GenomeNet

Database: UniProt
Entry: A0A2K6Q072_RHIRO
LinkDB: A0A2K6Q072_RHIRO
Original site: A0A2K6Q072_RHIRO 
ID   A0A2K6Q072_RHIRO        Unreviewed;       623 AA.
AC   A0A2K6Q072;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=ENAH actin regulator {ECO:0000313|Ensembl:ENSRROP00000022177.1};
GN   Name=ENAH {ECO:0000313|Ensembl:ENSRROP00000022177.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000022177.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000022177.1}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A2K6Q072; -.
DR   Ensembl; ENSRROT00000046374.1; ENSRROP00000022177.1; ENSRROG00000034960.1.
DR   GeneTree; ENSGT00940000157376; -.
DR   Proteomes; UP000233200; 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:UP000233200};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..623
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014336398"
FT   DOMAIN          19..132
FT                   /note="WH1"
FT                   /evidence="ECO:0000259|PROSITE:PS50229"
FT   REGION          163..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..402
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  69890 MW;  082195E8922D9D78 CRC64;
     MWLCGTFSIF NIVSLNILFY FYSEQSICQA RAAVMVYDDA NKKWVPAGGS TGFSRVHIYH
     HTGNNTFRVV GRKIQDHQVV INCAIPKGLK YNQATQTFHQ WRDARQVYGL NFGSKEDANV
     FASAMMHALE VLNSQETAQS KVTATQDSTN LRCIFCGPTL PRQNSQLPAQ VQNGPSQEEL
     EIQRRQLQEQ QRQKELERER LERERMERER LERERLERER LERERLEQEQ LERERQERER
     QERLERQERL DRERQERQER ERLERLERER QERERQEQLE REQLEWERER RISSAAAPAS
     VETPLNSVLG DSSASEPGLQ AASQPAETPA QQGIVLGPLA PPPPPPLPPG PAQASVALPP
     PPGPPPPPPL PSTGPPPPPP PPPLPNQVPP PPPPPPAPPL PASGFFLASV SEDNRPLTGL
     AAAIAGAKLR KVSRMEDASF PSGGNAIGVN SASSKADTGR GNGPLPLGGS GLMEEMSALL
     ARRRRIAEKG STVETEQKED KGEDSEPVTS KASSTSTPEP TRKPWERTNT MNGSKSPVIS
     RRDSPRKNQI VFDNRSYDSL HRPKSTPLSQ PSANGVQTEG LDYDRLKQDI LDEMRKELTK
     LKEELIDGKY LDKFTIPIPI NNV
//
DBGET integrated database retrieval system