ICAM1_CANLF
ID ICAM1_CANLF Reviewed; 528 AA.
AC P33729; Q28291;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Intercellular adhesion molecule 1;
DE Short=ICAM-1;
DE AltName: CD_antigen=CD54;
DE Flags: Precursor; Fragment;
GN Name=ICAM1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7758971; DOI=10.1016/0378-1119(95)00045-8;
RA Manning A.M., Lu H.F., Kukielka G.L., Oliver M.G., Ty T., Toman C.A.,
RA Drong R.F., Slightom J.L., Ballantyne C.M., Entman M.L.;
RT "Cloning and comparative sequence analysis of the gene encoding canine
RT intercellular adhesion molecule-1 (ICAM-1).";
RL Gene 156:291-295(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 184-413.
RC TISSUE=Cardiac myocyte;
RX PubMed=1680878; DOI=10.1172/jci115424;
RA Smith C.W., Entman M.L., Lane C.L., Beaudet A.L., Ty T.I., Youker K.,
RA Hawkins H.K., Anderson D.C.;
RT "Adherence of neutrophils to canine cardiac myocytes in vitro is dependent
RT on intercellular adhesion molecule-1.";
RL J. Clin. Invest. 88:1216-1223(1991).
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}.
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DR EMBL; L31625; AAA92551.1; -; mRNA.
DR EMBL; M68524; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; PC4025; PC4025.
DR AlphaFoldDB; P33729; -.
DR SMR; P33729; -.
DR STRING; 9612.ENSCAFP00000026375; -.
DR PaxDb; P33729; -.
DR eggNOG; ENOG502RZRA; Eukaryota.
DR InParanoid; P33729; -.
DR Proteomes; UP000002254; 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; 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.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..528
FT /note="Intercellular adhesion molecule 1"
FT /id="PRO_0000014781"
FT TOPO_DOM 25..476
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..99
FT /note="Ig-like C2-type 1"
FT DOMAIN 123..188
FT /note="Ig-like C2-type 2"
FT DOMAIN 225..292
FT /note="Ig-like C2-type 3"
FT DOMAIN 320..373
FT /note="Ig-like C2-type 4"
FT DOMAIN 407..460
FT /note="Ig-like C2-type 5"
FT MOTIF 147..149
FT /note="Cell attachment site; atypical"
FT /evidence="ECO:0000255"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..88
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 49..92
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 130..181
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 232..285
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 327..366
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 398..414
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 414..453
FT /evidence="ECO:0000250"
FT DISULFID 426..453
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT CONFLICT 225
FT /note="G -> D (in Ref. 2; M68524)"
FT /evidence="ECO:0000305"
FT CONFLICT 233..235
FT /note="TMD -> RHE (in Ref. 2; M68524)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="E -> V (in Ref. 2; M68524)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="L -> P (in Ref. 2; M68524)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="F -> S (in Ref. 2; M68524)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 528 AA; 57952 MW; 36BEDC1AF0FD6904 CRC64;
APALPRLPAL LALLGALLPG LGGAQTSVDP AEAIILRGGS VQVNCSTSCN QTSIFGLETL
LTKTEVTSGD NWVLFELTDV QEDSKLICFS NCHDETMAPI DLTVYWFPER VELAPLPRWQ
PVGENLTMTC QVAGGAPRTN LTVVLLRGEE ELSRQPAVGE PAEVTFTVAV GREDHLANFS
CRTDLDLRHR GLGLFQNSSA PRQLQTFVLP ETPPRLATPP IVEVGTQWSV DCTMDGVFPA
SEAQVHLALA EERLHSTVLY KKDSLLATAN VKANPEDEGT QQLWCEVTLG DENRRWQENV
TFYSFPAPNL TLSEPEVSEW TTVTVECEAP AGVVVSLSGL PSGLAVPRAQ FQLNASAADN
RRSFSCSAAL EVAGHMLQKN QTRELHVLYG PRLDQRDCPG NWTWEEGFHQ TLKCQAWGNP
VPELKCHRKG DDALLPIGDL RPVKREVAGT YLCQARSPRG EITREVVINV IYHQNNILII
ILVTTIVILG TVSVAAYLYN RQRKIQKYKL QKAQEAAAMK LNTPATPP
