:InterPro.
DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR013768; ICAM_N.
DR InterPro; IPR003987; ICAM_VCAM_N.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 29 Potential.
FT CHAIN 30 547 Intercellular adhesion molecule 3.
FT /FTId=PRO_0000014794.
FT TOPO_DOM 30 485 Extracellular (Potential).
FT TRANSMEM 486 510 Helical; (Potential).
FT TOPO_DOM 511 547 Cytoplasmic (Potential).
FT DOMAIN 46 103 Ig-like C2-type 1.
FT DOMAIN 132 197 Ig-like C2-type 2.
FT DOMAIN 234 301 Ig-like C2-type 3.
FT DOMAIN 329 382 Ig-like C2-type 4.
FT DOMAIN 416 469 Ig-like C2-type 5.
FT CARBOHYD 52 52 N-linked (GlcNAc...).
FT CARBOHYD 84 84 N-linked (GlcNAc...).
FT CARBOHYD 87 87 N-linked (GlcNAc...).
FT CARBOHYD 91 91 N-linked (GlcNAc...); atypical.
FT CARBOHYD 101 101 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 110 110 N-linked (GlcNAc...).
FT CARBOHYD 134 134 N-linked (GlcNAc...).
FT CARBOHYD 206 206 N-linked (GlcNAc...).
FT CARBOHYD 264 264 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 295 295 N-linked (GlcNAc...).
FT CARBOHYD 308 308 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 320 320 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 363 363 N-linked (GlcNAc...).
FT CARBOHYD 389 389 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 453 453 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 457 457 N-linked (GlcNAc...) (Potential).
FT DISULFID 53 96
FT DISULFID 139 190 Potential.
FT DISULFID 241 294 Potential.
FT DISULFID 336 375 Potential.
FT DISULFID 423 462 Potential.
FT VARIANT 63 63 I -> V (in dbSNP:rs17697947).
FT /FTId=VAR_046547.
FT VARIANT 115 115 R -> G (in dbSNP:rs7258015).
FT /FTId=VAR_059394.
FT VARIANT 143 143 D -> G (in dbSNP:rs2304237).
FT /FTId=VAR_046548.
FT VARIANT 525 525 S -> T (in dbSNP:rs2230399).
FT /FTId=VAR_024498.
FT CONFLICT 60 60 S -> F (in Ref. 1; AAB24331).
FT STRAND 34 38
FT STRAND 48 55
FT STRAND 61 66
FT STRAND 68 77
FT STRAND 80 86
FT STRAND 92 100
FT STRAND 103 113
SQ SEQUENCE 547 AA; 59541 MW; 4B7BDC02F24F3031 CRC64;
MATMVPSVLW PRACWTLLVC CLLTPGVQGQ EFLLRVEPQN PVLSAGGSLF VNCSTDCPSS
EKIALETSLS KELVASGMGW AAFNLSNVTG NSRILCSVYC NGSQITGSSN ITVYRLPERV
ELAPLPPWQP VGQNFTLRCQ VEDGSPRTSL TVVLLRWEEE LSRQPAVEEP AEVTATVLAS
RDDHGAPFSC RTELDMQPQG LGLFVNTSAP RQLRTFVLPV TPPRLVAPRF LEVETSWPVD
CTLDGLFPAS EAQVYLALGD QMLNATVMNH GDTLTATATA TARADQEGAR EIVCNVTLGG
ERREARENLT VFSFLGPIVN LSEPTAHEGS TVTVSCMAGA RVQVTLDGVP AAAPGQPAQL
QLNATESDDG RSFFCSATLE VDGEFLHRNS SVQLRVLYGP KIDRATCPQH LKWKDKTRHV
LQCQARGNPY PELRCLKEGS SREVPVGIPF FVNVTHNGTY QCQASSSRGK YTLVVVMDIE
AGSSHFVPVF VAVLLTLGVV TIVLALMYVF REHQRSGSYH VREESTYLPL TSMQPTEAMG
EEPSRAE
//
ID ICAM3_HUMAN Reviewed; 547 AA.
AC P32942; Q6PD68;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 147.
DE RecName: Full=Intercellular adhesion molecule 3;
DE Short=ICAM-3;
DE AltName: Full=CDw50;
DE AltName: Full=ICAM-R;
DE AltName: CD_antigen=CD50;
DE Flags: Precursor;
GN Name=ICAM3;
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], AND VARIANTS AND GLY-115 GLY-143.
RX PubMed=1448173; DOI=10.1038/360481a0;
RA Fawcett J., Holness C.L., Needham L.A., Turley H., Gatter K.C.,
RA Mason D.Y., Simmons D.L.;
RT "Molecular cloning of ICAM-3, a third ligand for LFA-1, constitutively
RT expressed on resting leukocytes.";
RL Nature 360:481-484(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-115 AND GLY-143.
RX PubMed=1448174; DOI=10.1038/360485a0;
RA Vazeux R., Hoffman P.A., Tomita J.K., Dickinson E.S., Jasman R.L.,
RA St John T., Gallatin W.M.;
RT "Cloning and characterization of a new intercellular adhesion molecule
RT ICAM-R.";
RL Nature 360:485-488(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-115 AND GLY-143.
RX PubMed=8459213; DOI=10.1084/jem.177.4.1187;
RA de Fougerolles A.R., Kilckstein L.B., Springer T.A.;
RT "Cloning and expression of intercellular adhesion molecule 3 reveals
RT strong homology to other immunoglobulin family counter-receptors for
RT lymphocyte function-associated antigen 1.";
RL J. Exp. Med. 177:1187-1192(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tan J., Ong R., Hibberd M.L., Seielstad M.;
RT "Genetic variation in immune response genes.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 197-217; 269-293 AND 338-365.
RX PubMed=8325327; DOI=10.1002/eji.1830230717;
RA Juan M., Vilella R., Mila J., Yague J., Miralles A., Campbell K.S.,
RA Friedrich R.J., Cambier J., Vives J., de Fougerolles A.R.,
RA Springer T.A.;
RT "CDw50 and ICAM-3: two names for the same molecule.";
RL Eur. J. Immunol. 23:1508-1512(1993).
RN [8]
RP STRUCTURE OF N-LINKED CARBOHYDRATES.
RX PubMed=11179968; DOI=10.1046/j.1432-1327.2001.01960.x;
RA Funatsu O., Sato T., Kotovuori P., Gahmberg C.G., Ikekita M.,
RA Furukawa K.;
RT "Structural study of N-linked oligosaccharides of human intercellular
RT adhesion molecule-3 (CD50).";
RL Eur. J. Biochem. 268:1020-1029(2001).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363, 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 [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363, AND MASS
RP 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 [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-87; ASN-91;
RP ASN-134; ASN-206; ASN-295 AND ASN-363, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
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 [14]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 30-115 IN COMPLEX WITH
RP INTEGRIN ALPHALBETA2, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-52 AND
RP ASN-110.
RX PubMed=15728350; DOI=10.1073/pnas.0500200102;
RA Song G., Yang Y., Liu J.-H., Casasnovas J.M., Shimaoka M.,
RA Springer T.A., Wang J.-H.;
RT "An atomic resolution view of ICAM recognition in a complex between
RT the binding domains of ICAM-3 and integrin alphaLbeta2.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3366-3371(2005).
CC -!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion
CC protein LFA-1 (integrin alpha-L/beta-2). ICAM3 is also a ligand
CC for integrin alpha-D/beta-2.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein.
CC -!- PTM: Upon stimulation by a physiologic stimuli becomes rapidly and
CC transiently phosphorylated on serine residues.
CC -!- PTM: N-glycosylated; glycans consist of a mixture of tri- and
CC tetra-antennary complex-type chains and high-mannose chains.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM
CC family.
CC -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- WEB RESOURCE: Name=R&D; Systems' cytokine source book: ICAM-3;
CC URL="http://www.rndsystems.com/molecule_detail.aspx?m=1589";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=ICAM-3;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType;=view&cbpId;=cbp_hum_Itlect_263";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR EMBL; S50015; AAB24331.2; ALT_SEQ; mRNA.
DR EMBL; X69711; CAA49369.1; -; mRNA.
DR EMBL; X69819; CAA49473.1; -; mRNA.
DR EMBL; DQ217937; ABB01007.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84092.1; -; Genomic_DNA.
DR EMBL; BC058903; AAH58903.1; -; mRNA.
DR PIR; S28904; S28904.
DR RefSeq; NP_002153.2; NM_002162.3.
DR UniGene; Hs.654563; -.
DR PDB; 1T0P; X-ray; 1.66 A; B=30-114.
DR PDBsum; 1T0P; -.
DR ProteinModelPortal; P32942; -.
DR SMR; P32942; 30-479.
DR IntAct; P32942; 3.
DR MINT; MINT-1391707; -.
DR STRING; 9606.ENSP00000160262; -.
DR PhosphoSite; P32942; -.
DR UniCarbKB; P32942; -.
DR DMDM; 206729872; -.
DR PaxDb; P32942; -.
DR PRIDE; P32942; -.
DR DNASU; 3385; -.
DR Ensembl; ENST00000160262; ENSP00000160262; ENSG00000076662.
DR GeneID; 3385; -.
DR KEGG; hsa:3385; -.
DR UCSC; uc002mob.2; human.
DR CTD; 3385; -.
DR GeneCards; GC19M010444; -.
DR H-InvDB; HIX0014743; -.
DR HGNC; HGNC:5346; ICAM3.
DR HPA; CAB002498; -.
DR MIM; 146631; gene.
DR neXtProt; NX_P32942; -.
DR PharmGKB; PA29594; -.
DR eggNOG; NOG146347; -.
DR HOGENOM; HOG000059554; -.
DR HOVERGEN; HBG052074; -.
DR InParanoid; P32942; -.
DR KO; K06486; -.
DR OMA; YGPKIDR; -.
DR OrthoDB; EOG7QG43X; -.
DR PhylomeDB; P32942; -.
DR Reactome; REACT_118779; Extracellular matrix organization.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; P32942; -.
DR GeneWiki; ICAM3; -.
DR GenomeRNAi; 3385; -.
DR NextBio; 13392; -.
DR PRO; PR:P32942; -.
DR ArrayExpress; P32942; -.
DR Bgee; P32942; -.
DR CleanEx; HS_ICAM3; -.
DR Genevestigator; P32942; -.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005178; F:integrin binding; TAS:ProtInc.
DR GO; GO:0016337; P:cell-cell adhesion; IEA:InterPro.
DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR013768; ICAM_N.
DR InterPro; IPR003987; ICAM_VCAM_N.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 29 Potential.
FT CHAIN 30 547 Intercellular adhesion molecule 3.
FT /FTId=PRO_0000014794.
FT TOPO_DOM 30 485 Extracellular (Potential).
FT TRANSMEM 486 510 Helical; (Potential).
FT TOPO_DOM 511 547 Cytoplasmic (Potential).
FT DOMAIN 46 103 Ig-like C2-type 1.
FT DOMAIN 132 197 Ig-like C2-type 2.
FT DOMAIN 234 301 Ig-like C2-type 3.
FT DOMAIN 329 382 Ig-like C2-type 4.
FT DOMAIN 416 469 Ig-like C2-type 5.
FT CARBOHYD 52 52 N-linked (GlcNAc...).
FT CARBOHYD 84 84 N-linked (GlcNAc...).
FT CARBOHYD 87 87 N-linked (GlcNAc...).
FT CARBOHYD 91 91 N-linked (GlcNAc...); atypical.
FT CARBOHYD 101 101 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 110 110 N-linked (GlcNAc...).
FT CARBOHYD 134 134 N-linked (GlcNAc...).
FT CARBOHYD 206 206 N-linked (GlcNAc...).
FT CARBOHYD 264 264 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 295 295 N-linked (GlcNAc...).
FT CARBOHYD 308 308 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 320 320 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 363 363 N-linked (GlcNAc...).
FT CARBOHYD 389 389 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 453 453 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 457 457 N-linked (GlcNAc...) (Potential).
FT DISULFID 53 96
FT DISULFID 139 190 Potential.
FT DISULFID 241 294 Potential.
FT DISULFID 336 375 Potential.
FT DISULFID 423 462 Potential.
FT VARIANT 63 63 I -> V (in dbSNP:rs17697947).
FT /FTId=VAR_046547.
FT VARIANT 115 115 R -> G (in dbSNP:rs7258015).
FT /FTId=VAR_059394.
FT VARIANT 143 143 D -> G (in dbSNP:rs2304237).
FT /FTId=VAR_046548.
FT VARIANT 525 525 S -> T (in dbSNP:rs2230399).
FT /FTId=VAR_024498.
FT CONFLICT 60 60 S -> F (in Ref. 1; AAB24331).
FT STRAND 34 38
FT STRAND 48 55
FT STRAND 61 66
FT STRAND 68 77
FT STRAND 80 86
FT STRAND 92 100
FT STRAND 103 113
SQ SEQUENCE 547 AA; 59541 MW; 4B7BDC02F24F3031 CRC64;
MATMVPSVLW PRACWTLLVC CLLTPGVQGQ EFLLRVEPQN PVLSAGGSLF VNCSTDCPSS
EKIALETSLS KELVASGMGW AAFNLSNVTG NSRILCSVYC NGSQITGSSN ITVYRLPERV
ELAPLPPWQP VGQNFTLRCQ VEDGSPRTSL TVVLLRWEEE LSRQPAVEEP AEVTATVLAS
RDDHGAPFSC RTELDMQPQG LGLFVNTSAP RQLRTFVLPV TPPRLVAPRF LEVETSWPVD
CTLDGLFPAS EAQVYLALGD QMLNATVMNH GDTLTATATA TARADQEGAR EIVCNVTLGG
ERREARENLT VFSFLGPIVN LSEPTAHEGS TVTVSCMAGA RVQVTLDGVP AAAPGQPAQL
QLNATESDDG RSFFCSATLE VDGEFLHRNS SVQLRVLYGP KIDRATCPQH LKWKDKTRHV
LQCQARGNPY PELRCLKEGS SREVPVGIPF FVNVTHNGTY QCQASSSRGK YTLVVVMDIE
AGSSHFVPVF VAVLLTLGVV TIVLALMYVF REHQRSGSYH VREESTYLPL TSMQPTEAMG
EEPSRAE
//
MIM
146631
*RECORD*
*FIELD* NO
146631
*FIELD* TI
*146631 INTERCELLULAR ADHESION MOLECULE 3; ICAM3
*FIELD* TX
CLONING
Fawcett et al. (1992) cloned a third ligand for LFA1 (153370; 600065);
read morealso see intercellular adhesion molecules 1 and 2 (ICAM1, 147840; ICAM2,
146630). ICAM1 and ICAM2 are members of the immunoglobulin superfamily.
The interaction of LFA1 with ICAM provides essential accessory adhesion
signals in many immune interactions, including those between T and B
lymphocytes and cytotoxic T cells and their targets. Both ICAMs are
expressed at low levels on resting vascular endothelium; ICAM1 is
strongly upregulated by cytokine stimulation and plays a key role in the
arrest of leukocytes in blood vessels at sites of inflammation and
injury. Resting leukocytes were shown to express a third ligand, ICAM3,
for LFA1. ICAM3 is potentially the most important ligand for LFA1 in the
initiation of the immune response because the expression of ICAM1 on
resting leukocytes is low. Fawcett et al. (1992) used expression cloning
to isolate a cDNA encoding a protein which is constitutively expressed
on all leukocytes and which binds LFA1. ICAM3 is closely related to
ICAM1, consists of 5 immunoglobulin domains, and binds LFA1 through its
2 N-terminal domains. Vazeux et al. (1992) cloned the same intercellular
adhesion molecule, which they referred to as ICAM-R. The cDNA was 1,781
bp long, with a 1,640-bp open reading frame starting with an ATG at
position 16, followed by a second ATG at position 24. Overall identities
in protein structure with ICAM1 and ICAM2 were 48% and 31%,
respectively, with the degree of similarity varying between individual
domains.
MAPPING
Using the cDNA as a probe, Bossy et al. (1994) mapped the ICAM3 gene to
19p13.3-p13.2 by isotopic in situ hybridization. They also mapped the
gene to chromosome 19 by PCR amplification of DNAs from somatic cell
hybrids. ICAM1 maps to the same region of chromosome 19.
*FIELD* RF
1. Bossy, D.; Mattei, M.-G.; Simmons, D. L.: The human intracellular
adhesion molecule 3 (ICAM3) gene is located in the 19p13.2-p13.3 region,
close to the ICAM1 gene. Genomics 23: 712-713, 1994.
2. Fawcett, J.; Holness, C. L. L.; Needham, L. A.; Turley, H.; Gatter,
K. C.; Mason, D. Y.; Simmons, D. L.: Molecular cloning of ICAM-3,
a third ligand for LFA-1, constitutively expressed on resting leukocytes. Nature 360:
481-484, 1992.
3. Vazeux, R.; Hoffman, P. A.; Tomita, J. K.; Dickinson, E. S.; Jasman,
R. L.; St. John, T.; Gallatin, W. M.: Cloning and characterization
of a new intercellular adhesion molecule ICAM-R. Nature 360: 485-488,
1992.
*FIELD* CN
Victor A. McKusick - updated: 8/22/1997
*FIELD* CD
Victor A. McKusick: 1/6/1993
*FIELD* ED
carol: 05/16/2007
carol: 5/15/2007
mgross: 3/15/2000
terry: 2/25/2000
dkim: 7/2/1998
mark: 8/26/1997
terry: 8/22/1997
carol: 6/14/1995
terry: 5/10/1994
warfield: 3/31/1994
carol: 1/28/1993
carol: 1/6/1993
*RECORD*
*FIELD* NO
146631
*FIELD* TI
*146631 INTERCELLULAR ADHESION MOLECULE 3; ICAM3
*FIELD* TX
CLONING
Fawcett et al. (1992) cloned a third ligand for LFA1 (153370; 600065);
read morealso see intercellular adhesion molecules 1 and 2 (ICAM1, 147840; ICAM2,
146630). ICAM1 and ICAM2 are members of the immunoglobulin superfamily.
The interaction of LFA1 with ICAM provides essential accessory adhesion
signals in many immune interactions, including those between T and B
lymphocytes and cytotoxic T cells and their targets. Both ICAMs are
expressed at low levels on resting vascular endothelium; ICAM1 is
strongly upregulated by cytokine stimulation and plays a key role in the
arrest of leukocytes in blood vessels at sites of inflammation and
injury. Resting leukocytes were shown to express a third ligand, ICAM3,
for LFA1. ICAM3 is potentially the most important ligand for LFA1 in the
initiation of the immune response because the expression of ICAM1 on
resting leukocytes is low. Fawcett et al. (1992) used expression cloning
to isolate a cDNA encoding a protein which is constitutively expressed
on all leukocytes and which binds LFA1. ICAM3 is closely related to
ICAM1, consists of 5 immunoglobulin domains, and binds LFA1 through its
2 N-terminal domains. Vazeux et al. (1992) cloned the same intercellular
adhesion molecule, which they referred to as ICAM-R. The cDNA was 1,781
bp long, with a 1,640-bp open reading frame starting with an ATG at
position 16, followed by a second ATG at position 24. Overall identities
in protein structure with ICAM1 and ICAM2 were 48% and 31%,
respectively, with the degree of similarity varying between individual
domains.
MAPPING
Using the cDNA as a probe, Bossy et al. (1994) mapped the ICAM3 gene to
19p13.3-p13.2 by isotopic in situ hybridization. They also mapped the
gene to chromosome 19 by PCR amplification of DNAs from somatic cell
hybrids. ICAM1 maps to the same region of chromosome 19.
*FIELD* RF
1. Bossy, D.; Mattei, M.-G.; Simmons, D. L.: The human intracellular
adhesion molecule 3 (ICAM3) gene is located in the 19p13.2-p13.3 region,
close to the ICAM1 gene. Genomics 23: 712-713, 1994.
2. Fawcett, J.; Holness, C. L. L.; Needham, L. A.; Turley, H.; Gatter,
K. C.; Mason, D. Y.; Simmons, D. L.: Molecular cloning of ICAM-3,
a third ligand for LFA-1, constitutively expressed on resting leukocytes. Nature 360:
481-484, 1992.
3. Vazeux, R.; Hoffman, P. A.; Tomita, J. K.; Dickinson, E. S.; Jasman,
R. L.; St. John, T.; Gallatin, W. M.: Cloning and characterization
of a new intercellular adhesion molecule ICAM-R. Nature 360: 485-488,
1992.
*FIELD* CN
Victor A. McKusick - updated: 8/22/1997
*FIELD* CD
Victor A. McKusick: 1/6/1993
*FIELD* ED
carol: 05/16/2007
carol: 5/15/2007
mgross: 3/15/2000
terry: 2/25/2000
dkim: 7/2/1998
mark: 8/26/1997
terry: 8/22/1997
carol: 6/14/1995
terry: 5/10/1994
warfield: 3/31/1994
carol: 1/28/1993
carol: 1/6/1993