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Q00238 (ICAM1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Intercellular adhesion molecule 1

Short name=ICAM-1
Alternative name(s):
CD_antigen=CD54
Gene names
Name:Icam1
Synonyms:Icam-1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length545 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Subunit structure

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

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

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

Sequence similarities

Belongs to the immunoglobulin superfamily. ICAM family.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell

Inferred from electronic annotation. Source: Ensembl

T cell antigen processing and presentation

Inferred from electronic annotation. Source: Ensembl

acute inflammatory response to antigenic stimulus

Inferred from mutant phenotype PubMed 7641842. Source: RGD

adhesion to symbiont

Inferred from electronic annotation. Source: Ensembl

cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

cell aging

Inferred from expression pattern PubMed 20421514. Source: RGD

cell-cell adhesion

Inferred from direct assay PubMed 12097510. Source: RGD

cellular response to alkaloid

Inferred from expression pattern PubMed 20674665. Source: RGD

cellular response to glucose stimulus

Inferred from expression pattern PubMed 20627932. Source: RGD

cellular response to hypoxia

Inferred from expression pattern PubMed 20386459. Source: RGD

cellular response to interleukin-1

Inferred from expression pattern PubMed 20643106. Source: RGD

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 20674665. Source: RGD

cellular response to nutrient levels

Inferred from expression pattern PubMed 20643106. Source: RGD

cellular response to organic substance

Inferred from expression pattern PubMed 20870297. Source: RGD

cellular response to tumor necrosis factor

Inferred from expression pattern PubMed 15087287. Source: RGD

leukocyte cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Traceable author statement PubMed 12183646. Source: RGD

membrane to membrane docking

Inferred from electronic annotation. Source: Ensembl

negative regulation of calcium ion transport

Inferred from direct assay PubMed 15087287. Source: RGD

ovarian follicle development

Inferred from expression pattern PubMed 20591976. Source: RGD

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 9062344. Source: RGD

positive regulation of Rho GTPase activity

Inferred from direct assay PubMed 17662049. Source: RGD

positive regulation of actin filament polymerization

Inferred from direct assay PubMed 17662049. Source: RGD

positive regulation of cellular extravasation

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from mutant phenotype PubMed 9062344. Source: RGD

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 17662049. Source: RGD

positive regulation of vasoconstriction

Inferred from mutant phenotype PubMed 12296653. Source: RGD

receptor-mediated virion attachment to host cell

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from mutant phenotype PubMed 15087287. Source: RGD

response to amino acid

Inferred from expression pattern PubMed 20599905. Source: RGD

response to amphetamine

Inferred from expression pattern PubMed 21093552. Source: RGD

response to copper ion

Inferred from expression pattern PubMed 20544302. Source: RGD

response to drug

Inferred from expression pattern PubMed 20871620. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 20726338. Source: RGD

response to gonadotropin

Inferred from expression pattern PubMed 20591976. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 19823174. Source: RGD

response to ionizing radiation

Inferred from expression pattern PubMed 20385203. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 20871155. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 20740350. Source: RGD

response to sulfur dioxide

Inferred from expression pattern PubMed 20951496. Source: RGD

   Cellular_componentcell surface

Inferred from direct assay PubMed 8938183. Source: RGD

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 18413153. Source: RGD

immunological synapse

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 15087287. Source: RGD

   Molecular_functionintegrin binding

Inferred from mutant phenotype PubMed 16825578. Source: RGD

protein complex binding

Inferred from physical interaction PubMed 10556544. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Chain28 – 545518Intercellular adhesion molecule 1
PRO_0000014788

Regions

Topological domain28 – 492465Extracellular Potential
Transmembrane493 – 51725Helical; Potential
Topological domain518 – 54528Cytoplasmic Potential
Domain41 – 10363Ig-like C2-type 1
Domain128 – 19366Ig-like C2-type 2
Domain230 – 29768Ig-like C2-type 3
Domain325 – 38965Ig-like C2-type 4
Domain423 – 47654Ig-like C2-type 5
Motif177 – 1793Cell attachment site Potential

Amino acid modifications

Glycosylation471N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation1831N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation3441N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4391N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Potential
Disulfide bond48 ↔ 92 By similarity
Disulfide bond52 ↔ 96 By similarity
Disulfide bond135 ↔ 186 By similarity
Disulfide bond237 ↔ 290 By similarity
Disulfide bond332 ↔ 382 By similarity
Disulfide bond430 ↔ 469 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q00238 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 30F4546FA4D0CFF4

FASTA54560,142
        10         20         30         40         50         60 
MASTRARPML PLLLVLVAVV IPGPVGAQVS IHPTEAFLPR GGSVQVNCSS SCEDENLGLG 

        70         80         90        100        110        120 
LETNWMKDEL SSGHNWKLFK LSDIGEDSRP LCFENCGTTQ SSASATITVY SFPERVELDP 

       130        140        150        160        170        180 
LPAWQQVGKN LILRCLVEGG APRTQLSVVL LRGNETLSRQ AVDGDPKEIT FTVLASRGDH 

       190        200        210        220        230        240 
GANFSCFTEL DLRPQGLSLF KNVSEVRQLR TFDLPTRVLK LDTPDLLEVG TQQKFLCSLE 

       250        260        270        280        290        300 
GLFPASEAQI YLEMGGQMLT LESTNSRDFV SATASVEVTE KLDRTLQLRC VLELADQTLE 

       310        320        330        340        350        360 
MEKTLRIYNF SAPILTLSQP EVSEGDQVTV KCEAHGGAQV VLLNSTSPRP PTSQGTSPRP 

       370        380        390        400        410        420 
PTSQIQFTLN ASPEDHKRRF FCSAALEVDG KSLFKNQTLE LHVLYGPHLD KKDCLGNWTW 

       430        440        450        460        470        480 
QEGSQQTLTC QPQGNPAPNL TCSRKADGVP LPIGMVKSVK REMNGTYKCR AFSSRGSITR 

       490        500        510        520        530        540 
DVHLTVLYHD QNTWVIIVGV LVLIIAGFVI VASIYTYYRQ RKIRIYKLQK AQEEALKLKV 


QAPPP 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and expression of rat ICAM-1."
Kita Y., Takashi T., Iigo Y., Tamatani T., Miyasaka M., Horiuchi T.
Biochim. Biophys. Acta 1131:108-110(1992) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00913 mRNA. Translation: BAA00759.1.
BC081837 mRNA. Translation: AAH81837.1.
PIRJU0341. S21765.
RefSeqNP_037099.1. NM_012967.1.
UniGeneRn.12.

3D structure databases

ProteinModelPortalQ00238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4997073.
STRING10116.ENSRNOP00000028066.

PTM databases

PhosphoSiteQ00238.

Proteomic databases

PaxDbQ00238.
PRIDEQ00238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000028066; ENSRNOP00000028066; ENSRNOG00000020679.
GeneID25464.
KEGGrno:25464.
UCSCRGD:2857. rat.

Organism-specific databases

CTD3383.
RGD2857. Icam1.

Phylogenomic databases

eggNOGNOG146347.
GeneTreeENSGT00530000063246.
HOGENOMHOG000059554.
HOVERGENHBG052074.
InParanoidQ00238.
KOK06490.
OMARDCPGNW.
OrthoDBEOG7QG43X.
PhylomeDBQ00238.
TreeFamTF333745.

Gene expression databases

GenevestigatorQ00238.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PfamPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSPR01473. ICAM.
PR01472. ICAMVCAM1.
SMARTSM00409. IG. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio606747.
PROQ00238.

Entry information

Entry nameICAM1_RAT
AccessionPrimary (citable) accession number: Q00238
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families