ICAM1_RAT
ID ICAM1_RAT Reviewed; 545 AA.
AC Q00238;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Intercellular adhesion molecule 1;
DE Short=ICAM-1;
DE AltName: CD_antigen=CD54;
DE Flags: Precursor;
GN Name=Icam1; Synonyms=Icam-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1349828; DOI=10.1016/0167-4781(92)90107-b;
RA Kita Y., Takashi T., Iigo Y., Tamatani T., Miyasaka M., Horiuchi T.;
RT "Sequence and expression of rat ICAM-1.";
RL Biochim. Biophys. Acta 1131:108-110(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; D00913; BAA00759.1; -; mRNA.
DR EMBL; BC081837; AAH81837.1; -; mRNA.
DR PIR; S21765; JU0341.
DR RefSeq; NP_037099.1; NM_012967.1.
DR AlphaFoldDB; Q00238; -.
DR SMR; Q00238; -.
DR STRING; 10116.ENSRNOP00000028066; -.
DR GlyGen; Q00238; 10 sites.
DR PhosphoSitePlus; Q00238; -.
DR PaxDb; Q00238; -.
DR PRIDE; Q00238; -.
DR GeneID; 25464; -.
DR KEGG; rno:25464; -.
DR UCSC; RGD:2857; rat.
DR CTD; 3383; -.
DR RGD; 2857; Icam1.
DR VEuPathDB; HostDB:ENSRNOG00000020679; -.
DR eggNOG; ENOG502RZRA; Eukaryota.
DR HOGENOM; CLU_036160_1_1_1; -.
DR InParanoid; Q00238; -.
DR OMA; NLTVYWF; -.
DR OrthoDB; 731140at2759; -.
DR PhylomeDB; Q00238; -.
DR TreeFam; TF333745; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR PRO; PR:Q00238; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000020679; Expressed in lung and 18 other tissues.
DR Genevisible; Q00238; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005178; F:integrin binding; IMP:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IMP:RGD.
DR GO; GO:0044406; P:adhesion of symbiont to host; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:RGD.
DR GO; GO:0071312; P:cellular response to alkaloid; IEP:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0031669; P:cellular response to nutrient levels; IEP:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0090398; P:cellular senescence; IEP:RGD.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:RGD.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; IDA:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0050900; P:leukocyte migration; ISO:RGD.
DR GO; GO:0022614; P:membrane to membrane docking; ISO:RGD.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:RGD.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:RGD.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:RGD.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:RGD.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IMP:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
DR GO; GO:0070234; P:positive regulation of T cell apoptotic process; ISO:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; IMP:RGD.
DR GO; GO:1900027; P:regulation of ruffle assembly; ISO:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010477; P:response to sulfur dioxide; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007605; P:sensory perception of sound; IMP:RGD.
DR GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; ISO:RGD.
DR GO; GO:0002457; P:T cell antigen processing and presentation; ISO:RGD.
DR GO; GO:0072683; P:T cell extravasation; ISO:RGD.
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; 4.
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; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..545
FT /note="Intercellular adhesion molecule 1"
FT /id="PRO_0000014788"
FT TOPO_DOM 28..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..545
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..389
FT /note="Ig-like C2-type 4"
FT DOMAIN 423..476
FT /note="Ig-like C2-type 5"
FT REGION 343..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 177..179
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
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 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
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..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 414..430
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 430..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 442..469
FT /evidence="ECO:0000250|UniProtKB:P05362"
SQ SEQUENCE 545 AA; 60142 MW; 30F4546FA4D0CFF4 CRC64;
MASTRARPML PLLLVLVAVV IPGPVGAQVS IHPTEAFLPR GGSVQVNCSS SCEDENLGLG
LETNWMKDEL SSGHNWKLFK LSDIGEDSRP LCFENCGTTQ SSASATITVY SFPERVELDP
LPAWQQVGKN LILRCLVEGG APRTQLSVVL LRGNETLSRQ AVDGDPKEIT FTVLASRGDH
GANFSCFTEL DLRPQGLSLF KNVSEVRQLR TFDLPTRVLK LDTPDLLEVG TQQKFLCSLE
GLFPASEAQI YLEMGGQMLT LESTNSRDFV SATASVEVTE KLDRTLQLRC VLELADQTLE
MEKTLRIYNF SAPILTLSQP EVSEGDQVTV KCEAHGGAQV VLLNSTSPRP PTSQGTSPRP
PTSQIQFTLN ASPEDHKRRF FCSAALEVDG KSLFKNQTLE LHVLYGPHLD KKDCLGNWTW
QEGSQQTLTC QPQGNPAPNL TCSRKADGVP LPIGMVKSVK REMNGTYKCR AFSSRGSITR
DVHLTVLYHD QNTWVIIVGV LVLIIAGFVI VASIYTYYRQ RKIRIYKLQK AQEEALKLKV
QAPPP
