VCAM1_RAT
ID VCAM1_RAT Reviewed; 739 AA.
AC P29534; Q5FVS3; Q63669;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC 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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=1377031; DOI=10.1016/0167-4781(92)90081-a;
RA Williams A.J., Atkins R.C., Fries J.W.U., Gimbrone M.A. Jr., Cybulsky M.I.,
RA Collins T.;
RT "Nucleotide sequence of rat vascular cell adhesion molecule-1 cDNA.";
RL Biochim. Biophys. Acta 1131:214-216(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=28167758; DOI=10.1073/pnas.1621425114;
RA Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L., Shih Y.T.,
RA Chien S., Chiu J.J.;
RT "MicroRNA-10a is crucial for endothelial response to different flow
RT patterns via interaction of retinoid acid receptors and histone
RT deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
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: Binds to ECMV-D capsid proteins and acts as a receptor for
CC this virus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in aortic endothelial cells, with low
CC expression in the descending thoracic aorta and the outer curvature of
CC the aortic arch, where pulsatory shear stress exists, and high in the
CC inner curvature of the aortic arch, where oscillatory shear stress
CC prevails (at protein level) (PubMed:28167758). Expressed on inflamed
CC vascular endothelium, as well as on macrophage-like and dendritic cell
CC types in both normal and inflamed tissue (PubMed:1371918).
CC {ECO:0000269|PubMed:28167758, ECO:0000303|PubMed:1371918}.
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DR EMBL; M84488; AAA42332.1; -; mRNA.
DR EMBL; X63722; CAA45254.1; -; mRNA.
DR EMBL; BC089812; AAH89812.1; -; mRNA.
DR PIR; JS0675; JS0675.
DR RefSeq; NP_037021.1; NM_012889.1.
DR AlphaFoldDB; P29534; -.
DR STRING; 10116.ENSRNOP00000019377; -.
DR CarbonylDB; P29534; -.
DR GlyGen; P29534; 5 sites.
DR PhosphoSitePlus; P29534; -.
DR PaxDb; P29534; -.
DR PRIDE; P29534; -.
DR Ensembl; ENSRNOT00000078806; ENSRNOP00000071423; ENSRNOG00000014333.
DR GeneID; 25361; -.
DR KEGG; rno:25361; -.
DR UCSC; RGD:3952; rat.
DR CTD; 7412; -.
DR RGD; 3952; Vcam1.
DR eggNOG; ENOG502QSKQ; Eukaryota.
DR GeneTree; ENSGT00940000156511; -.
DR InParanoid; P29534; -.
DR OMA; TYVCEGV; -.
DR OrthoDB; 544376at2759; -.
DR PhylomeDB; P29534; -.
DR TreeFam; TF333571; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR PRO; PR:P29534; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000014333; Expressed in spleen and 19 other tissues.
DR ExpressionAtlas; P29534; baseline and differential.
DR Genevisible; P29534; RN.
DR GO; GO:0071065; C:alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex; ISO:RGD.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0002102; C:podosome; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; IMP:RGD.
DR GO; GO:0008131; F:primary amine oxidase activity; ISO:RGD.
DR GO; GO:0002526; P:acute inflammatory response; IEP:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0009308; P:amine metabolic process; ISO:RGD.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:RGD.
DR GO; GO:0060945; P:cardiac neuron differentiation; IMP:RGD.
DR GO; GO:0007155; P:cell adhesion; IMP:RGD.
DR GO; GO:0060326; P:cell chemotaxis; IMP:RGD.
DR GO; GO:0140039; P:cell-cell adhesion in response to extracellular stimulus; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEP:RGD.
DR GO; GO:0060710; P:chorio-allantoic fusion; ISO:RGD.
DR GO; GO:0002544; P:chronic inflammatory response; IEP:RGD.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0060384; P:innervation; IMP:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
DR GO; GO:0022614; P:membrane to membrane docking; ISO:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
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; 6.
DR Pfam; PF05790; C2-set; 2.
DR Pfam; PF07679; I-set; 2.
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 Cell adhesion; Disulfide bond; Glycoprotein; Host-virus interaction;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW 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_0000014999"
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..397
FT /note="Ig-like C2-type 4"
FT DOMAIN 408..506
FT /note="Ig-like C2-type 5"
FT DOMAIN 514..595
FT /note="Ig-like C2-type 6"
FT DOMAIN 601..682
FT /note="Ig-like C2-type 7"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 CONFLICT 3
FT /note="V -> G (in Ref. 2; CAA45254)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..123
FT /note="QF -> HL (in Ref. 2; CAA45254)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="D -> N (in Ref. 2; CAA45254)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="V -> G (in Ref. 2; CAA45254)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 81246 MW; 5C608E5A1A1B100C CRC64;
MPVKMVAIFG ASTVLWILFA VSQAFKIEIS PEYKTLAQIG DSMLLTCSTT GCESPSFSWR
TQIDSPLNGK VKTEGAKSVL TMDPVSFENE HSYLCTATCN SGKLERGIQV DIYSFPKDPE
IQFSGPLEVG KPVMVKCLAP DVYPIDRLEI ELFKGDRLMK KQDFVDEMAK KSLETKSLEV
IFTPVIEDIE KALVCRAKLY IDQTDSIPKE RETVRELQVY TSPKNTEISV HPSTRLHEGA
AVTMTCASEG LPAPEIFWSK KLDNGVLQLL SGNATLTLIA MRMEDSGIYV CEGVNLVGRD
KTEVELIVQE KPFTVDISPG SQVAAQVGDS VVLTCAAVGC DSPSFSWRTQ TDSPLNGEVR
DEGATSTLTL SPVGVEDEHS YLCTVTCQRR KLEKTIQVEV YSFPEDPEIE ISGPLVHGRP
VTVNCTVPNV YPFDHLEIEL LKGETTLLNK FLREEIGTKS LETKSLEMTF IPTAEDTGKA
LVCLAKLHSS QMESEPKQRQ STQTLYVNVA PKEPTIWVSP SPVPEEGSPV NLTCSSDGFP
TPKILWSRQL KNGELQPLSQ NTTLSFMATK MEDSGIYVCE GINEAGISKK SVELIIQGSS
KDIQLTVFPS KSVKEGDTVI ISCTCGSVPE IWIILKKKAK TGDMVLKSVN GSYTIRKAQL
QDAGVYECES KTEVGSQLRS LTLDVKGKEN NKDYFSPELL ALYFASSLVI PAIGMIIYFA
RKANMKGSYS LVEAQKSKV
