VCAM1_MOUSE
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 03-AUG-2022, entry version 197.
DE RecName: Full=Vascular cell adhesion protein 1;
DE Short=V-CAM 1;
DE Short=VCAM-1;
DE AltName: CD_antigen=CD106;
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;
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: Important in cell-cell recognition. Appears to function in
CC leukocyte-endothelial cell adhesion. Interacts with integrin alpha-
CC 4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and
CC signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a
CC pathophysiologic role both in immune responses and in leukocyte
CC emigration to sites of inflammation.
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: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Lipid-anchor, GPI-
CC anchor.
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 -!- 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";
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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; 3.
DR DIP; DIP-29097N; -.
DR IntAct; P29533; 1.
DR STRING; 10090.ENSMUSP00000029574; -.
DR GlyConnect; 2815; 6 N-Linked glycans (2 sites).
DR GlyGen; P29533; 5 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; P29533; -.
DR PhosphoSitePlus; P29533; -.
DR CPTAC; non-CPTAC-3397; -.
DR MaxQB; P29533; -.
DR PaxDb; P29533; -.
DR PeptideAtlas; P29533; -.
DR PRIDE; P29533; -.
DR ProteomicsDB; 275174; -. [P29533-1]
DR ProteomicsDB; 275175; -. [P29533-2]
DR Antibodypedia; 3955; 2127 antibodies from 52 providers.
DR Ensembl; ENSMUST00000196449; ENSMUSP00000142876; ENSMUSG00000027962. [P29533-2]
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 ChiTaRS; Vcam1; mouse.
DR PRO; PR:P29533; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P29533; protein.
DR Bgee; ENSMUSG00000027962; Expressed in stroma of bone marrow and 249 other tissues.
DR ExpressionAtlas; P29533; baseline and differential.
DR GO; GO:0071065; C:alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex; ISO:MGI.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
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:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0002102; C:podosome; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0008131; F:primary amine oxidase activity; ISO:MGI.
DR GO; GO:0009308; P:amine metabolic process; ISO:MGI.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:MGI.
DR GO; GO:0060945; P:cardiac neuron differentiation; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0140039; P:cell-cell adhesion in response to extracellular stimulus; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix 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: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 via plasma membrane cell adhesion molecules; IMP:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0060384; P:innervation; ISO:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0061032; P:visceral serous pericardium development; TAS:DFLAT.
DR Gene3D; 2.60.40.10; -; 7.
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; IPR013151; Immunoglobulin.
DR InterPro; IPR003989; VCAM-1.
DR PANTHER; PTHR13771:SF14; PTHR13771:SF14; 5.
DR Pfam; PF05790; C2-set; 2.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 1.
DR PRINTS; PR01472; ICAMVCAM1.
DR PRINTS; PR01474; VCAM1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 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; GPI-anchor;
KW Host-virus interaction; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000305"
FT CHAIN 25..739
FT /note="Vascular cell adhesion protein 1"
FT /id="PRO_0000014998"
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
