ICAM1_MOUSE
ID ICAM1_MOUSE Reviewed; 537 AA.
AC P13597; Q61828;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Intercellular adhesion molecule 1;
DE Short=ICAM-1;
DE AltName: Full=MALA-2;
DE AltName: Full=MyD10;
DE AltName: CD_antigen=CD54;
DE Flags: Precursor;
GN Name=Icam1; Synonyms=Icam-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=BALB/cJ; TISSUE=Myeloma;
RX PubMed=2573511; DOI=10.1002/j.1460-2075.1989.tb08437.x;
RA Horley K.J., Carpenito C., Baker B., Takei F.;
RT "Molecular cloning of murine intercellular adhesion molecule (ICAM-1).";
RL EMBO J. 8:2889-2896(1989).
RN [2]
RP SEQUENCE REVISION.
RA Takei F.;
RL Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2479693;
RA Siu G., Hedrick S.M., Brian A.A.;
RT "Isolation of the murine intercellular adhesion molecule 1 (ICAM-1) gene.
RT ICAM-1 enhances antigen-specific T cell activation.";
RL J. Immunol. 143:3813-3820(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX PubMed=2762164; DOI=10.1093/nar/17.14.5853;
RA Ballantyne C.M., O'Brien W.E., Beaudet A.L.;
RT "Nucleotide sequence of the cDNA for murine intercellular adhesion
RT molecule-1 (ICAM-1).";
RL Nucleic Acids Res. 17:5853-5853(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NIH Swiss;
RX PubMed=1362180; DOI=10.1016/s0888-7543(05)80132-6;
RA Ballantyne C.M., Sligh J.E., Dai X.Y., Beaudet A.L.;
RT "Characterization of the murine Icam-1 gene.";
RL Genomics 14:1076-1080(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-131.
RX PubMed=1690380;
RA Lord K.A., Hoffman-Liebermann B., Liebermann D.A.;
RT "Complexity of the immediate early response of myeloid cells to terminal
RT differentiation and growth arrest includes ICAM-1, Jun-B and histone
RT variants.";
RL Oncogene 5:387-396(1990).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=9207125; DOI=10.1073/pnas.94.14.7526;
RA Dong Z.M., Gutierrez-Ramos J.C., Coxon A., Mayadas T.N., Wagner D.D.;
RT "A new class of obesity genes encodes leukocyte adhesion receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7526-7530(1997).
RN [8]
RP GLYCOSYLATION AT ASN-47; ASN-185; ASN-204; ASN-267; ASN-311; ASN-362;
RP ASN-388; ASN-409 AND ASN-456, LACK OF GLYCOSYLATION AT ASN-469 AND ASN-485,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16877748; DOI=10.1093/glycob/cwl032;
RA Otto V.I., Damoc E., Cueni L.N., Schurpf T., Frei R., Ali S.,
RA Callewaert N., Moise A., Leary J.A., Folkers G., Przybylski M.;
RT "N-glycan structures and N-glycosylation sites of mouse soluble
RT intercellular adhesion molecule-1 revealed by MALDI-TOF and FTICR mass
RT spectrometry.";
RL Glycobiology 16:1033-1044(2006).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185; ASN-204; ASN-362; ASN-388;
RP ASN-409 AND ASN-469.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P13597-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13597-2; Sequence=VSP_002518;
CC -!- TISSUE SPECIFICITY: Expressed at low level on a subpopulation of
CC lymphocytes, macrophages, and endothelial cells, but is strongly
CC induced on these cells, and on fibroblasts and epithelial cells.
CC -!- PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to
CC endocytosis. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Spontaneous onset of obesity in 16-week old mice
CC with higher levels of white and brown fat and a slightly heavier liver.
CC Enhanced susceptibility to high fat diet-induced obesity characterized
CC by a weight increase and higher levels of white and brown fat.
CC {ECO:0000269|PubMed:9207125}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=ICAM-1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_288";
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DR EMBL; X16624; CAA34621.1; -; mRNA.
DR EMBL; X16625; CAA34622.1; -; mRNA.
DR EMBL; M31585; AAA37876.1; -; mRNA.
DR EMBL; X52264; CAA36507.1; -; mRNA.
DR EMBL; M90551; AAA37875.1; -; Genomic_DNA.
DR EMBL; M90546; AAA37875.1; JOINED; Genomic_DNA.
DR EMBL; M90547; AAA37875.1; JOINED; Genomic_DNA.
DR EMBL; M90548; AAA37875.1; JOINED; Genomic_DNA.
DR EMBL; M90549; AAA37875.1; JOINED; Genomic_DNA.
DR EMBL; M90550; AAA37875.1; JOINED; Genomic_DNA.
DR EMBL; X54331; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS22889.1; -. [P13597-1]
DR PIR; A45815; A45815.
DR PIR; I49769; I49769.
DR PIR; S06016; S06016.
DR RefSeq; NP_034623.1; NM_010493.3. [P13597-1]
DR AlphaFoldDB; P13597; -.
DR SMR; P13597; -.
DR DIP; DIP-29096N; -.
DR IntAct; P13597; 1.
DR STRING; 10090.ENSMUSP00000083587; -.
DR GlyGen; P13597; 10 sites.
DR iPTMnet; P13597; -.
DR PhosphoSitePlus; P13597; -.
DR CPTAC; non-CPTAC-3362; -.
DR EPD; P13597; -.
DR jPOST; P13597; -.
DR MaxQB; P13597; -.
DR PaxDb; P13597; -.
DR PeptideAtlas; P13597; -.
DR PRIDE; P13597; -.
DR ProteomicsDB; 269522; -. [P13597-1]
DR ProteomicsDB; 269523; -. [P13597-2]
DR Antibodypedia; 795; 3102 antibodies from 53 providers.
DR DNASU; 15894; -.
DR Ensembl; ENSMUST00000086399; ENSMUSP00000083587; ENSMUSG00000037405. [P13597-1]
DR GeneID; 15894; -.
DR KEGG; mmu:15894; -.
DR UCSC; uc009ojx.1; mouse. [P13597-1]
DR CTD; 3383; -.
DR MGI; MGI:96392; Icam1.
DR VEuPathDB; HostDB:ENSMUSG00000037405; -.
DR eggNOG; ENOG502S45R; Eukaryota.
DR GeneTree; ENSGT00940000162311; -.
DR HOGENOM; CLU_036160_1_1_1; -.
DR InParanoid; P13597; -.
DR OMA; NLTVYWF; -.
DR PhylomeDB; P13597; -.
DR TreeFam; TF333745; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR BioGRID-ORCS; 15894; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Icam1; mouse.
DR PRO; PR:P13597; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P13597; protein.
DR Bgee; ENSMUSG00000037405; Expressed in right lung lobe and 188 other tissues.
DR ExpressionAtlas; P13597; baseline and differential.
DR Genevisible; P13597; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; ISO:MGI.
DR GO; GO:0044406; P:adhesion of symbiont to host; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:MGI.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; ISO:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
DR GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; ISO:MGI.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:1900027; P:regulation of ruffle assembly; IDA:MGI.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; ISO:MGI.
DR GO; GO:0002457; P:T cell antigen processing and presentation; IDA:MGI.
DR GO; GO:0072683; P:T cell extravasation; IMP:MGI.
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 Pfam; PF13895; Ig_2; 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 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..537
FT /note="Intercellular adhesion molecule 1"
FT /id="PRO_0000014785"
FT TOPO_DOM 28..485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..102
FT /note="Ig-like C2-type 1"
FT DOMAIN 127..195
FT /note="Ig-like C2-type 2"
FT DOMAIN 232..299
FT /note="Ig-like C2-type 3"
FT DOMAIN 327..381
FT /note="Ig-like C2-type 4"
FT DOMAIN 415..468
FT /note="Ig-like C2-type 5"
FT MOTIF 151..153
FT /note="Cell attachment site; atypical"
FT /evidence="ECO:0000255"
FT MOTIF 179..181
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT SITE 469
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:16877748"
FT SITE 485
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:16877748"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16877748"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16877748,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16877748,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16877748"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16877748"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16877748,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16877748,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16877748,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16877748"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 48..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 52..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 134..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 239..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 334..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 406..422
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT DISULFID 422..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 434..461
FT /evidence="ECO:0000250|UniProtKB:P05362"
FT VAR_SEQ 1..34
FT /note="MASTRAKPTLPLLLALVTVVIPGPGDAQVSIHPR -> MITHRHPVREKSIN
FT SYQFIKEKQFPAEN (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002518"
FT CONFLICT 243
FT /note="G -> A (in Ref. 3; AAA37876)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="R -> A (in Ref. 1; CAA34621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 58844 MW; 6124167753774555 CRC64;
MASTRAKPTL PLLLALVTVV IPGPGDAQVS IHPREAFLPQ GGSVQVNCSS SCKEDLSLGL
ETQWLKDELE SGPNWKLFEL SEIGEDSSPL CFENCGTVQS SASATITVYS FPESVELRPL
PAWQQVGKDL TLRCHVDGGA PRTQLSAVLL RGEEILSRQP VGGHPKDPKE ITFTVLASRG
DHGANFSCRT ELDLRPQGLA LFSNVSEARS LRTFDLPATI PKLDTPDLLE VGTQQKLFCS
LEGLFPASEA RIYLELGGQM PTQESTNSSD SVSATALVEV TEEFDRTLPL RCVLELADQI
LETQRTLTVY NFSAPVLTLS QLEVSEGSQV TVKCEAHSGS KVVLLSGVEP RPPTPQVQFT
LNASSEDHKR SFFCSAALEV AGKFLFKNQT LELHVLYGPR LDETDCLGNW TWQEGSQQTL
KCQAWGNPSP KMTCRRKADG ALLPIGVVKS VKQEMNGTYV CHAFSSHGNV TRNVYLTVLY
HSQNNWTIII LVPVLLVIVG LVMAASYVYN RQRKIRIYKL QKAQEEAIKL KGQAPPP
