ID A0A3B4TNE0_SERDU Unreviewed; 420 AA.
AC A0A3B4TNE0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Vasodilator-stimulated phosphoprotein-like {ECO:0000313|Ensembl:ENSSDUP00000007542.1};
GN Name=VASP {ECO:0000313|Ensembl:ENSSDUP00000007542.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000007542.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000007542.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family.
CC {ECO:0000256|ARBA:ARBA00009785}.
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DR AlphaFoldDB; A0A3B4TNE0; -.
DR STRING; 41447.ENSSDUP00000007542; -.
DR Ensembl; ENSSDUT00000007681.1; ENSSDUP00000007542.1; ENSSDUG00000005533.1.
DR GeneTree; ENSGT00940000156765; -.
DR OMA; QGPRVKH; -.
DR OrthoDB; 2884005at2759; -.
DR Proteomes; UP000261420; Unplaced.
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; SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1.
DR PANTHER; PTHR11202:SF12; VASODILATOR-STIMULATED PHOSPHOPROTEIN; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 1..113
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 123..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 386..413
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 137..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..230
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 44598 MW; 44C7A9C2D89A4A76 CRC64;
MSESSICQAR ATVMIYDDGN KKWLPAGAGA QTFSRVQIYH NPSNNAFRIV GRKMQTDQQV
VINCPIVRGL KYNQATPNFH QWRDARQVWG LNFGSKEDAT LFANCMAHAL EVLNSMADAG
YATLPRPVSN GPSPEELEQQ RRLEQQRSEQ QERERQERER QERERQERER QDRERQAAAV
PIPPAPPLAP GGPAPPPAPP PPPGLPPAAG IPPPPGPPPS GPPPAPPLPA AGGGGGLGGG
GIGGGGGLAA ALAGAKLRKT SKQEDTGSAA PIGRGDPSRS SNSSIGGGGG GGGGGGLMGE
MSAILARRRK AADTGEKPPV KPQDNDDSEP QGQSDTLRRP WEKSSMTRNN SIAKNMDSTP
SLSQGSRVKP ASNSNDAGGM DDSDLEKMKQ EILEEVRKEL QKVKEEIIGA FIQELQKRST
//
