ID A0A3B5QGK8_XIPMA Unreviewed; 669 AA.
AC A0A3B5QGK8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ena/VASP-like protein {ECO:0000256|ARBA:ARBA00017156};
DE AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like {ECO:0000256|ARBA:ARBA00033193};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000030048.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000030048.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000030048.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000256|ARBA:ARBA00004529}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family.
CC {ECO:0000256|ARBA:ARBA00009785}.
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DR AlphaFoldDB; A0A3B5QGK8; -.
DR STRING; 8083.ENSXMAP00000030048; -.
DR Ensembl; ENSXMAT00000040718.1; ENSXMAP00000030048.1; ENSXMAG00000024161.1.
DR GeneTree; ENSGT00940000157826; -.
DR InParanoid; A0A3B5QGK8; -.
DR OMA; YQQMVQV; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR CDD; cd01207; EVH1_Ena_VASP-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR11202:SF4; ENA_VASP-LIKE PROTEIN; 1.
DR PANTHER; PTHR11202; SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1.
DR Pfam; PF08776; VASP_tetra; 1.
DR Pfam; PF00568; WH1; 1.
DR SMART; SM00461; WH1; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF118370; Vasodilator-stimulated phosphoprotein, VASP, tetramerisation domain; 1.
DR PROSITE; PS50229; WH1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 4..118
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 123..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..518
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 71658 MW; 333E58FB43AFF7B4 CRC64;
MYSLDDFGEQ SICQARASVM VYDDASKKWV PIKPGQQGFS RINIYHNTAN NTFRVVGVKL
QDQQVVINYS IVKGLKYNQA TPTFHQWRDA RQVYGLNFAS KEEATTFSNA MLFALNVLSS
PDSGGPVVQR QNGPSSEESE AQRRMMEQHQ MQAHKERERR TSGSVVSTLQ YKVSTPPTHP
DTPPEYRQFR ASTLPPSYVR VASSSSPPSQ EKELGAIRDK AQLSSQLSTS LASAFSPVQT
GVNTQGRQVR QIPLSPPTAA RHLQQQQQQQ DILLPPKHGT WSASLLQQMY PQPSSSPPVM
MPVKQGLPPQ PVLPVAHPLP PVSTRMKPPP LEPPAVGGLS QPPHPHSNGQ PDDSYSPLSQ
HLPLTPQYCE AIPLPPLIGQ SGPNHHPQNQ LTFHSQQHLH QQHQQQHHQQ AQTPTTITSS
SSSSSPPSYT AMSDGGSPKK TPSPVPQPAP AASSSGQVSA GHPAMLSVVP PPAAAPAPMA
GPPAPPPPPG PPPPMAVPPP MPPPLPTGGG PPGGPPGVQP SGLAAALAGA KLRKVQRDES
SPPGSGGKCD SNRSSGGSGG GGGEGLMQEM NALLARRRKA SEKPDEDDSG GRGQQNSTDA
LKKPWERSNS AEKSSLVSRV RPIGSTGEAD TEFDRMKQEI LDEVVRELHK VKDEIINAIR
HEIGRISTS
//
