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

 ICAM1_BOVIN             Reviewed;         535 AA.
Q95132;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 119.
RecName: Full=Intercellular adhesion molecule 1;
Short=ICAM-1;
AltName: CD_antigen=CD54;
Flags: Precursor;
Name=ICAM1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9437830; DOI=10.1016/S0165-2427(97)00051-2;
Lee E.K., Kang S.G., Kehrli M.E. Jr.;
"Cloning, sequencing and analysis of cDNA encoding bovine
intercellular adhesion molecule-1 (ICAM-1).";
Vet. Immunol. Immunopathol. 59:121-129(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; Single-pass type I membrane
protein.
-!- 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; U65789; AAB06749.1; -; mRNA.
RefSeq; NP_776773.1; NM_174348.2.
UniGene; Bt.5372; -.
ProteinModelPortal; Q95132; -.
SMR; Q95132; -.
STRING; 9913.ENSBTAP00000013608; -.
PaxDb; Q95132; -.
PRIDE; Q95132; -.
GeneID; 281839; -.
KEGG; bta:281839; -.
CTD; 3383; -.
eggNOG; ENOG410IPHM; Eukaryota.
eggNOG; ENOG410YQ1Q; LUCA.
HOGENOM; HOG000059554; -.
HOVERGEN; HBG052074; -.
InParanoid; Q95132; -.
KO; K06490; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005178; F:integrin binding; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
Gene3D; 2.60.40.10; -; 6.
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 28 535 Intercellular adhesion molecule 1.
/FTId=PRO_0000014780.
TOPO_DOM 28 480 Extracellular. {ECO:0000255}.
TRANSMEM 481 503 Helical. {ECO:0000255}.
TOPO_DOM 504 535 Cytoplasmic. {ECO:0000255}.
DOMAIN 41 102 Ig-like C2-type 1.
DOMAIN 127 193 Ig-like C2-type 2.
DOMAIN 230 295 Ig-like C2-type 3.
DOMAIN 323 376 Ig-like C2-type 4.
DOMAIN 410 463 Ig-like C2-type 5.
MOTIF 151 153 Cell attachment site; atypical.
{ECO:0000255}.
MOD_RES 533 533 Phosphothreonine.
{ECO:0000250|UniProtKB:P05362}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 131 131 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 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 357 357 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 404 404 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 91 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 52 95 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 134 186 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 237 288 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 330 369 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 401 417 {ECO:0000250|UniProtKB:P05362}.
DISULFID 417 456 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 429 456 {ECO:0000250|UniProtKB:P05362}.
SEQUENCE 535 AA; 58429 MW; 7485EBE9C04D10B3 CRC64;
MALGAAPAAQ LALLALLGTL LPGPGGAGIS IHPSKAIIPR GDSLTVNCSN SCDQKSTFGL
ETVLIKEEVG RGDNWKVFQL RDVQEDIELF CYSNCHKEQT IASMNLTVYW FPEHVELAPL
PLWQPVGEEL NLSCLVSGGA PRAHLSVVLL RGEEELGRQP VGKGEPAKVM FTVQSRREDH
GTNFSCRWEL DLRSQGLELF QNTSAPRKLQ TYVLPSIDPH LEVPPIVEVG SRWPVNCTLD
GLFPASDAKV YLVLGDQKLE SNITYDGDSV LAKAWMEENE EGTHSLKCSV TLGEVSRRTQ
ENVTVYSFPL PTLTLSPPEV SEWTTVTVEC VTRDGAVVKL NGTSAVPPGP RAQLKLNASA
SDHRSNFSCS AALEIAGQVV HKHQTLELHV LYGPRLDQRD CPGNWTWQEG SEQTLKCEAQ
GNPIPKLNCS RKGDGASLPI GDLRPVRREV AGTYLCRATS ARGRVTREVV LNVLHGQNIL
DIVIPVVAVT LILGALGTAG YVYNYQRKIQ KYELQKARKA QEEAALKLNA QSTPP


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