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Database: UniProt
Entry: K7G7J4_PELSI
LinkDB: K7G7J4_PELSI
Original site: K7G7J4_PELSI 
ID   K7G7J4_PELSI            Unreviewed;       775 AA.
AC   K7G7J4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=ENAH actin regulator {ECO:0000313|Ensembl:ENSPSIP00000016255.1};
GN   Name=ENAH {ECO:0000313|Ensembl:ENSPSIP00000016255.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000016255.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000016255.1}
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; AGCU01051859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01051860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01051861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01051862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01051863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01051864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01051865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01051866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01051867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01051868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006118095.1; XM_006118033.2.
DR   AlphaFoldDB; K7G7J4; -.
DR   STRING; 13735.ENSPSIP00000016255; -.
DR   Ensembl; ENSPSIT00000016331.1; ENSPSIP00000016255.1; ENSPSIG00000014372.1.
DR   GeneID; 102454611; -.
DR   CTD; 55740; -.
DR   eggNOG; KOG4590; Eukaryota.
DR   GeneTree; ENSGT00940000157376; -.
DR   HOGENOM; CLU_017790_1_0_1; -.
DR   OMA; APMPPNM; -.
DR   OrthoDB; 2884005at2759; -.
DR   TreeFam; TF321411; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
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:UP000007267};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          1..111
FT                   /note="WH1"
FT                   /evidence="ECO:0000259|PROSITE:PS50229"
FT   REGION          127..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..389
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..458
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..587
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..684
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  84214 MW;  3BACB8DF398C1BA5 CRC64;
     MSEQSICQAR AAVMVYDDTN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
     NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAVFYL
     GPTLPRQNSQ LPPQVQNGPS QEELEIQRRQ LQEQQRQKEL ERERLDRERM ERERLERDRL
     ERERLERERL EQEQLERERQ ERERQERLER ERQERERQDR ERLERLERER QERERQEQLE
     REQLEWERER RISNAASSFD NSLYSTPLPE YSSCQPPSAP PPSYAKAISA AGSDSAPDYA
     VVTSAQATST PPTPPLRHSA SRFATSLGSA FHPVLPHYAT VPRPLNKNSR PPSPVNAPAS
     LPPNTKSIVW SAPSFAPLPP SPPVMISSPP GKAAGPKPVL PISASSSVSQ MHQSPPPPNG
     LPESVTYPVP SPSTSGPTPP PPPPPPLPSF PPVSLSGPQA SPSPSSPNAS TPSSKPSVLP
     SPSAATPASV ENSLNSVLGD SSASEPVLQA AFQLIEPPTQ QGVIQGPPAP PPPPPLPPGP
     AQSSTAIPPP PGPPPPLPPS GPPPPPPLPS QVPPPVPPPP PAPPLPASGF SMGSMSEDSR
     PLTGLAAALA GAKLRKVSRN EESSSPCGGA LSKADSVRGN GPLPLGGSGL MEEMSALLAR
     RRRIAEKGST EPEQKEDKPE ESEPSTSKPS STSTPELTRK PWERTNTVNG SKSPVISRPK
     STPSGQPSAN GVQSEGLDYD RLKQDILDEM RKELTKLKEE LIDAIRQELN KSNTA
//
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