EVL_RAT
ID EVL_RAT Reviewed; 420 AA.
AC O08719; A0A0G2K217;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ena/VASP-like protein;
DE AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like;
GN Name=Evl {ECO:0000312|RGD:621150}; Synonyms=Rnb6;
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] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=9268706; DOI=10.1006/bbrc.1997.7113;
RA Ohta S., Mineta T., Kimoto M., Tabuchi K.;
RT "Differential display cloning of a novel rat cDNA (RNB6) that shows high
RT expression in the neonatal brain revealed a member of Ena/VASP family.";
RL Biochem. Biophys. Res. Commun. 237:307-312(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-263; SER-308;
RP SER-335 AND SER-373, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a
CC range of processes dependent on cytoskeleton remodeling and cell
CC polarity such as axon guidance and lamellipodial and filopodial
CC dynamics in migrating cells. EVL enhances actin nucleation and
CC polymerization (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer (By similarity). Binds to the SH3 domains of
CC ABL1, LYN and SRC. Also binds to profilin, with preference for isoform
CC IIa of PFN2, and the WW domain of APBB1/FE65. Binds to SEMA6A.
CC Interacts, via the Pro-rich region, with the C-terminal SH3 domain of
CC DNMBP. Interacts with RAPH1. Binds, via the EVH1 domain, the Pro-rich
CC domain of Listeria monocytogenes actA (By similarity). Binds, via the
CC EVH1 domain, the Pro-rich domain of ZYX. Interacts with FYB1. Interacts
CC with ZDHHC17 (By similarity). {ECO:0000250|UniProtKB:P70429,
CC ECO:0000250|UniProtKB:Q9UI08}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P70429}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:P70429}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P70429}. Note=Targeted to the leading edge of
CC lamellipodia and the distal tip of stress fibers through interaction
CC with a number of proteins. In activated T-cells, localizes to the F-
CC actin collar and the distal tip of microspikes.
CC {ECO:0000250|UniProtKB:P70429}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O08719-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O08719-2; Sequence=VSP_059220, VSP_059221;
CC -!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
CC thymosin-like domain required for G-actin binding. The KLKR motif
CC within this block is essential for the G-actin binding and for actin
CC polymerization. Block B is required for F-actin binding and subcellular
CC location, and Block C for tetramerization.
CC -!- PTM: Phosphorylated by PKA; phosphorylation abolishes binding to SH3
CC domains of ABL and SRC. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
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DR EMBL; U70211; AAC53322.1; -; mRNA.
DR EMBL; AABR07065505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JC5614; JC5614.
DR RefSeq; NP_077061.1; NM_024147.1. [O08719-2]
DR RefSeq; XP_008763073.1; XM_008764851.2. [O08719-1]
DR RefSeq; XP_008763074.1; XM_008764852.2. [O08719-1]
DR AlphaFoldDB; O08719; -.
DR SMR; O08719; -.
DR BioGRID; 249400; 1.
DR IntAct; O08719; 2.
DR MINT; O08719; -.
DR STRING; 10116.ENSRNOP00000019584; -.
DR CarbonylDB; O08719; -.
DR iPTMnet; O08719; -.
DR PhosphoSitePlus; O08719; -.
DR PaxDb; O08719; -.
DR PRIDE; O08719; -.
DR GeneID; 79115; -.
DR KEGG; rno:79115; -.
DR UCSC; RGD:621150; rat. [O08719-1]
DR CTD; 51466; -.
DR RGD; 621150; Evl.
DR VEuPathDB; HostDB:ENSRNOG00000014476; -.
DR eggNOG; KOG4590; Eukaryota.
DR InParanoid; O08719; -.
DR OMA; RTHYGIN; -.
DR OrthoDB; 972128at2759; -.
DR PhylomeDB; O08719; -.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR PRO; PR:O08719; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000014476; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; O08719; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0008154; P:actin polymerization or depolymerization; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; NAS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0007417; P:central nervous system development; TAS:RGD.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR034319; ENA/VASP-like_protein.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR017354; VASP/EVL.
DR InterPro; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR11202:SF4; PTHR11202:SF4; 1.
DR Pfam; PF08776; VASP_tetra; 1.
DR Pfam; PF00568; WH1; 1.
DR PIRSF; PIRSF038010; Vasodilator_Phospo; 1.
DR SMART; SM00461; WH1; 1.
DR SUPFAM; SSF118370; SSF118370; 1.
DR PROSITE; PS50229; WH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; SH3-binding.
FT CHAIN 1..420
FT /note="Ena/VASP-like protein"
FT /id="PRO_0000087106"
FT DOMAIN 1..118
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 163..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..417
FT /note="EVH2"
FT REGION 226..246
FT /note="EVH2 block A"
FT REGION 269..286
FT /note="EVH2 block B"
FT REGION 346..366
FT /note="Required for interaction with ZDHHC17"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT REGION 383..417
FT /note="EVH2 block C"
FT COILED 138..164
FT /evidence="ECO:0000255"
FT COILED 386..412
FT /evidence="ECO:0000255"
FT MOTIF 235..238
FT /note="KLKR"
FT COMPBIAS 183..212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..7
FT /note="MFAFEEF -> M (in isoform 2)"
FT /id="VSP_059220"
FT VAR_SEQ 344..365
FT /note="LSRTPSVAKSPEAKSPLQSQPH -> L (in isoform 2)"
FT /id="VSP_059221"
FT CONFLICT 102
FT /note="E -> G (in Ref. 1; AAC53322)"
SQ SEQUENCE 420 AA; 45152 MW; FEEE5E87F4784989 CRC64;
MFAFEEFSEQ SICQARASVM VYDDTSKKWV PIKPGQQGFS RINIYHNTAS NTFRVVGVKL
QDQQVVINYS IVKGLKYNQA TPTFHQWRDA RQVYGLNFAS KEEATTFSNA MLFALNIMNS
QEGGPSTQRQ VQNGPSPEEM DIQRRQVMEQ QHRQESLERR ISATGPILPP GHPSSAASAT
FSCSGPPPPP PPPVPPPPTG STPPPPPPLP AGGAQGTNHD ESSASGLAAA LAGAKLRRVQ
RPEDASGGSS PSGTSKSDAN RASSGGGGGG LMEEMNKLLA KRRKAASQTD KPADRKEDEN
QTEDPSTSPS PGSRATSQPP NSSEAGRKPW ERSNSVEKPV SSLLSRTPSV AKSPEAKSPL
QSQPHSRVKP AGSVNDVGLD ALDLDRMKQE ILEEVVRELH KVKEEIIDAI RQELSGISTT
