ICAM1_PANPA
ID ICAM1_PANPA Reviewed; 532 AA.
AC Q5NKV4;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Intercellular adhesion molecule 1;
DE Short=ICAM-1;
DE AltName: CD_antigen=CD54;
DE Flags: Precursor;
GN Name=ICAM1;
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC 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; AF340048; AAQ14905.1; -; Genomic_DNA.
DR EMBL; AF340042; AAQ14905.1; JOINED; Genomic_DNA.
DR EMBL; AF340043; AAQ14905.1; JOINED; Genomic_DNA.
DR EMBL; AF340044; AAQ14905.1; JOINED; Genomic_DNA.
DR EMBL; AF340045; AAQ14905.1; JOINED; Genomic_DNA.
DR EMBL; AF340046; AAQ14905.1; JOINED; Genomic_DNA.
DR EMBL; AF340047; AAQ14905.1; JOINED; Genomic_DNA.
DR RefSeq; XP_003809639.1; XM_003809591.3.
DR AlphaFoldDB; Q5NKV4; -.
DR SMR; Q5NKV4; -.
DR STRING; 9597.XP_003809639.1; -.
DR PRIDE; Q5NKV4; -.
DR Ensembl; ENSPPAT00000044874; ENSPPAP00000022067; ENSPPAG00000034232.
DR GeneID; 100980120; -.
DR KEGG; pps:100980120; -.
DR CTD; 3383; -.
DR eggNOG; ENOG502S45R; Eukaryota.
DR GeneTree; ENSGT00940000162311; -.
DR OMA; NLTVYWF; -.
DR OrthoDB; 731140at2759; -.
DR Proteomes; UP000240080; Chromosome 19.
DR Bgee; ENSPPAG00000034232; Expressed in placenta and 6 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
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 3: Inferred from homology;
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_0000014786"
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 145
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 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
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:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 52..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 135..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 237..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 332..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 403..419
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 419..457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 431..457
FT /evidence="ECO:0000250|UniProtKB:P05362"
SQ SEQUENCE 532 AA; 57787 MW; 796DBC7A22628260 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 EDEGTQRLMC 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
