ID ICAM1_GORGO Reviewed; 532 AA.
AC Q5NKV9;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 110.
DE RecName: Full=Intercellular adhesion molecule 1;
DE Short=ICAM-1;
DE AltName: CD_antigen=CD54;
DE Flags: Precursor;
GN Name=ICAM1;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate Kudzu, and Isolate Rok; TISSUE=Blood;
RA Messier W., Walter N.A.R., Hink R.L.;
RT "The chimpanzee ICAM proteins have been positively selected.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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}.
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DR EMBL; AF340036; AAQ14899.1; -; mRNA.
DR EMBL; AF340037; AAQ14900.1; -; mRNA.
DR RefSeq; NP_001266532.1; NM_001279603.1.
DR AlphaFoldDB; Q5NKV9; -.
DR SMR; Q5NKV9; -.
DR STRING; 9593.ENSGGOP00000038077; -.
DR GlyCosmos; Q5NKV9; 4 sites, No reported glycans.
DR Ensembl; ENSGGOT00000064956.1; ENSGGOP00000038077.1; ENSGGOG00000005980.3.
DR GeneID; 101127502; -.
DR KEGG; ggo:101127502; -.
DR CTD; 3383; -.
DR eggNOG; ENOG502RZRA; Eukaryota.
DR GeneTree; ENSGT00940000162311; -.
DR HOGENOM; CLU_036160_1_1_1; -.
DR InParanoid; Q5NKV9; -.
DR OrthoDB; 4014106at2759; -.
DR Proteomes; UP000001519; Chromosome 19.
DR Bgee; ENSGGOG00000005980; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:Ensembl.
DR GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
DR GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IEA:Ensembl.
DR GO; GO:0002457; P:T cell antigen processing and presentation; IEA:Ensembl.
DR GO; GO:0072683; P:T cell extravasation; IEA:Ensembl.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR048679; ICAM1_3_5_D2.
DR InterPro; IPR013768; ICAM_N.
DR InterPro; IPR047012; ICAM_VCAM.
DR InterPro; IPR003987; ICAM_VCAM_N.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1.
DR PANTHER; PTHR13771:SF18; INTERCELLULAR ADHESION MOLECULE 1; 1.
DR Pfam; PF21146; ICAM1_3_5_D2; 1.
DR Pfam; PF03921; ICAM_N; 1.
DR Pfam; PF13895; Ig_2; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
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..532
FT /note="Intercellular adhesion molecule 1"
FT /id="PRO_0000014782"
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..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..103
FT /note="Ig-like C2-type 1"
FT DOMAIN 128..193
FT /note="Ig-like C2-type 2"
FT DOMAIN 230..297
FT /note="Ig-like C2-type 3"
FT DOMAIN 325..378
FT /note="Ig-like C2-type 4"
FT DOMAIN 412..464
FT /note="Ig-like C2-type 5"
FT MOTIF 152..154
FT /note="Cell attachment site; atypical"
FT /evidence="ECO:0000255"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT MOD_RES 530
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..92
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 52..96
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 135..186
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 237..290
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 332..371
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 403..419
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 419..457
FT /evidence="ECO:0000250"
FT DISULFID 431..457
FT /evidence="ECO:0000250|UniProtKB:P05362"
SQ SEQUENCE 532 AA; 57848 MW; 53D400591CCE0B52 CRC64;
MAPSSPRPAL PALLVLLGAL FPGPGNAQTS VSPPKVILPR GGSVLVTCST SCDQPTLLGI
ETPLPKKELL LLGNNQKVYE LSNVQEDSQP MCYSNCPDGQ STAKTFLTVY WTPERVELAP
LPSWQPVGKD LTLRCQVEGG APRANLIVVL LRGEEELKRE PAVGEPAEVT TTVPVEKDHH
GANFLCRTEL DLRPQGLKLF ENTSAPYQLQ TFVLPATPPQ LVSPRVLEVD TQGTVVCSLD
GLFPVSEAQV HLALGDQRLN PTVTYGNDSF SAKASVSVTA EDEGTQWLTC AVILGTQSQE
TLQTVTIYSF PAPNVILTKP EVSEGTEVTV KCEAHPRAKV TLNGVPAQPP GPRTQFLLKA
TPEDNGRSFS CSATLEVAGQ LIHKNQTREL RVLYGPRLDE RDCPGNWTWP ENSQQTPMCQ
AWGNPLPELK CLKDGTFPLP VGESVTVTRD LEGTYLCRAR STQGEVTREV TVNVLSPRYE
FVIIAVVAAA VIMGTAGLST YLYNRQRKIR KYRLQQAQKG TPMKPNTQAT PP
//
