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Protein

Intercellular adhesion molecule 1

Gene

Icam1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

  • integrin binding Source: RGD
  • protein complex binding Source: RGD

GO - Biological processi

  • acute inflammatory response to antigenic stimulus Source: RGD
  • cell adhesion mediated by integrin Source: Ensembl
  • cell aging Source: RGD
  • cellular response to alkaloid Source: RGD
  • cellular response to glucose stimulus Source: RGD
  • cellular response to hypoxia Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to nutrient levels Source: RGD
  • cellular response to organic substance Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • establishment of endothelial barrier Source: Ensembl
  • establishment of Sertoli cell barrier Source: RGD
  • leukocyte migration Source: RGD
  • membrane to membrane docking Source: Ensembl
  • negative regulation of calcium ion transport Source: RGD
  • negative regulation of endothelial cell apoptotic process Source: Ensembl
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  • ovarian follicle development Source: RGD
  • positive regulation of actin filament polymerization Source: RGD
  • positive regulation of cellular extravasation Source: Ensembl
  • positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  • positive regulation of GTPase activity Source: RGD
  • positive regulation of NF-kappaB transcription factor activity Source: RGD
  • positive regulation of nitric oxide biosynthetic process Source: RGD
  • positive regulation of peptidyl-tyrosine phosphorylation Source: RGD
  • positive regulation of vasoconstriction Source: RGD
  • receptor-mediated virion attachment to host cell Source: Ensembl
  • regulation of cell adhesion Source: Ensembl
  • regulation of cell shape Source: RGD
  • regulation of ruffle assembly Source: Ensembl
  • response to amino acid Source: RGD
  • response to amphetamine Source: RGD
  • response to copper ion Source: RGD
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to gonadotropin Source: RGD
  • response to hypoxia Source: RGD
  • response to ionizing radiation Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to sulfur dioxide Source: RGD
  • sensory perception of sound Source: RGD
  • single organismal cell-cell adhesion Source: RGD
  • T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Source: Ensembl
  • T cell antigen processing and presentation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_307069. Integrin cell surface interactions.
REACT_310843. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Names & Taxonomyi

Protein namesi
Recommended name:
Intercellular adhesion molecule 1
Short name:
ICAM-1
Alternative name(s):
CD_antigen: CD54
Gene namesi
Name:Icam1
Synonyms:Icam-1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi2857. Icam1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 492465ExtracellularSequence AnalysisAdd
BLAST
Transmembranei493 – 51725HelicalSequence AnalysisAdd
BLAST
Topological domaini518 – 54528CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: RGD
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • focal adhesion Source: Ensembl
  • immunological synapse Source: Ensembl
  • integral component of plasma membrane Source: GO_Central
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727By similarityAdd
BLAST
Chaini28 – 545518Intercellular adhesion molecule 1PRO_0000014788Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi48 ↔ 92PROSITE-ProRule annotation
Disulfide bondi52 ↔ 96PROSITE-ProRule annotation
Disulfide bondi135 ↔ 186PROSITE-ProRule annotation
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi237 ↔ 290PROSITE-ProRule annotation
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi332 ↔ 382PROSITE-ProRule annotation
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi430 ↔ 469PROSITE-ProRule annotation
Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Monoubiquitinated, which is promoted by MARCH9 and leads to endocytosis.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ00238.
PRIDEiQ00238.

PTM databases

PhosphoSiteiQ00238.

Expressioni

Gene expression databases

GenevisibleiQ00238. RN.

Interactioni

Subunit structurei

Homodimer. Interacts with MUC1 and promotes cell aggregation in epithelial cells. Interacts with ARHGEF26/SGEF (By similarity).By similarity

Protein-protein interaction databases

MINTiMINT-4997073.
STRINGi10116.ENSRNOP00000028066.

Structurei

3D structure databases

ProteinModelPortaliQ00238.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 10363Ig-like C2-type 1Add
BLAST
Domaini128 – 19366Ig-like C2-type 2Add
BLAST
Domaini230 – 29768Ig-like C2-type 3Add
BLAST
Domaini325 – 38965Ig-like C2-type 4Add
BLAST
Domaini423 – 47654Ig-like C2-type 5Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi177 – 1793Cell attachment siteSequence Analysis

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. ICAM family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG146347.
GeneTreeiENSGT00530000063246.
HOGENOMiHOG000059554.
HOVERGENiHBG052074.
InParanoidiQ00238.
KOiK06490.
OMAiRDCPGNW.
OrthoDBiEOG7QG43X.
PhylomeDBiQ00238.
TreeFamiTF333745.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PfamiPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSiPR01473. ICAM.
PR01472. ICAMVCAM1.
SMARTiSM00409. IG. 2 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00238-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTRARPML PLLLVLVAVV IPGPVGAQVS IHPTEAFLPR GGSVQVNCSS
60 70 80 90 100
SCEDENLGLG LETNWMKDEL SSGHNWKLFK LSDIGEDSRP LCFENCGTTQ
110 120 130 140 150
SSASATITVY SFPERVELDP LPAWQQVGKN LILRCLVEGG APRTQLSVVL
160 170 180 190 200
LRGNETLSRQ AVDGDPKEIT FTVLASRGDH GANFSCFTEL DLRPQGLSLF
210 220 230 240 250
KNVSEVRQLR TFDLPTRVLK LDTPDLLEVG TQQKFLCSLE GLFPASEAQI
260 270 280 290 300
YLEMGGQMLT LESTNSRDFV SATASVEVTE KLDRTLQLRC VLELADQTLE
310 320 330 340 350
MEKTLRIYNF SAPILTLSQP EVSEGDQVTV KCEAHGGAQV VLLNSTSPRP
360 370 380 390 400
PTSQGTSPRP PTSQIQFTLN ASPEDHKRRF FCSAALEVDG KSLFKNQTLE
410 420 430 440 450
LHVLYGPHLD KKDCLGNWTW QEGSQQTLTC QPQGNPAPNL TCSRKADGVP
460 470 480 490 500
LPIGMVKSVK REMNGTYKCR AFSSRGSITR DVHLTVLYHD QNTWVIIVGV
510 520 530 540
LVLIIAGFVI VASIYTYYRQ RKIRIYKLQK AQEEALKLKV QAPPP
Length:545
Mass (Da):60,142
Last modified:December 1, 1992 - v1
Checksum:i30F4546FA4D0CFF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00913 mRNA. Translation: BAA00759.1.
BC081837 mRNA. Translation: AAH81837.1.
PIRiS21765. JU0341.
RefSeqiNP_037099.1. NM_012967.1.
UniGeneiRn.12.

Genome annotation databases

EnsembliENSRNOT00000028066; ENSRNOP00000028066; ENSRNOG00000020679.
GeneIDi25464.
KEGGirno:25464.
UCSCiRGD:2857. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00913 mRNA. Translation: BAA00759.1.
BC081837 mRNA. Translation: AAH81837.1.
PIRiS21765. JU0341.
RefSeqiNP_037099.1. NM_012967.1.
UniGeneiRn.12.

3D structure databases

ProteinModelPortaliQ00238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4997073.
STRINGi10116.ENSRNOP00000028066.

PTM databases

PhosphoSiteiQ00238.

Proteomic databases

PaxDbiQ00238.
PRIDEiQ00238.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028066; ENSRNOP00000028066; ENSRNOG00000020679.
GeneIDi25464.
KEGGirno:25464.
UCSCiRGD:2857. rat.

Organism-specific databases

CTDi3383.
RGDi2857. Icam1.

Phylogenomic databases

eggNOGiNOG146347.
GeneTreeiENSGT00530000063246.
HOGENOMiHOG000059554.
HOVERGENiHBG052074.
InParanoidiQ00238.
KOiK06490.
OMAiRDCPGNW.
OrthoDBiEOG7QG43X.
PhylomeDBiQ00238.
TreeFamiTF333745.

Enzyme and pathway databases

ReactomeiREACT_307069. Integrin cell surface interactions.
REACT_310843. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Miscellaneous databases

NextBioi606747.
PROiQ00238.

Gene expression databases

GenevisibleiQ00238. RN.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PfamiPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSiPR01473. ICAM.
PR01472. ICAMVCAM1.
SMARTiSM00409. IG. 2 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.

Entry informationi

Entry nameiICAM1_RAT
AccessioniPrimary (citable) accession number: Q00238
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 24, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.