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Vasodilator-stimulated phosphoprotein
F7EWC1_RAT Unreviewed; 374 AA.
F7EWC1;
03-APR-2013, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 2.
28-MAR-2018, entry version 37.
SubName: Full=Vasodilator-stimulated phosphoprotein {ECO:0000313|Ensembl:ENSRNOP00000022214};
Name=Vasp {ECO:0000313|Ensembl:ENSRNOP00000022214,
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:ENSRNOP00000022214, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000022214, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000022214,
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:ENSRNOP00000022214}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000022214};
Ensembl;
Submitted (FEB-2012) 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.
Ensembl; ENSRNOT00000022214; ENSRNOP00000022214; ENSRNOG00000016367.
RGD; 1311542; Vasp.
eggNOG; KOG4590; Eukaryota.
eggNOG; ENOG41101TS; LUCA.
GeneTree; ENSGT00730000110272; -.
HOVERGEN; HBG006655; -.
InParanoid; F7EWC1; -.
Reactome; R-RNO-376176; Signaling by ROBO receptors.
Reactome; R-RNO-446353; Cell-extracellular matrix interactions.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000016367; -.
ExpressionAtlas; F7EWC1; baseline and differential.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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: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:F7EWC1};
Reference proteome {ECO:0000313|Proteomes:UP000002494}.
DOMAIN 1 114 WH1. {ECO:0000259|PROSITE:PS50229}.
COILED 339 366 {ECO:0000256|SAM:Coils}.
SEQUENCE 374 AA; 39485 MW; 88B0469DD21338EF CRC64;
MSNETVICSS RATVMLYDDS NKRWLPAGTG PQAFSRVQIY HNPTANSFRV VGRKLQPDQQ
VVINCAIIRG VKYNQATPIF HQWRDARQVW GLNFGSKEDA AQFAIGMANA LEALEGGGPP
PAPAPPAWST QNGPSPEELE QQKRQPEHLE RRVSNAGGPP APPAGGPPPP PGPPPPPGPP
PPPGLPPSGV SGAGHGTGVA PPPAPPLPTA QGPSSGGSGA PGLAAAIAGA KLRKVSKEEA
SGGPLAPKAE NSRGTGGGLM EEMNAMLARR RKATQVGEKP PKDESASQEE SEARIPAQSE
PVRRPWEKNS SSRMKSSSSV TTSEAHPSVP SSSDDSDLER VKQELVEEVR KELQKMKEEI
IEVFVQELRK RGSP
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[VASP] Vasodilator-stimulated phosphoprotein (VASP)
[Vasp] Vasodilator-stimulated phosphoprotein (VASP)
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[Evl] Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like)
[VASP] Vasodilator-stimulated phosphoprotein (VASP)
[VASP] Vasodilator-stimulated phosphoprotein (VASP)
[Evl Rnb6] Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like)
[EVL] Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like)
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[hppA TM_0174] K(+)-stimulated pyrophosphate-energized sodium pump (EC 3.6.1.1) (Membrane-bound sodium-translocating pyrophosphatase) (Pyrophosphate-energized inorganic pyrophosphatase) (Na(+)-PPase) (Tm-PPase)
[RPS6KA3 ISPK1 MAPKAPK1B RSK2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (Insulin-stimulated protein kinase 1) (ISPK-1) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)
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[ASNA1 ARSA TRC40] ATPase ASNA1 (EC 3.6.-.-) (Arsenical pump-driving ATPase) (Arsenite-stimulated ATPase) (Transmembrane domain recognition complex 40 kDa ATPase subunit) (hARSA-I) (hASNA-I)
[Mapk3 Erk1 Prkm3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (MNK1) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[PDE2A] cGMP-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) (Cyclic GMP-stimulated phosphodiesterase) (CGS-PDE) (cGSPDE)
[Pde2a] cGMP-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) (Cyclic GMP-stimulated phosphodiesterase) (CGS-PDE) (cGSPDE)
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[Stra8] Stimulated by retinoic acid gene 8 protein
[evl] Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like)
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