EVL_HUMAN
ID EVL_HUMAN Reviewed; 416 AA.
AC Q9UI08; A8K105; B7Z3I5; O95884; Q7Z522; Q8TBV1; Q9UF25; Q9UIC2;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Ena/VASP-like protein;
DE AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like;
GN Name=EVL; Synonyms=RNB6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Ohta S., Mineta T., Kimoto M., Tabuchi K.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wan Y.Z., Yu L., Yue P., Tu Q., Fu S.N., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to R.norvegicus RNB6 mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Substantia nigra;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Pancreas;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-416.
RC TISSUE=Brain;
RA Mei G., Yu W., Gibbs R.A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-364.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP INTERACTION WITH FYB1.
RX PubMed=10747096; DOI=10.1083/jcb.149.1.181;
RA Krause M., Sechi A.S., Konradt M., Monner D., Gertler F.B., Wehland J.;
RT "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP),
RT Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3
RT complex link T cell receptor (TCR) signaling to the actin cytoskeleton.";
RL J. Cell Biol. 149:181-194(2000).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-369, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-304; SER-306;
RP SER-329; SER-331 AND SER-349, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-341 AND SER-354, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-331 AND SER-369, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-369, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP IDENTIFICATION (ISOFORM 5).
RC TISSUE=Fetal brain;
RA Lemonidis K.;
RL Submitted (NOV-2016) to UniProtKB.
RN [20]
RP INTERACTION WITH SEMA6A.
RX PubMed=10993894; DOI=10.1074/jbc.m006316200;
RA Klostermann A., Lutz B., Gertler F., Behl C.;
RT "The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-
RT 1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like
RT protein (EVL) via a novel carboxyl-terminal zyxin-like domain.";
RL J. Biol. Chem. 275:39647-39653(2000).
RN [21]
RP INTERACTION WITH RAPH1.
RX PubMed=15469845; DOI=10.1016/j.devcel.2004.07.024;
RA Krause M., Leslie J.D., Stewart M., Lafuente E.M., Valderrama F.,
RA Jagannathan R., Strasser G.A., Rubinson D.A., Liu H., Way M., Yaffe M.B.,
RA Boussiotis V.A., Gertler F.B.;
RT "Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of
RT lamellipodial dynamics.";
RL Dev. Cell 7:571-583(2004).
RN [22]
RP INTERACTION WITH ZYX.
RX PubMed=18158903; DOI=10.1016/j.molcel.2007.10.033;
RA Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J.,
RA McDonald N.Q., Way M.;
RT "Tes, a specific Mena interacting partner, breaks the rules for EVH1
RT binding.";
RL Mol. Cell 28:1071-1082(2007).
RN [23]
RP INTERACTION WITH ZDHHC17.
RX PubMed=28882895; DOI=10.1074/jbc.m117.799650;
RA Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
RT "Peptide array based screening reveals a large number of proteins
RT interacting with the ankyrin repeat domain of the zDHHC17 S-
RT acyltransferase.";
RL J. Biol. Chem. 292:17190-17202(2017).
RN [24]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-188 AND LEU-247.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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.
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
CC (PubMed:10747096). Interacts with ZDHHC17 (PubMed:28882895).
CC {ECO:0000250|UniProtKB:P70429, ECO:0000269|PubMed:10747096,
CC ECO:0000269|PubMed:10993894, ECO:0000269|PubMed:15469845,
CC ECO:0000269|PubMed:18158903, ECO:0000269|PubMed:28882895}.
CC -!- INTERACTION:
CC Q9UI08; Q9P2A4: ABI3; NbExp=4; IntAct=EBI-346653, EBI-742038;
CC Q9UI08; Q13813: SPTAN1; NbExp=4; IntAct=EBI-346653, EBI-351450;
CC Q9UI08; Q9C026: TRIM9; NbExp=3; IntAct=EBI-346653, EBI-720828;
CC Q9UI08-2; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-6448852, EBI-742038;
CC Q9UI08-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-6448852, EBI-10968534;
CC Q9UI08-2; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-6448852, EBI-11110431;
CC Q9UI08-2; P42858: HTT; NbExp=20; IntAct=EBI-6448852, EBI-466029;
CC Q9UI08-2; O14656-2: TOR1A; NbExp=3; IntAct=EBI-6448852, EBI-25847109;
CC Q9UI08-2; Q9C026: TRIM9; NbExp=3; IntAct=EBI-6448852, EBI-720828;
CC Q9UI08-2; P09936: UCHL1; NbExp=3; IntAct=EBI-6448852, EBI-714860;
CC Q9UI08-2; O76024: WFS1; NbExp=3; IntAct=EBI-6448852, EBI-720609;
CC Q9UI08-2; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-6448852, EBI-524753;
CC Q9UI08-2; Q8N720: ZNF655; NbExp=3; IntAct=EBI-6448852, EBI-625509;
CC Q9UI08-2; Q15942: ZYX; NbExp=5; IntAct=EBI-6448852, EBI-444225;
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=5;
CC Name=2; Synonyms=EVL-I;
CC IsoId=Q9UI08-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9UI08-2; Sequence=VSP_004044;
CC Name=3;
CC IsoId=Q9UI08-3; Sequence=VSP_057322, VSP_057323;
CC Name=4;
CC IsoId=Q9UI08-4; Sequence=VSP_058779;
CC Name=5;
CC IsoId=Q9UI08-5; Sequence=VSP_004044, VSP_058778;
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 -!- MISCELLANEOUS: Required to transform actin polymerization into active
CC movement for the propulsive force of Listeria monocytogenes.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
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DR EMBL; AF052504; AAF21709.1; -; mRNA.
DR EMBL; AF087843; AAP97156.1; -; mRNA.
DR EMBL; AF112209; AAF17197.1; -; mRNA.
DR EMBL; AK289720; BAF82409.1; -; mRNA.
DR EMBL; AK295919; BAH12221.1; -; mRNA.
DR EMBL; AL133368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81684.1; -; Genomic_DNA.
DR EMBL; BC023997; AAH23997.1; -; mRNA.
DR EMBL; BC032358; AAH32358.1; -; mRNA.
DR EMBL; AF131766; AAD20040.1; -; mRNA.
DR EMBL; AL133642; CAB63763.2; -; mRNA.
DR CCDS; CCDS81851.1; -. [Q9UI08-1]
DR CCDS; CCDS9955.1; -. [Q9UI08-2]
DR RefSeq; NP_001317150.1; NM_001330221.1. [Q9UI08-1]
DR RefSeq; NP_057421.1; NM_016337.2. [Q9UI08-2]
DR AlphaFoldDB; Q9UI08; -.
DR SMR; Q9UI08; -.
DR BioGRID; 119556; 59.
DR ELM; Q9UI08; -.
DR IntAct; Q9UI08; 44.
DR MINT; Q9UI08; -.
DR STRING; 9606.ENSP00000376652; -.
DR GlyGen; Q9UI08; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UI08; -.
DR MetOSite; Q9UI08; -.
DR PhosphoSitePlus; Q9UI08; -.
DR BioMuta; EVL; -.
DR DMDM; 25090276; -.
DR EPD; Q9UI08; -.
DR jPOST; Q9UI08; -.
DR MassIVE; Q9UI08; -.
DR MaxQB; Q9UI08; -.
DR PaxDb; Q9UI08; -.
DR PeptideAtlas; Q9UI08; -.
DR PRIDE; Q9UI08; -.
DR ProteomicsDB; 6523; -.
DR ProteomicsDB; 84445; -. [Q9UI08-1]
DR ProteomicsDB; 84446; -. [Q9UI08-2]
DR Antibodypedia; 14371; 163 antibodies from 33 providers.
DR DNASU; 51466; -.
DR Ensembl; ENST00000392920.8; ENSP00000376652.3; ENSG00000196405.13. [Q9UI08-2]
DR Ensembl; ENST00000402714.6; ENSP00000384720.2; ENSG00000196405.13. [Q9UI08-1]
DR Ensembl; ENST00000544450.6; ENSP00000437904.2; ENSG00000196405.13. [Q9UI08-3]
DR GeneID; 51466; -.
DR KEGG; hsa:51466; -.
DR MANE-Select; ENST00000392920.8; ENSP00000376652.3; NM_016337.3; NP_057421.1. [Q9UI08-2]
DR UCSC; uc001ygt.4; human. [Q9UI08-1]
DR CTD; 51466; -.
DR DisGeNET; 51466; -.
DR GeneCards; EVL; -.
DR HGNC; HGNC:20234; EVL.
DR HPA; ENSG00000196405; Low tissue specificity.
DR neXtProt; NX_Q9UI08; -.
DR OpenTargets; ENSG00000196405; -.
DR PharmGKB; PA134890866; -.
DR VEuPathDB; HostDB:ENSG00000196405; -.
DR eggNOG; KOG4590; Eukaryota.
DR GeneTree; ENSGT00940000157826; -.
DR InParanoid; Q9UI08; -.
DR OMA; RTHYGIN; -.
DR PhylomeDB; Q9UI08; -.
DR TreeFam; TF321411; -.
DR PathwayCommons; Q9UI08; -.
DR Reactome; R-HSA-202433; Generation of second messenger molecules.
DR Reactome; R-HSA-376176; Signaling by ROBO receptors.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR SignaLink; Q9UI08; -.
DR SIGNOR; Q9UI08; -.
DR BioGRID-ORCS; 51466; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; EVL; human.
DR GeneWiki; Enah/Vasp-like; -.
DR GenomeRNAi; 51466; -.
DR Pharos; Q9UI08; Tbio.
DR PRO; PR:Q9UI08; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UI08; protein.
DR Bgee; ENSG00000196405; Expressed in granulocyte and 191 other tissues.
DR ExpressionAtlas; Q9UI08; baseline and differential.
DR Genevisible; Q9UI08; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; TAS:ProtInc.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0008154; P:actin polymerization or depolymerization; ISS:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; NAS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
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; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome; SH3-binding.
FT CHAIN 1..416
FT /note="Ena/VASP-like protein"
FT /id="PRO_0000087104"
FT DOMAIN 1..112
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 114..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..413
FT /note="EVH2"
FT REGION 222..242
FT /note="EVH2 block A"
FT REGION 265..282
FT /note="EVH2 block B"
FT REGION 342..362
FT /note="Required for interaction with ZDHHC17"
FT /evidence="ECO:0000269|PubMed:28882895"
FT REGION 379..413
FT /note="EVH2 block C"
FT MOTIF 231..234
FT /note="KLKR"
FT COMPBIAS 178..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08719"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08719"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:24275569"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1
FT /note="M -> MAT (in isoform 1 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.19,
FT ECO:0000303|Ref.2"
FT /id="VSP_004044"
FT VAR_SEQ 1
FT /note="M -> MFAFEEF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057322"
FT VAR_SEQ 342..362
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.19"
FT /id="VSP_058778"
FT VAR_SEQ 364..416
FT /note="MKPAGSVNDMALDAFDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGIST
FT T -> YRTTLLLTCPPGFGAPLSPVP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057323"
FT VAR_SEQ 368..397
FT /note="Missing (in isoform 4)"
FT /id="VSP_058779"
FT VARIANT 188
FT /note="P -> L (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs367737727)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036464"
FT VARIANT 247
FT /note="P -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036465"
FT CONFLICT 201
FT /note="P -> S (in Ref. 3; AAF17197)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="S -> N (in Ref. 2; AAP97156)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="M -> Y (in Ref. 9; CAB63763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 44620 MW; AD5B67458755D659 CRC64;
MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASNTFRVV GVKLQDQQVV
INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT FSNAMLFALN IMNSQEGGPS
SQRQVQNGPS PDEMDIQRRQ VMEQHQQQRQ ESLERRTSAT GPILPPGHPS SAASAPVSCS
GPPPPPPPPV PPPPTGATPP PPPPLPAGGA QGSSHDESSM SGLAAAIAGA KLRRVQRPED
ASGGSSPSGT SKSDANRASS GGGGGGLMEE MNKLLAKRRK AASQSDKPAE KKEDESQMED
PSTSPSPGTR AASQPPNSSE AGRKPWERSN SVEKPVSSIL SRTPSVAKSP EAKSPLQSQP
HSRMKPAGSV NDMALDAFDL DRMKQEILEE VVRELHKVKE EIIDAIRQEL SGISTT
