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 24-JAN-2024, entry version 181. 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}. 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; 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 GlyCosmos; Q00238; 10 sites, No reported glycans. DR GlyGen; Q00238; 10 sites. DR PhosphoSitePlus; Q00238; -. DR PaxDb; 10116-ENSRNOP00000028066; -. DR Ensembl; ENSRNOT00055020953; ENSRNOP00055016925; ENSRNOG00055012304. DR Ensembl; ENSRNOT00060044644; ENSRNOP00060036996; ENSRNOG00060025722. DR Ensembl; ENSRNOT00065019442; ENSRNOP00065014883; ENSRNOG00065011961. DR GeneID; 25464; -. DR KEGG; rno:25464; -. DR UCSC; RGD:2857; rat. DR AGR; RGD:2857; -. 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 OrthoDB; 4014106at2759; -. 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 cell types or tissues. 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: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: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: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:0071346; P:cellular response to type II interferon; 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:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; 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: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: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 CDD; cd05755; IgC2_2_ICAM-1_like; 1. DR CDD; cd20996; IgI_N_ICAM-1; 1. 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; IPR007110; Ig-like_dom. 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; 4. DR SUPFAM; SSF48726; Immunoglobulin; 5. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; Q00238; RN. 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 //