ID A0A4W5NCS4_9TELE Unreviewed; 521 AA.
AC A0A4W5NCS4;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE SubName: Full=Enah/Vasp-like a {ECO:0000313|Ensembl:ENSHHUP00000047728.1};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000047728.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000047728.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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DR AlphaFoldDB; A0A4W5NCS4; -.
DR STRING; 62062.ENSHHUP00000047728; -.
DR Ensembl; ENSHHUT00000049472.1; ENSHHUP00000047728.1; ENSHHUG00000028975.1.
DR GeneTree; ENSGT00940000157826; -.
DR Proteomes; UP000314982; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; IEA:TreeGrafter.
DR GO; GO:0017124; F:SH3 domain binding; IEA:TreeGrafter.
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 Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
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 PRINTS; PR01217; PRICHEXTENSN.
DR SUPFAM; SSF118370; Vasodilator-stimulated phosphoprotein, VASP, tetramerisation domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000314982}.
FT DOMAIN 483..515
FT /note="VASP tetramerisation"
FT /evidence="ECO:0000259|Pfam:PF08776"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..71
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..353
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..419
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 54870 MW; D9C26B60AC5CCDBC CRC64;
MDPHQMQGVA HKERERRTSG SVVSTLQYKV AFPPSHPSNT PLEYRHYRAA TLPPPYARGA
SNSSPSSTSS SQEREVAGGQ AGDNSAQLSQ LSTSLVSAFS PVQPGVPTAL TRQVRQIPLS
PPTARALHHT KSLHQGDPQQ DPVLLPKHGT WSASHTHIYG PVHMPPVPQP VLPVALPLPP
RHSRVKPHTL DQAGQPHIPP HLPHANGQSE DYYNLAQQQQ QQLGYCEATS LPPLIGQSAQ
GPVPVSSNQP QYPSSFHPQQ QMSQAAPPPP PPAAQFSPPS YTPAPSEWGS PKQTPSPVSQ
AATATCSPVS LPAMLAVAPP VAPPAPMAPM APPPPPGPPP PATVPPPMPP PLPVGGGHGG
PQIEGAGNEL AQPLSGLAAA LAGAKLRKVA RDENSPPGTG GAKNDGNRSS GGSGGGGEGL
MQEMNALLAR RRKASEKPEE EDPKPGQNST DAGKNPWDRA NSVDKASLVS RVRPVGSTSE
GDLDFDRMKQ EILDEVVREL QKVKDEIINA IRQEIGRIHT C
//
