GenomeNet

Database: UniProt
Entry: A0A1X7TVA5_AMPQE
LinkDB: A0A1X7TVA5_AMPQE
Original site: A0A1X7TVA5_AMPQE 
ID   A0A1X7TVA5_AMPQE        Unreviewed;       437 AA.
AC   A0A1X7TVA5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=WW domain-containing oxidoreductase {ECO:0000256|ARBA:ARBA00016094};
GN   Name=100638016 {ECO:0000313|EnsemblMetazoa:Aqu2.1.18820_001};
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.18820_001, ECO:0000313|Proteomes:UP000007879};
RN   [1] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20686567; DOI=10.1038/nature09201;
RA   Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA   Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA   Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA   Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA   Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA   Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The Amphimedon queenslandica genome and the evolution of animal
RT   complexity.";
RL   Nature 466:720-726(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA   Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA   Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA   Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA   Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA   Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT   evolution of animal complexity.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.18820_001}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2017) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi
CC       apparatus {ECO:0000256|ARBA:ARBA00004555}. Lysosome
CC       {ECO:0000256|ARBA:ARBA00004371}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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   RefSeq; XP_011406756.1; XM_011408454.2.
DR   AlphaFoldDB; A0A1X7TVA5; -.
DR   STRING; 400682.A0A1X7TVA5; -.
DR   EnsemblMetazoa; Aqu2.1.18820_001; Aqu2.1.18820_001; Aqu2.1.18820.
DR   GeneID; 100638016; -.
DR   KEGG; aqu:100638016; -.
DR   eggNOG; KOG1208; Eukaryota.
DR   InParanoid; A0A1X7TVA5; -.
DR   OMA; RATWTHV; -.
DR   OrthoDB; 2466675at2759; -.
DR   Proteomes; UP000007879; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd05327; retinol-DH_like_SDR_c_like; 1.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR24320; RETINOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR24320:SF269; WW DOMAIN-CONTAINING OXIDOREDUCTASE; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF00397; WW; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   DOMAIN          33..66
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   437 AA;  48902 MW;  D046C5ECC7386651 CRC64;
     MASSEEADVR SPPYPDPLES LPYWGHGPGE DITSLPAGWE GRVTSEGRVF FIDHNERETH
     WSHPVTKMKY RVQSHLSYGW QLFKDEDDAV VFVDHLEGVC SKVDPRLLNR RAFDFPEEYG
     IRSFNPLQHR LKPYSTADDV LKDISLQGKV AIVTGANSGL GYETARSLAS HGAHVILACR
     DRGRGATAVN LIQKSHPRAK VEHRDLDLAS LRSVRLFSEF FIASGLSLDI LVCNAGLLEP
     SFTLTEDGLE SHFAVNYLGH FYLINLLKDI LSKSTLPRIV IVSSESHWYP SPKSTKLELQ
     YLKNPNRENY NYFAAYGASK LCCILLMQEL YRRHPLICTN AVHPGNFLPT GLLRRTNCMY
     KLLRITARPF TSSVAQAASG IVFCGAHPVM EGVSGLYMYR CSVAEPSGEA QSHGTAAALW
     DLSTQIIRDK MTQWGKD
//
DBGET integrated database retrieval system