ICAM1_BOVIN
ID ICAM1_BOVIN Reviewed; 535 AA.
AC Q95132;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Intercellular adhesion molecule 1;
DE Short=ICAM-1;
DE AltName: CD_antigen=CD54;
DE Flags: Precursor;
GN Name=ICAM1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9437830; DOI=10.1016/s0165-2427(97)00051-2;
RA Lee E.K., Kang S.G., Kehrli M.E. Jr.;
RT "Cloning, sequencing and analysis of cDNA encoding bovine intercellular
RT adhesion molecule-1 (ICAM-1).";
RL Vet. Immunol. Immunopathol. 59:121-129(1997).
CC -!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein
CC LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial
CC migration, ICAM1 engagement promotes the assembly of endothelial apical
CC cups through ARHGEF26/SGEF and RHOG activation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with MUC1 and promotes cell aggregation
CC in epithelial cells. Interacts with ARHGEF26/SGEF. Interacts (on T cell
CC side) with CD81, CD247 and CD9 at immunological synapses between
CC antigen-presenting cells and T cells. {ECO:0000250|UniProtKB:P05362}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to
CC endocytosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U65789; AAB06749.1; -; mRNA.
DR RefSeq; NP_776773.1; NM_174348.2.
DR AlphaFoldDB; Q95132; -.
DR SMR; Q95132; -.
DR STRING; 9913.ENSBTAP00000013608; -.
DR PaxDb; Q95132; -.
DR PRIDE; Q95132; -.
DR GeneID; 281839; -.
DR KEGG; bta:281839; -.
DR CTD; 3383; -.
DR eggNOG; ENOG502S45R; Eukaryota.
DR InParanoid; Q95132; -.
DR OrthoDB; 731140at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
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; IPR036179; Ig-like_dom_sf.
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; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..535
FT /note="Intercellular adhesion molecule 1"
FT /id="PRO_0000014780"
FT TOPO_DOM 28..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..102
FT /note="Ig-like C2-type 1"
FT DOMAIN 127..193
FT /note="Ig-like C2-type 2"
FT DOMAIN 230..295
FT /note="Ig-like C2-type 3"
FT DOMAIN 323..376
FT /note="Ig-like C2-type 4"
FT DOMAIN 410..463
FT /note="Ig-like C2-type 5"
FT MOTIF 151..153
FT /note="Cell attachment site; atypical"
FT /evidence="ECO:0000255"
FT MOD_RES 533
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 52..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 134..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 237..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 330..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 401..417
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 417..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 429..456
FT /evidence="ECO:0000250|UniProtKB:P05362"
SQ 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
