ID A0A9D3SA75_ANGAN Unreviewed; 648 AA.
AC A0A9D3SA75;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 11.
DE RecName: Full=Ena/VASP-like protein {ECO:0000256|ARBA:ARBA00017156};
DE AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like {ECO:0000256|ARBA:ARBA00033193};
GN ORFNames=ANANG_G00016130 {ECO:0000313|EMBL:KAG5857156.1};
OS Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC Anguilla.
OX NCBI_TaxID=7936 {ECO:0000313|EMBL:KAG5857156.1, ECO:0000313|Proteomes:UP001044222};
RN [1] {ECO:0000313|EMBL:KAG5857156.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tag_6206 {ECO:0000313|EMBL:KAG5857156.1};
RC TISSUE=Liver {ECO:0000313|EMBL:KAG5857156.1};
RA Henkel C., Jong-Raadsen S.A., Dufour S., Weltzien F.-A., Palstra A.P.,
RA Pelster B., Spaink H.P., Van Den Thillart G.E., Jansen H., Zahm M.,
RA Klopp C., Cedric C., Louis A., Berthelot C., Parey E., Roest Crollius H.,
RA Montfort J., Robinson-Rechavi M., Bucao C., Bouchez O., Gislard M.,
RA Lluch J., Milhes M., Lampietro C., Lopez Roques C., Donnadieu C.,
RA Braasch I., Desvignes T., Postlethwait J., Bobe J., Guiguen Y., Dirks R.;
RT "A chromosome-scale assembly of European eel, Anguilla anguilla.";
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00057639}.
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000256|ARBA:ARBA00004529}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family.
CC {ECO:0000256|ARBA:ARBA00009785}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG5857156.1}.
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DR EMBL; JAFIRN010000001; KAG5857156.1; -; Genomic_DNA.
DR Proteomes; UP001044222; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; IEA:TreeGrafter.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:TreeGrafter.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:TreeGrafter.
DR CDD; cd01207; EVH1_Ena_VASP-like; 1.
DR FunFam; 1.20.5.1160:FF:000004; Enah/Vasp-like, isoform CRA_a; 1.
DR FunFam; 2.30.29.30:FF:000071; Enah/Vasp-like, isoform CRA_a; 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:UP001044222};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 6..120
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 151..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..217
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..277
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..515
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 70088 MW; 119867C58AE39DE7 CRC64;
MTSCLSFPFS EQSICQARAS VMVYDDTSKK WVPIKPGQQG FSRINIYHNT ASNTFRVVGV
KLQDQQVVIN YSIVKGLKYN QATPTFHQWR DARQVYGLNF ASKEEATTFS NAMLFALNVL
NTQEGGPRSP FTGSFAAVAL RAAGSVRSLS QSEVGRSRLA MPGQEPSPGQ LRRVSSAVIR
LSSPAGQRQV QNGPSTDDAE GQRRMMEQQQ QQQMQAQIER ERRTSASVST LQFKVCPSPY
QSEAPPPEYR HYRASTLPPP SYARVTSSPS SCSSSSSQGT EVVCPPQQAQ TSQLSTSLAS
AFSPVQSGVG GAQSRNVRQI PISPPTTPRH QGRKLPQAWH LVLRLLILCS AIFASQCDCV
PPASGPSFAP PQSSSPHPGL PLTRGALPLQ ARLHLSPRAP PNSSHSLPFK CNSYTRPCPP
STLHPPLTTL SLKGQHPRRP PRSHPTPVLL SHQGIPLYSQ WLLPLLHQPL HCGGPGGPGE
EAPSGLAAAL AGAKLRRVQR SEDGSVGASA GGAKSDANRS SGGGGGGLME EMNALLARRR
KAATQTEKPG DRKEDDSQNE DPNSPITRVP GQPNSTDPVK KPWDRANSAE KSSLVSRVRP
IGSSSDTDAL DFDRMKQEIL EEVVRELHKV KNEIIDAIRH ELSRISTT
//
