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Intercellular adhesion molecule 1 (ICAM-1) (CD antigen CD54)

 ICAM1_PANTR             Reviewed;         532 AA.
Q28806; Q5NKW2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 2.
25-OCT-2017, entry version 132.
RecName: Full=Intercellular adhesion molecule 1;
Short=ICAM-1;
AltName: CD_antigen=CD54;
Flags: Precursor;
Name=ICAM1;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Isolate Bonnie, Isolate Caesar, and Isolate Jenny;
TISSUE=Blood;
Messier W., Walter N.A.R., Hink R.L.;
"The chimpanzee ICAM proteins have been positively selected.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-532.
PubMed=9105055; DOI=10.1164/ajrccm.155.4.9105055;
Huguenel E.D., Cohn D., Dockum D.P., Greve J.M., Fournel M.A.,
Hammond L., Irwin R., Mahoney J., McClelland A., Muchmore E.,
Ohlin A.C., Scuderi P.;
"Prevention of rhinovirus infection in chimpanzees by soluble
intercellular adhesion molecule-1.";
Am. J. Respir. Crit. Care Med. 155:1206-1210(1997).
-!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion
protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-
endothelial migration, ICAM1 engagement promotes the assembly of
endothelial apical cups through ARHGEF26/SGEF and RHOG activation
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with MUC1 and promotes cell
aggregation in epithelial cells. Interacts with ARHGEF26/SGEF (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}.
-!- PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to
endocytosis. {ECO:0000250}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM
family. {ECO:0000305}.
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EMBL; AF340033; AAQ14896.1; -; mRNA.
EMBL; AF340034; AAQ14897.1; -; mRNA.
EMBL; AF340035; AAQ14898.1; -; mRNA.
EMBL; M86848; AAA35415.1; -; mRNA.
RefSeq; NP_001009946.1; NM_001009946.1.
UniGene; Ptr.2910; -.
ProteinModelPortal; Q28806; -.
SMR; Q28806; -.
STRING; 9598.ENSPTRP00000017827; -.
PaxDb; Q28806; -.
Ensembl; ENSPTRT00000019261; ENSPTRP00000017827; ENSPTRG00000010463.
GeneID; 450196; -.
KEGG; ptr:450196; -.
CTD; 3383; -.
eggNOG; ENOG410IPHM; Eukaryota.
eggNOG; ENOG410YQ1Q; LUCA.
GeneTree; ENSGT00530000063246; -.
HOGENOM; HOG000059554; -.
HOVERGEN; HBG052074; -.
InParanoid; Q28806; -.
KO; K06490; -.
OMA; QTLRCQA; -.
OrthoDB; EOG091G022Y; -.
TreeFam; TF333745; -.
Proteomes; UP000002277; Chromosome 19.
Bgee; ENSPTRG00000010463; -.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0002693; P:positive regulation of cellular extravasation; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:Ensembl.
GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IEA:Ensembl.
GO; GO:0002457; P:T cell antigen processing and presentation; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR003988; ICAM.
InterPro; IPR013768; ICAM_N.
InterPro; IPR003987; ICAM_VCAM_N.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
Pfam; PF03921; ICAM_N; 1.
PRINTS; PR01473; ICAM.
PRINTS; PR01472; ICAMVCAM1.
SMART; SM00409; IG; 3.
SUPFAM; SSF48726; SSF48726; 5.
PROSITE; PS50835; IG_LIKE; 1.
2: Evidence at transcript level;
Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 27 {ECO:0000250}.
CHAIN 28 532 Intercellular adhesion molecule 1.
/FTId=PRO_0000014787.
TOPO_DOM 28 480 Extracellular. {ECO:0000255}.
TRANSMEM 481 503 Helical. {ECO:0000255}.
TOPO_DOM 504 532 Cytoplasmic. {ECO:0000255}.
DOMAIN 41 103 Ig-like C2-type 1.
DOMAIN 128 193 Ig-like C2-type 2.
DOMAIN 230 297 Ig-like C2-type 3.
DOMAIN 325 378 Ig-like C2-type 4.
DOMAIN 412 464 Ig-like C2-type 5.
MOTIF 152 154 Cell attachment site; atypical.
{ECO:0000255}.
MOD_RES 521 521 Phosphothreonine.
{ECO:0000250|UniProtKB:P05362}.
MOD_RES 530 530 Phosphothreonine.
{ECO:0000250|UniProtKB:P05362}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 385 385 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 92 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 52 96 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 135 186 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 237 290 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 332 371 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 403 419 {ECO:0000250|UniProtKB:P05362}.
DISULFID 419 457 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 431 457 {ECO:0000250|UniProtKB:P05362}.
SEQUENCE 532 AA; 57757 MW; 896DBC7E9C5A61E4 CRC64;
MAPSSPRPAL PALLVLLGAL FPGPGNAQTS VSPPKVILPR GGSVQVTCST SCDQPDLLGI
ETPLPKKELL LGGNNWKVYE LSNVQEDSQP MCYSNCPDGQ STAKTFLTVY WTPERVELAP
LPSWQPVGKD LTLRCQVEGG APRANLTVVL LRGEKELKRE PAVGEPAEVT TTVLVERDHH
GANFSCRTEL DLRPQGLQLF ENTSAPHQLQ TFVLPATPPQ LVSPRVLEVD TQGTVVCSLD
GLFPVLEAQV HLALGDQRLN PTVTYGNDSF SAKASVSVTA EDEGTQRLTC AVILGNQSRE
TLQTVTIYSF PAPNVILTKP EVSEGTEVTV KCEAHPRAKV TLNGVPAQPV GPRVQLLLKA
TPEDNGRSFS CSATLEVAGQ LIHKNQTREL RVLYGPRLDE RDCPGNWTWP ENSQQTPMCQ
ASGNPLPELK CLKDGTFPLP VGESVTVTRD LEGTYLCRAR STQGEVTRKV TVNVLSPRYE
IVIITVVAAA VIMGTAGLST YLYNRQRKIR KYRLQQAQKG TPMKPNTQAT PP


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