GENTAUR Molecular Products.

 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}.
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution-NoDerivs License
 -----------------------------------------------------------------------
 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

Related products :