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Vasodilator-stimulated phosphoprotein

 A0A0G2K9C0_RAT          Unreviewed;       375 AA.
A0A0G2K9C0;
22-JUL-2015, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 1.
28-MAR-2018, entry version 22.
SubName: Full=Vasodilator-stimulated phosphoprotein {ECO:0000313|Ensembl:ENSRNOP00000074940};
Name=Vasp {ECO:0000313|Ensembl:ENSRNOP00000074940,
ECO:0000313|RGD:1311542};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000074940, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000074940, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000074940,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000213|PubMed:22673903}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[3] {ECO:0000313|Ensembl:ENSRNOP00000074940}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000074940};
Ensembl;
Submitted (JUN-2015) to UniProtKB.
-!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved
in a range of processes dependent on cytoskeleton remodeling and
cell polarity such as axon guidance, lamellipodial and filopodial
dynamics, platelet activation and cell migration.
{ECO:0000256|PIRNR:PIRNR038010}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000256|PIRNR:PIRNR038010}.
-!- SIMILARITY: Belongs to the Ena/VASP family.
{ECO:0000256|PIRNR:PIRNR038010}.
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EMBL; AABR07002673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07002674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
STRING; 10116.ENSRNOP00000022214; -.
PaxDb; A0A0G2K9C0; -.
Ensembl; ENSRNOT00000088676; ENSRNOP00000074940; ENSRNOG00000016367.
RGD; 1311542; Vasp.
GeneTree; ENSGT00730000110272; -.
OMA; MSETVIC; -.
Reactome; R-RNO-376176; Signaling by ROBO receptors.
Reactome; R-RNO-446353; Cell-extracellular matrix interactions.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000016367; -.
ExpressionAtlas; A0A0G2K9C0; baseline and differential.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0030175; C:filopodium; ISO:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0030027; C:lamellipodium; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; ISO:RGD.
GO; GO:0005522; F:profilin binding; ISO:RGD.
GO; GO:0017124; F:SH3 domain binding; IEA:InterPro.
GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
GO; GO:0008154; P:actin polymerization or depolymerization; IEA:UniProtKB-UniRule.
GO; GO:0007411; P:axon guidance; ISO:RGD.
GO; GO:0001843; P:neural tube closure; ISO:RGD.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR034367; VASP.
InterPro; IPR017354; VASP/EVL.
InterPro; IPR038023; VASP_sf.
InterPro; IPR014885; VASP_tetra.
InterPro; IPR000697; WH1/EVH1_dom.
PANTHER; PTHR11202:SF12; PTHR11202:SF12; 1.
Pfam; PF08776; VASP_tetra; 1.
Pfam; PF00568; WH1; 1.
PIRSF; PIRSF038010; Vasodilator_Phospo; 1.
SMART; SM00461; WH1; 1.
SUPFAM; SSF118370; SSF118370; 1.
PROSITE; PS50229; WH1; 1.
1: Evidence at protein level;
Actin-binding {ECO:0000256|PIRNR:PIRNR038010};
Cell projection {ECO:0000256|PIRNR:PIRNR038010};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Cytoplasm {ECO:0000256|PIRNR:PIRNR038010};
Cytoskeleton {ECO:0000256|PIRNR:PIRNR038010};
Proteomics identification {ECO:0000213|PeptideAtlas:A0A0G2K9C0};
Reference proteome {ECO:0000313|Proteomes:UP000002494}.
DOMAIN 1 113 WH1. {ECO:0000259|PROSITE:PS50229}.
COILED 340 367 {ECO:0000256|SAM:Coils}.
SEQUENCE 375 AA; 39578 MW; 96C10FB18722D3D7 CRC64;
SNETVICSSR ATVMLYDDSN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKLQPDQQV
VINCAIIRGV KYNQATPIFH QWRDARQVWG LNFGSKEDAA QFAIGMANAL EALEGGGPPP
APAPPAWSTQ NGPSPEELEQ QKRQPEHLER RVSNAGGPPA PPAGGPPPPP GPPPPPGPPP
PPGLPPSGVS GAGHGTGVAP PPAPPLPTAQ GPSSGGSGAP GLAAAIAGAK LRKVSKEEAS
GGPLAPKAEN SRGTGGGLME EMNAMLARRR KATQVGEKPP KDESASQEES EARIPAQSEP
VRRPWEKNTT TLPQMKSSSS VTTSEAHPSV PSSSDDSDLE RVKQELVEEV RKELQKMKEE
IIEVFVQELR KRGSP


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