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Vascular cell adhesion protein 1 (V-CAM 1) (VCAM-1) (CD antigen CD106)

 VCAM1_MOUSE             Reviewed;         739 AA.
P29533;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
30-AUG-2017, entry version 162.
RecName: Full=Vascular cell adhesion protein 1;
Short=V-CAM 1;
Short=VCAM-1;
AltName: CD_antigen=CD106;
Flags: Precursor;
Name=Vcam1; Synonyms=Vcam-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=FVB/NJ; TISSUE=Lung;
PubMed=1371918; DOI=10.1016/0006-291X(92)91623-X;
Hession C., Moy P., Tizard R., Chisholm P., Williams C., Wysk M.,
Burkly L., Miyake K., Kincade P., Lobb R.;
"Cloning of murine and rat vascular cell adhesion molecule-1.";
Biochem. Biophys. Res. Commun. 183:163-169(1992).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
TISSUE=Lymph node;
PubMed=7683304; DOI=10.1016/0378-1119(93)90377-F;
Araki M., Araki K., Vassalli P.;
"Cloning and sequencing of mouse VCAM-1 cDNA.";
Gene 126:261-264(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
STRAIN=129; TISSUE=Embryo;
PubMed=7507076; DOI=10.1006/geno.1993.1480;
Cybulsky M.I., Allan-Motamed M., Collins T.;
"Structure of the murine VCAM1 gene.";
Genomics 18:387-391(1993).
[4]
NUCLEOTIDE SEQUENCE OF 1-693 (ISOFORM 1).
STRAIN=129/Sv, and NIH Swiss;
Kumar A.G., Dai Y.X., Kozak C.A., Mims M.P., Gotto A.M. Jr.,
Ballantyne C.M.;
Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=FVB/NJ; TISSUE=Lung;
PubMed=7682556;
Moy P., Lobb R., Tizard R., Olson D., Hession C.;
"Cloning of an inflammation-specific phosphatidyl inositol-linked form
of murine vascular cell adhesion molecule-1.";
J. Biol. Chem. 268:8835-8841(1993).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=7523515;
Kumar A.G., Dai X.Y., Kozak C.A., Mims M.P., Gotto A.M. Jr.,
Ballantyne C.M.;
"Murine VCAM-1. Molecular cloning, mapping, and analysis of a
truncated form.";
J. Immunol. 153:4088-4098(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 311-345 (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=7687058; DOI=10.1073/pnas.90.13.5919;
Terry R.W., Kwee L., Levine J.F., Labow M.A.;
"Cytokine induction of an alternatively spliced murine vascular cell
adhesion molecule (VCAM) mRNA encoding a glycosylphosphatidylinositol-
anchored VCAM protein.";
Proc. Natl. Acad. Sci. U.S.A. 90:5919-5923(1993).
[8]
NUCLEOTIDE SEQUENCE OF 1-21.
TISSUE=Endothelial cell;
Korenaga R., Ando J., Tsuboi H., Kamiya A.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[9]
INTERACTION WITH ECMV-D CAPSID PROTEINS.
PubMed=7514674;
Huber S.A.;
"VCAM-1 is a receptor for encephalomyocarditis virus on murine
vascular endothelial cells.";
J. Virol. 68:3453-3458(1994).
[10]
PROTEIN SEQUENCE OF 27-32, AND TISSUE SPECIFICITY.
PubMed=1713592; DOI=10.1083/jcb.114.3.557;
Miyake K., Medina K., Ishihara K., Kimoto M., Auerbach R.,
Kincade P.W.;
"A VCAM-like adhesion molecule on murine bone marrow stromal cells
mediates binding of lymphocyte precursors in culture.";
J. Cell Biol. 114:557-565(1991).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225; ASN-264; ASN-273;
ASN-552 AND ASN-561.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Important in cell-cell recognition. Appears to function
in leukocyte-endothelial cell adhesion. Interacts with integrin
alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both
adhesion and signal transduction. The VCAM1/ITGA4/ITGB1
interaction may play a pathophysiologic role both in immune
responses and in leukocyte emigration to sites of inflammation.
-!- SUBUNIT: Binds to ECMV-D capsid proteins and acts as a receptor
for this virus.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Lipid-anchor, GPI-
anchor.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=P29533-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P29533-2; Sequence=VSP_002581, VSP_002582;
Note=Contains a GPI-anchor amidated asparagine at position 319.;
-!- TISSUE SPECIFICITY: Expressed on inflamed vascular endothelium, as
well as on macrophage-like and dendritic cell types in both normal
and inflamed tissue. Expressed in the bone marrow.
{ECO:0000269|PubMed:1713592}.
-!- PTM: The GPI-anchor is located on position 319 of isoform 2.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=VCAM-1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_192";
-----------------------------------------------------------------------
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EMBL; M84487; AAA40545.1; -; mRNA.
EMBL; X67783; CAA47989.1; -; mRNA.
EMBL; L22355; AAA16921.1; -; Genomic_DNA.
EMBL; L22301; AAA16921.1; JOINED; Genomic_DNA.
EMBL; L22349; AAA16921.1; JOINED; Genomic_DNA.
EMBL; L22350; AAA16921.1; JOINED; Genomic_DNA.
EMBL; L22351; AAA16921.1; JOINED; Genomic_DNA.
EMBL; L22352; AAA16921.1; JOINED; Genomic_DNA.
EMBL; L22353; AAA16921.1; JOINED; Genomic_DNA.
EMBL; L22354; AAA16921.1; JOINED; Genomic_DNA.
EMBL; L22350; AAA16920.1; -; Genomic_DNA.
EMBL; L22301; AAA16920.1; JOINED; Genomic_DNA.
EMBL; L22349; AAA16920.1; JOINED; Genomic_DNA.
EMBL; U12878; AAB60659.1; ALT_SEQ; Genomic_DNA.
EMBL; U12879; AAB60660.1; ALT_SEQ; Genomic_DNA.
EMBL; U12880; AAB60661.1; ALT_SEQ; Genomic_DNA.
EMBL; U12874; AAB60662.1; ALT_SEQ; Genomic_DNA.
EMBL; U12871; AAB60663.1; ALT_SEQ; Genomic_DNA.
EMBL; U12883; AAB60664.1; ALT_SEQ; Genomic_DNA.
EMBL; U12881; AAA80010.1; ALT_SEQ; Genomic_DNA.
EMBL; U12882; AAA80011.1; ALT_SEQ; Genomic_DNA.
EMBL; U12875; AAA80012.1; ALT_SEQ; Genomic_DNA.
EMBL; U12872; AAA80013.1; ALT_SEQ; Genomic_DNA.
EMBL; U12876; AAA80014.1; ALT_SEQ; Genomic_DNA.
EMBL; U12873; AAA80015.1; ALT_SEQ; Genomic_DNA.
EMBL; U12877; AAA80016.1; ALT_SEQ; Genomic_DNA.
EMBL; L08431; AAA40546.1; -; mRNA.
EMBL; U12884; AAA64832.1; -; mRNA.
EMBL; L12541; AAC37607.1; -; mRNA.
EMBL; U42327; AAB88576.1; -; Genomic_DNA.
CCDS; CCDS17785.1; -. [P29533-1]
PIR; B48919; A46052.
PIR; JN0581; JN0581.
UniGene; Mm.440909; -.
UniGene; Mm.76649; -.
ProteinModelPortal; P29533; -.
DIP; DIP-29097N; -.
IntAct; P29533; 1.
MINT; MINT-4139873; -.
STRING; 10090.ENSMUSP00000029574; -.
iPTMnet; P29533; -.
PhosphoSitePlus; P29533; -.
MaxQB; P29533; -.
PaxDb; P29533; -.
PeptideAtlas; P29533; -.
PRIDE; P29533; -.
Ensembl; ENSMUST00000196449; ENSMUSP00000142876; ENSMUSG00000027962. [P29533-2]
MGI; MGI:98926; Vcam1.
eggNOG; ENOG410IIKS; Eukaryota.
eggNOG; ENOG4111F4V; LUCA.
GeneTree; ENSGT00830000128299; -.
HOGENOM; HOG000004820; -.
HOVERGEN; HBG053965; -.
InParanoid; P29533; -.
PhylomeDB; P29533; -.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-216083; Integrin cell surface interactions.
PRO; PR:P29533; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027962; -.
CleanEx; MM_VCAM1; -.
ExpressionAtlas; P29533; baseline and differential.
GO; GO:0071065; C:alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex; ISO:MGI.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0045177; C:apical part of cell; ISO:MGI.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0030175; C:filopodium; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005902; C:microvillus; ISO:MGI.
GO; GO:0002102; C:podosome; ISO:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0008131; F:primary amine oxidase activity; ISO:MGI.
GO; GO:0009308; P:amine metabolic process; ISO:MGI.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:MGI.
GO; GO:0007155; P:cell adhesion; IDA:MGI.
GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
GO; GO:0071333; P:cellular response to glucose stimulus; IDA:MGI.
GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI.
GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:MGI.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0061032; P:visceral serous pericardium development; TAS:DFLAT.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR003987; ICAM_VCAM_N.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR008424; Ig_C2-set.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR003989; VCAM-1.
Pfam; PF05790; C2-set; 2.
Pfam; PF07679; I-set; 3.
Pfam; PF00047; ig; 1.
PRINTS; PR01472; ICAMVCAM1.
PRINTS; PR01474; VCAM1.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 5.
SUPFAM; SSF48726; SSF48726; 7.
PROSITE; PS50835; IG_LIKE; 5.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
Host-virus interaction; Immunoglobulin domain; Lipoprotein; Membrane;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24 {ECO:0000305}.
CHAIN 25 739 Vascular cell adhesion protein 1.
/FTId=PRO_0000014998.
TOPO_DOM 25 698 Extracellular. {ECO:0000255}.
TRANSMEM 699 720 Helical. {ECO:0000255}.
TOPO_DOM 721 739 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 111 Ig-like C2-type 1.
DOMAIN 119 212 Ig-like C2-type 2.
DOMAIN 223 309 Ig-like C2-type 3.
DOMAIN 312 393 Ig-like C2-type 4.
DOMAIN 408 506 Ig-like C2-type 5.
DOMAIN 511 595 Ig-like C2-type 6.
DOMAIN 600 682 Ig-like C2-type 7.
CARBOHYD 225 225 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19656770}.
CARBOHYD 273 273 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 424 424 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 531 531 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 552 552 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19656770}.
CARBOHYD 561 561 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
DISULFID 47 95 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 52 99 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 137 195 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 246 291 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 335 383 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 534 579 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 310 345 EKPFIVDISPGSQVAAQVGDSVVLTCAAIGCDSPSF -> D
GRMKSQITNGHQLTVHLMFAKSFYFICYLCLYLAL (in
isoform 2). {ECO:0000303|PubMed:7523515,
ECO:0000303|PubMed:7682556,
ECO:0000303|PubMed:7687058}.
/FTId=VSP_002581.
VAR_SEQ 346 739 Missing (in isoform 2).
{ECO:0000303|PubMed:7523515,
ECO:0000303|PubMed:7682556,
ECO:0000303|PubMed:7687058}.
/FTId=VSP_002582.
CONFLICT 693 693 D -> N (in Ref. 3; AAA16921).
{ECO:0000305}.
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


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