ID VCAM1_MOUSE Reviewed; 739 AA. AC P29533; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 02-SEP-2026, entry version 215. DE RecName: Full=Vascular cell adhesion protein 1; DE Short=V-CAM 1; DE Short=VCAM-1; DE AltName: CD_antigen=CD106; DE Contains: DE RecName: Full=Soluble Vascular Cell Adhesion Molecule-1; DE Flags: Precursor; GN Name=Vcam1; Synonyms=Vcam-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] (ISOFORM 1). RC STRAIN=FVB/NJ; TISSUE=Lung; RX PubMed=1371918; DOI=10.1016/0006-291x(92)91623-x; RA Hession C., Moy P., Tizard R., Chisholm P., Williams C., Wysk M., RA Burkly L., Miyake K., Kincade P., Lobb R.; RT "Cloning of murine and rat vascular cell adhesion molecule-1."; RL Biochem. Biophys. Res. Commun. 183:163-169(1992). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC TISSUE=Lymph node; RX PubMed=7683304; DOI=10.1016/0378-1119(93)90377-f; RA Araki M., Araki K., Vassalli P.; RT "Cloning and sequencing of mouse VCAM-1 cDNA."; RL Gene 126:261-264(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RC STRAIN=129; TISSUE=Embryo; RX PubMed=7507076; DOI=10.1006/geno.1993.1480; RA Cybulsky M.I., Allan-Motamed M., Collins T.; RT "Structure of the murine VCAM1 gene."; RL Genomics 18:387-391(1993). RN [4] RP NUCLEOTIDE SEQUENCE OF 1-693 (ISOFORM 1). RC STRAIN=129/Sv, and NIH Swiss; RA Kumar A.G., Dai Y.X., Kozak C.A., Mims M.P., Gotto A.M. Jr., RA Ballantyne C.M.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=FVB/NJ; TISSUE=Lung; RX PubMed=7682556; DOI=10.1016/s0021-9258(18)52949-5; RA Moy P., Lobb R., Tizard R., Olson D., Hession C.; RT "Cloning of an inflammation-specific phosphatidyl inositol-linked form of RT murine vascular cell adhesion molecule-1."; RL J. Biol. Chem. 268:8835-8841(1993). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=7523515; DOI=10.4049/jimmunol.153.9.4088; RA Kumar A.G., Dai X.Y., Kozak C.A., Mims M.P., Gotto A.M. Jr., RA Ballantyne C.M.; RT "Murine VCAM-1. Molecular cloning, mapping, and analysis of a truncated RT form."; RL J. Immunol. 153:4088-4098(1994). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 311-345 (ISOFORM 2), AND GPI-ANCHOR AT RP ASN-319 (ISOFORM 2). RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=7687058; DOI=10.1073/pnas.90.13.5919; RA Terry R.W., Kwee L., Levine J.F., Labow M.A.; RT "Cytokine induction of an alternatively spliced murine vascular cell RT adhesion molecule (VCAM) mRNA encoding a glycosylphosphatidylinositol- RT anchored VCAM protein."; RL Proc. Natl. Acad. Sci. U.S.A. 90:5919-5923(1993). RN [8] RP NUCLEOTIDE SEQUENCE OF 1-21. RC TISSUE=Endothelial cell; RA Korenaga R., Ando J., Tsuboi H., Kamiya A.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. RN [9] RP INTERACTION WITH ECMV-D CAPSID PROTEINS (MICROBIAL INFECTION). RX PubMed=7514674; DOI=10.1128/jvi.68.6.3453-3458.1994; RA Huber S.A.; RT "VCAM-1 is a receptor for encephalomyocarditis virus on murine vascular RT endothelial cells."; RL J. Virol. 68:3453-3458(1994). RN [10] RP PROTEIN SEQUENCE OF 27-32, AND TISSUE SPECIFICITY. RX PubMed=1713592; DOI=10.1083/jcb.114.3.557; RA Miyake K., Medina K., Ishihara K., Kimoto M., Auerbach R., Kincade P.W.; RT "A VCAM-like adhesion molecule on murine bone marrow stromal cells mediates RT binding of lymphocyte precursors in culture."; RL J. Cell Biol. 114:557-565(1991). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225; ASN-273 AND ASN-561. RC TISSUE=Myoblast; RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200; RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.; RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome: RT identification, glycosite occupancy, and membrane orientation."; RL Mol. Cell. Proteomics 8:2555-2569(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, 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: Cell adhesion glycoprotein predominantly expressed on the CC surface of endothelial cells that plays an important role in immune CC surveillance and inflammation. Acts as a major regulator of leukocyte CC adhesion to the endothelium through interaction with different types of CC integrins. During inflammatory responses, binds ligands on the surface CC of activated endothelial cells to initiate the activation of calcium CC channels and the plasma membrane-associated small GTPase RAC1 leading CC to leukocyte transendothelial migration. Also serves as a quality- CC control checkpoint for entry into bone marrow by providing a 'don't- CC eat-me' stamping in the context of major histocompatibility complex CC (MHC) class-I presentation. {ECO:0000250|UniProtKB:P19320}. CC -!- SUBUNIT: (Microbial infection) Interacts with ECMV-D capsid proteins CC and acts as a receptor for this virus. {ECO:0000269|PubMed:7514674}. CC -!- SUBCELLULAR LOCATION: [Vascular cell adhesion protein 1]: Cell membrane CC {ECO:0000250|UniProtKB:P19320}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:P19320}. CC -!- SUBCELLULAR LOCATION: [Soluble Vascular Cell Adhesion Molecule-1]: CC Secreted {ECO:0000250|UniProtKB:P19320}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long; CC IsoId=P29533-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=P29533-2; Sequence=VSP_002581, VSP_002582; CC -!- TISSUE SPECIFICITY: Expressed on inflamed vascular endothelium, as well CC as on macrophage-like and dendritic cell types in both normal and CC inflamed tissue. Expressed in the bone marrow. CC {ECO:0000269|PubMed:1713592}. CC -!- PTM: Cleaved by the metalloproteinase ADAM17 to generate the soluble CC form. {ECO:0000250|UniProtKB:P19320}. CC -!- PTM: Sialoglycoprotein. {ECO:0000250|UniProtKB:P19320}. CC -!- PTM: Ubiquitinated by TRIM65 via 'Lys-48'-linked ubiquitination; CC leading to proteasomal degradation. {ECO:0000250|UniProtKB:P19320}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=VCAM-1; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_192"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M84487; AAA40545.1; -; mRNA. DR EMBL; X67783; CAA47989.1; -; mRNA. DR EMBL; L22355; AAA16921.1; -; Genomic_DNA. DR EMBL; L22301; AAA16921.1; JOINED; Genomic_DNA. DR EMBL; L22349; AAA16921.1; JOINED; Genomic_DNA. DR EMBL; L22350; AAA16921.1; JOINED; Genomic_DNA. DR EMBL; L22351; AAA16921.1; JOINED; Genomic_DNA. DR EMBL; L22352; AAA16921.1; JOINED; Genomic_DNA. DR EMBL; L22353; AAA16921.1; JOINED; Genomic_DNA. DR EMBL; L22354; AAA16921.1; JOINED; Genomic_DNA. DR EMBL; L22350; AAA16920.1; -; Genomic_DNA. DR EMBL; L22301; AAA16920.1; JOINED; Genomic_DNA. DR EMBL; L22349; AAA16920.1; JOINED; Genomic_DNA. DR EMBL; U12878; AAB60659.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12879; AAB60660.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12880; AAB60661.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12874; AAB60662.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12871; AAB60663.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12883; AAB60664.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12881; AAA80010.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12882; AAA80011.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12875; AAA80012.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12872; AAA80013.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12876; AAA80014.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12873; AAA80015.1; ALT_SEQ; Genomic_DNA. DR EMBL; U12877; AAA80016.1; ALT_SEQ; Genomic_DNA. DR EMBL; L08431; AAA40546.1; -; mRNA. DR EMBL; U12884; AAA64832.1; -; mRNA. DR EMBL; L12541; AAC37607.1; -; mRNA. DR EMBL; U42327; AAB88576.1; -; Genomic_DNA. DR CCDS; CCDS17785.1; -. [P29533-1] DR PIR; B48919; A46052. DR PIR; JN0581; JN0581. DR AlphaFoldDB; P29533; -. DR BioGRID; 204505; 4. DR CORUM; P29533; -. DR DIP; DIP-29097N; -. DR FunCoup; P29533; 583. DR IntAct; P29533; 1. DR STRING; 10090.ENSMUSP00000029574; -. DR GlyConnect; P29533; 6 N-Linked glycans (2 sites). DR GlyCosmos; P29533; 5 sites, 6 glycans. DR GlyGen; P29533; 5 sites, 10 N-linked glycans (4 sites). DR iPTMnet; P29533; -. DR PhosphoSitePlus; P29533; -. DR SwissPalm; P29533; -. DR CPTAC; non-CPTAC-3397; -. DR PaxDb; 10090-ENSMUSP00000029574; -. DR PeptideAtlas; P29533; -. DR ProteomicsDB; 275174; -. [P29533-1] DR ProteomicsDB; 275175; -. [P29533-2] DR Pumba; P29533; -. DR ABCD; P29533; 4 sequenced antibodies. DR Antibodypedia; 3955; 2255 antibodies from 55 providers. DR Ensembl; ENSMUST00000196449.5; ENSMUSP00000142876.2; ENSMUSG00000027962.15. [P29533-2] DR AGR; MGI:98926; -. DR MGI; MGI:98926; Vcam1. DR VEuPathDB; HostDB:ENSMUSG00000027962; -. DR eggNOG; ENOG502QSKQ; Eukaryota. DR GeneTree; ENSGT00940000156511; -. DR InParanoid; P29533; -. DR PhylomeDB; P29533; -. 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 PRO; PR:P29533; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P29533; protein. DR Bgee; ENSMUSG00000027962; Expressed in stroma of bone marrow and 250 other cell types or tissues. DR ExpressionAtlas; P29533; baseline and differential. DR GO; GO:0071065; C:alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex; ISO:GO_Central. DR GO; GO:0045177; C:apical part of cell; ISO:GO_Central. DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI. DR GO; GO:0071944; C:cell periphery; IDA:MGI. DR GO; GO:0009986; C:cell surface; ISO:GO_Central. DR GO; GO:0005769; C:early endosome; ISO:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:GO_Central. DR GO; GO:0009897; C:external side of plasma membrane; ISO:GO_Central. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0030175; C:filopodium; ISO:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; ISO:GO_Central. DR GO; GO:0005902; C:microvillus; ISO:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0002102; C:podosome; ISO:GO_Central. DR GO; GO:0042383; C:sarcolemma; ISO:GO_Central. DR GO; GO:0098631; F:cell adhesion mediator activity; ISO:GO_Central. DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:GO_Central. DR GO; GO:0005178; F:integrin binding; ISO:GO_Central. DR GO; GO:0008131; F:primary methylamine oxidase activity; ISO:GO_Central. DR GO; GO:0009308; P:amine metabolic process; ISO:GO_Central. DR GO; GO:0060945; P:cardiac neuron differentiation; ISO:GO_Central. DR GO; GO:0007155; P:cell adhesion; IDA:MGI. DR GO; GO:0060326; P:cell chemotaxis; ISO:GO_Central. DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; ISO:GO_Central. DR GO; GO:0007160; P:cell-matrix adhesion; ISO:GO_Central. DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:GO_Central. DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:MGI. DR GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI. DR GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0007157; P:heterophilic cell-cell adhesion; IMP:MGI. DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:GO_Central. DR GO; GO:0006954; P:inflammatory response; ISO:GO_Central. DR GO; GO:0060384; P:innervation; ISO:GO_Central. DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI. DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:GO_Central. DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:GO_Central. DR GO; GO:0061032; P:visceral serous pericardium development; TAS:DFLAT. DR CDD; cd07689; IgC2_VCAM-1; 1. DR CDD; cd20943; IgI_VCAM-1; 1. DR FunFam; 2.60.40.10:FF:000625; Vascular cell adhesion molecule 1; 2. DR FunFam; 2.60.40.10:FF:000671; Vascular cell adhesion molecule 1; 2. DR FunFam; 2.60.40.10:FF:000782; Vascular cell adhesion molecule 1; 2. DR FunFam; 2.60.40.10:FF:000817; Vascular cell adhesion molecule 1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 7. 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; IPR008424; Ig_C2-set. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR003989; VCAM-1. DR PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1. DR PANTHER; PTHR13771:SF14; VASCULAR CELL ADHESION PROTEIN 1; 1. DR Pfam; PF05790; C2-set; 2. DR Pfam; PF07679; I-set; 2. DR Pfam; PF13927; Ig_3; 3. DR PRINTS; PR01472; ICAMVCAM1. DR PRINTS; PR01474; VCAM1. DR SMART; SM00409; IG; 5. DR SMART; SM00408; IGc2; 5. DR SUPFAM; SSF48726; Immunoglobulin; 7. DR PROSITE; PS50835; IG_LIKE; 5. PE 1: Evidence at protein level; KW Alternative splicing; Cell adhesion; Cell membrane; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Host-virus interaction; Immunoglobulin domain; Membrane; KW Reference proteome; Repeat; Secreted; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1..24 FT /evidence="ECO:0000305" FT CHAIN 25..739 FT /note="Vascular cell adhesion protein 1" FT /id="PRO_0000014998" FT CHAIN 25..? FT /note="Soluble Vascular Cell Adhesion Molecule-1" FT /id="PRO_0000457763" FT TOPO_DOM 25..698 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 699..720 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 721..739 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 25..111 FT /note="Ig-like C2-type 1" FT DOMAIN 119..212 FT /note="Ig-like C2-type 2" FT DOMAIN 223..309 FT /note="Ig-like C2-type 3" FT DOMAIN 312..393 FT /note="Ig-like C2-type 4" FT DOMAIN 408..506 FT /note="Ig-like C2-type 5" FT DOMAIN 511..595 FT /note="Ig-like C2-type 6" FT DOMAIN 600..682 FT /note="Ig-like C2-type 7" FT CARBOHYD 225 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19656770" FT CARBOHYD 273 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19656770" FT CARBOHYD 424 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 531 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 561 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19656770" FT DISULFID 47..95 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 52..99 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 137..195 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 246..291 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 335..383 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 534..579 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 310..345 FT /note="EKPFIVDISPGSQVAAQVGDSVVLTCAAIGCDSPSF -> DGRMKSQITNGH FT QLTVHLMFAKSFYFICYLCLYLAL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7523515, FT ECO:0000303|PubMed:7682556, ECO:0000303|PubMed:7687058" FT /id="VSP_002581" FT VAR_SEQ 346..739 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7523515, FT ECO:0000303|PubMed:7682556, ECO:0000303|PubMed:7687058" FT /id="VSP_002582" FT CONFLICT 693 FT /note="D -> N (in Ref. 3; AAA16921)" FT /evidence="ECO:0000305" FT LIPID P29533-2:319 FT /note="GPI-anchor amidated asparagine" FT /evidence="ECO:0000303|PubMed:7687058" SQ SEQUENCE 739 AA; 81317 MW; 3D2134C341E5E449 CRC64; MPVKMVAVLG ASTVLWILFA VSQAFKIEIS PEYKTIAQIG DSMALTCSTT GCESPLFSWR TQIDSPLNAK VRTEGSKSVL TMEPVSFENE HSYLCTATCG SGKLERSIHV DIYSFPKDPE IQFSGPLEVG KPVTVKCLAP DIYPVYRLEI DLFKGDQLMN RQEFSSEEMT KSLETKSLEV TFTPVIEDIG KALVCRAKLH IDQIDSTLKE RETVKELQVY ISPRNTTISV HPSTRLQEGG AVTMTCSSEG LPAPEIFWGR KLDNEVLQLL SGNATLTLIA MRMEDSGVYV CEGVNLIGRD KAEVELVVQE KPFIVDISPG SQVAAQVGDS VVLTCAAIGC DSPSFSWRTQ TDSPLNGVVR NEGAKSTLVL SSVGFEDEHS YLCAVTCLQR TLEKRTQVEV YSFPEDPVIK MSGPLVHGRP VTVNCTVPNV YPFDHLEIEL LKGETTLMKK YFLEEMGIKS LETKILETTF IPTIEDTGKS LVCLARLHSG EMESEPKQRQ SVQPLYVNVA PKETTIWVSP SPILEEGSPV NLTCSSDGIP APKILWSRQL NNGELQPLSE NTTLTFMSTK RDDSGIYVCE GINEAGISRK SVELIIQVSP KDIQLTVFPS KSVKEGDTVI ISCTCGNVPE TWIILKKKAK TGDMVLKSVD GSYTIRQAQL QDAGIYECES KTEVGSQLRS LTLDVKGKEH NKDYFSPELL ALYCASSLVI PAIGMIVYFA RKANMKGSYS LVEAQKSKV //