ID W5NG30_LEPOC Unreviewed; 764 AA.
AC W5NG30;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=ENAH actin regulator {ECO:0000313|Ensembl:ENSLOCP00000019589.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000019589.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000019589.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AHAT01008384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NG30; -.
DR STRING; 7918.ENSLOCP00000019589; -.
DR Ensembl; ENSLOCT00000019621.1; ENSLOCP00000019589.1; ENSLOCG00000015905.1.
DR eggNOG; KOG4590; Eukaryota.
DR GeneTree; ENSGT00940000157376; -.
DR HOGENOM; CLU_017790_1_0_1; -.
DR InParanoid; W5NG30; -.
DR OMA; APMPPNM; -.
DR Proteomes; UP000018468; Linkage group LG1.
DR Bgee; ENSLOCG00000015905; Expressed in muscle tissue and 11 other cell types or tissues.
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:0005522; F:profilin binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0070358; P:actin polymerization-dependent cell motility; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
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:SF1; PROTEIN ENABLED HOMOLOG; 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:UP000018468};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 8..121
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 124..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 83618 MW; C7BFB7DC467F341A CRC64;
RDTLASMFGI SNEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNAFRVVG
RKIQDHQVVI NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV
LNSQDTGPTL PRQNPQLSPQ VQNGPSQEEL EIQRRQLQEQ QRLKELERER LERDRLERER
LERERLERER LERERLERER LERERLERER LERERLERER LERERLERER LEQEQLEREK
LERERLEREH HEQHDREQME WERERRMSNA AFESTLYTTP PPEYSSCLPP AAPPPSYAKA
IATPLSSSSP DYTASPSPAA PPTPPLRHSA SRFATSLGSA FHPVLPHYAT IPRPLNKHPA
APPAPAPLPP APPSTKSMVW SATNFSPLPP SPPVMISSPP GKAAGPRPVL PIPAPSPLSQ
KALSQPPPLP PPPPPPPLPP LSLSSSSQVS PTSPISPLVS SPSSQPAVLP SPSAASPASA
EHSLNSVLGD SCSSAPEPVA SQPAEPHTLP GKAFSVSPPP LTNGLISWRV ARFSKGAGHV
QFESPVKLPK RLLPKGLPVP PPPPPPPPPP PPLPPQASEE NRPLAGLAAA LAGAKLRKVP
RNDEAPNAAP GGAMGSAASK TESSRGNGPL SVGGGGLMEE MSALLARRRR IAEKGSTPEP
EQKDKADEPE PSAPKVSSSG TPDMARKPWE RTNTMNGSKS PVISRPKSTP TPTGSLSANG
MPTEGLDYDR LKQDILDEMR KELTKLKEEL IDAIRQELGK SNTA
//
