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Intercellular adhesion molecule 1 (ICAM-1) (CD antigen CD54)

 ICAM1_RAT               Reviewed;         545 AA.
Q00238;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
22-NOV-2017, entry version 152.
RecName: Full=Intercellular adhesion molecule 1;
Short=ICAM-1;
AltName: CD_antigen=CD54;
Flags: Precursor;
Name=Icam1; Synonyms=Icam-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1349828; DOI=10.1016/0167-4781(92)90107-B;
Kita Y., Takashi T., Iigo Y., Tamatani T., Miyasaka M., Horiuchi T.;
"Sequence and expression of rat ICAM-1.";
Biochim. Biophys. Acta 1131:108-110(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion
protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-
endothelial migration, ICAM1 engagement promotes the assembly of
endothelial apical cups through ARHGEF26/SGEF and RHOG activation
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with MUC1 and promotes cell
aggregation in epithelial cells. Interacts with ARHGEF26/SGEF (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to
endocytosis. {ECO:0000250}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D00913; BAA00759.1; -; mRNA.
EMBL; BC081837; AAH81837.1; -; mRNA.
PIR; S21765; JU0341.
RefSeq; NP_037099.1; NM_012967.1.
UniGene; Rn.12; -.
ProteinModelPortal; Q00238; -.
SMR; Q00238; -.
MINT; MINT-4997073; -.
STRING; 10116.ENSRNOP00000028066; -.
PhosphoSitePlus; Q00238; -.
PaxDb; Q00238; -.
PRIDE; Q00238; -.
Ensembl; ENSRNOT00000028066; ENSRNOP00000028066; ENSRNOG00000020679.
GeneID; 25464; -.
KEGG; rno:25464; -.
UCSC; RGD:2857; rat.
CTD; 3383; -.
RGD; 2857; Icam1.
eggNOG; ENOG410IPHM; Eukaryota.
eggNOG; ENOG410YQ1Q; LUCA.
GeneTree; ENSGT00530000063246; -.
HOGENOM; HOG000059554; -.
HOVERGEN; HBG052074; -.
InParanoid; Q00238; -.
KO; K06490; -.
OMA; QTLRCQA; -.
OrthoDB; EOG091G022Y; -.
PhylomeDB; Q00238; -.
TreeFam; TF333745; -.
Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-RNO-216083; Integrin cell surface interactions.
Reactome; R-RNO-877300; Interferon gamma signaling.
PRO; PR:Q00238; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000020679; -.
Genevisible; Q00238; RN.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031012; C:extracellular matrix; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0001772; C:immunological synapse; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005178; F:integrin binding; IMP:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IMP:RGD.
GO; GO:0044406; P:adhesion of symbiont to host; ISO:RGD.
GO; GO:0007155; P:cell adhesion; ISO:RGD.
GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:RGD.
GO; GO:0007569; P:cell aging; IEP:RGD.
GO; GO:0098609; P:cell-cell adhesion; IDA:RGD.
GO; GO:0071312; P:cellular response to alkaloid; IEP:RGD.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0071346; P:cellular response to interferon-gamma; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0031669; P:cellular response to nutrient levels; IEP:RGD.
GO; GO:0071310; P:cellular response to organic substance; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0061028; P:establishment of endothelial barrier; ISO:RGD.
GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:RGD.
GO; GO:0097368; P:establishment of Sertoli cell barrier; IDA:RGD.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
GO; GO:0050900; P:leukocyte migration; ISO:RGD.
GO; GO:0022614; P:membrane to membrane docking; ISO:RGD.
GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:RGD.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:RGD.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:RGD.
GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:RGD.
GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IMP:RGD.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; ISO:RGD.
GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
GO; GO:0008360; P:regulation of cell shape; IMP:RGD.
GO; GO:1900027; P:regulation of ruffle assembly; ISO:RGD.
GO; GO:0043200; P:response to amino acid; IEP:RGD.
GO; GO:0001975; P:response to amphetamine; IEP:RGD.
GO; GO:0046688; P:response to copper ion; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010477; P:response to sulfur dioxide; IEP:RGD.
GO; GO:0007605; P:sensory perception of sound; IMP:RGD.
GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; ISO:RGD.
GO; GO:0002457; P:T cell antigen processing and presentation; ISO:RGD.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR003988; ICAM.
InterPro; IPR013768; ICAM_N.
InterPro; IPR003987; ICAM_VCAM_N.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
Pfam; PF03921; ICAM_N; 1.
PRINTS; PR01473; ICAM.
PRINTS; PR01472; ICAMVCAM1.
SMART; SM00409; IG; 4.
SUPFAM; SSF48726; SSF48726; 5.
PROSITE; PS50835; IG_LIKE; 1.
2: Evidence at transcript level;
Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 27 {ECO:0000250}.
CHAIN 28 545 Intercellular adhesion molecule 1.
/FTId=PRO_0000014788.
TOPO_DOM 28 492 Extracellular. {ECO:0000255}.
TRANSMEM 493 517 Helical. {ECO:0000255}.
TOPO_DOM 518 545 Cytoplasmic. {ECO:0000255}.
DOMAIN 41 103 Ig-like C2-type 1.
DOMAIN 128 193 Ig-like C2-type 2.
DOMAIN 230 297 Ig-like C2-type 3.
DOMAIN 325 389 Ig-like C2-type 4.
DOMAIN 423 476 Ig-like C2-type 5.
MOTIF 177 179 Cell attachment site. {ECO:0000255}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 344 344 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 439 439 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 92 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 52 96 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 135 186 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 237 290 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 332 382 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 414 430 {ECO:0000250|UniProtKB:P05362}.
DISULFID 430 469 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 442 469 {ECO:0000250|UniProtKB:P05362}.
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


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