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   27-MAR-2024, entry version 222.
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   GlyCosmos; P13597; 10 sites, No reported glycans.
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; 10090-ENSMUSP00000083587; -.
DR   PeptideAtlas; P13597; -.
DR   ProteomicsDB; 269522; -. [P13597-1]
DR   ProteomicsDB; 269523; -. [P13597-2]
DR   Antibodypedia; 795; 3640 antibodies from 54 providers.
DR   DNASU; 15894; -.
DR   Ensembl; ENSMUST00000086399.6; ENSMUSP00000083587.5; ENSMUSG00000037405.9. [P13597-1]
DR   GeneID; 15894; -.
DR   KEGG; mmu:15894; -.
DR   UCSC; uc009ojx.1; mouse. [P13597-1]
DR   AGR; MGI:96392; -.
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   OrthoDB; 4014106at2759; -.
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 80 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 191 other cell types or tissues.
DR   ExpressionAtlas; P13597; baseline and differential.
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: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:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; 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: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   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; P13597; MM.
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
//