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Database: UniProt
Entry: A0A2Y9K3L5_ENHLU
LinkDB: A0A2Y9K3L5_ENHLU
Original site: A0A2Y9K3L5_ENHLU 
ID   A0A2Y9K3L5_ENHLU        Unreviewed;       570 AA.
AC   A0A2Y9K3L5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Protein enabled homolog isoform X1 {ECO:0000313|RefSeq:XP_022364275.1};
GN   Name=LOC111150887 {ECO:0000313|RefSeq:XP_022364275.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022364275.1};
RN   [1] {ECO:0000313|RefSeq:XP_022364275.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022364275.1};
RG   RefSeq;
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   RefSeq; XP_022364275.1; XM_022508567.1.
DR   AlphaFoldDB; A0A2Y9K3L5; -.
DR   STRING; 391180.A0A2Y9K3L5; -.
DR   KEGG; elk:111150887; -.
DR   OrthoDB; 2884005at2759; -.
DR   Proteomes; UP000248482; 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   CDD; cd22185; WH2_hVASP-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   PRINTS; PR01217; PRICHEXTENSN.
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:UP000248482};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          1..111
FT                   /note="WH1"
FT                   /evidence="ECO:0000259|PROSITE:PS50229"
FT   REGION          115..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..353
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  63351 MW;  87286B8A1E3E643D CRC64;
     MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
     NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQETGPTL
     PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ QRQKELERER VERAERERLE QEQLEREQRE
     RERQDRLERE RLERIDRERE QRERQERQEQ RERQEQRERE REQRERQEQL EREQLEWERE
     RRLSAAAAPA SAETPLNSVL GDSSASEPGL QAASQPAETP AQQGLVLGPP APPPPPPLPP
     GPVPAPAVLH PHPGPPPPPP LPAAGPPPPP PPPPLPNQAP PPPPPPPAPP LPASGFFAGS
     ASEDNRPLTG LAAAIAGAKL RKVSRMEDGS FPSGGTTVGV NAASLKSDTG RGNGPLPLGG
     SGLMEEMSAL LARRRRIAEK GSTVETEQKE DKNEESEPVT SKASSTSTPE PTRKPWERTN
     TMNGSKSPVI SRRDSPRKNQ IVFDNRSYDS LHRPKSAPSS QPSANGVQTE GLDYDRLKQD
     ILDEMRKELT KLKEELIDAI RQELSKSNSA
//
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