ID A0A3Q3ART9_KRYMA Unreviewed; 829 AA.
AC A0A3Q3ART9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=ENAH actin regulator {ECO:0000313|Ensembl:ENSKMAP00000019120.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000019120.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000019120.1}
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 Ensembl; ENSKMAT00000019384.1; ENSKMAP00000019120.1; ENSKMAG00000014186.1.
DR GeneTree; ENSGT00940000157376; -.
DR Proteomes; UP000264800; 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: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:UP000264800};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 1..114
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 115..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..628
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 89095 MW; 92A458F7F8A75711 CRC64;
MTRDSEQSIC QARAAVMVYD DANKKWVPAG GSTGFSRVHI YHHTGTNAFR VVGRKIQDHQ
VVINCAIPKG LKYNQATQTF HQWRDARQVY GLNFGSKEDA NVFASAMMHA LEVLNSQDTG
PTLPRQGQQV QNGPTQEEMD LQRRQLEELQ RQKEVERERQ ERESQERERQ EQERQEQERQ
ERERLEREAA ERQERERQER AEQAERERQE QQERAERELM EREKAERERL EKEQQEQLDR
EQQDWERGRR ISNAAFESTL YTPTPLEYSR TSSTPVSPST PTYPAPSTPS PSSTAPPTPP
LRQSASRFAT SLGSAFHPVL PHYATVPRRQ QAFPQALNPA PVPAPIPTPP PKSVVWSASN
FTPLPPSPPV MISSPPGKAT GPRPLIPVAT PSPLSQKPPS PSPNGPPMFP APSPVTIPHS
HTPLGISCPT PPPPPTPPPL PLPXXXXXXX XXXXXXXXXX PLPLPMALPP FSSSVSSPPS
SSQAPGVPSP STAPPAAAAA ATSASAEHLS LPVGLGLSGP EEPGTAAGPE PHSTQGGSSW
QPQPQDVVQG PALTAPSXXX XXXXXXXGST VTSATATPAI TPTTPVGHPP PPPPPPPLPP
TLTPSGTPPP PPGAPLPPPA PPLPAGLFSP TEDRPFSGLA AALAGAKLRK VPRSDDAGAA
LAAAISGAAG AKSEARGNGP LPGGGGLMEE MSALLARRRR IAEKGSSPEP DQRSEEGEIN
TTPKVSACST PDMPRKPWER TNTMNGSKSP VIGRREPPWR NPVGADSSSR PKSTPTPTAS
LSANGVPTEA VDYDRLKQDI LDEMRKELLK LKEELIDAIR EELGKSSTA
//
