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Database: UniProt
Entry: B3SBN3_TRIAD
LinkDB: B3SBN3_TRIAD
Original site: B3SBN3_TRIAD 
ID   B3SBN3_TRIAD            Unreviewed;       414 AA.
AC   B3SBN3;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=WW domain-containing oxidoreductase {ECO:0000256|ARBA:ARBA00016094};
GN   ORFNames=TRIADDRAFT_32795 {ECO:0000313|EMBL:EDV19893.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV19893.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV19893.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV19893.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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}.
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DR   EMBL; DS985265; EDV19893.1; -; Genomic_DNA.
DR   RefSeq; XP_002117635.1; XM_002117599.1.
DR   AlphaFoldDB; B3SBN3; -.
DR   STRING; 10228.B3SBN3; -.
DR   EnsemblMetazoa; TriadT32795; TriadP32795; TriadG32795.
DR   GeneID; 6758869; -.
DR   KEGG; tad:TRIADDRAFT_32795; -.
DR   CTD; 6758869; -.
DR   eggNOG; KOG1208; Eukaryota.
DR   HOGENOM; CLU_010194_44_0_1; -.
DR   InParanoid; B3SBN3; -.
DR   OMA; VHPGNMV; -.
DR   OrthoDB; 2466675at2759; -.
DR   PhylomeDB; B3SBN3; -.
DR   Proteomes; UP000009022; 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; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 2.
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; 2.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
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:UP000009022};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   DOMAIN          22..55
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          64..97
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  46232 MW;  9F8317889CAC7B5C CRC64;
     MQVSNLYSND ADTTSSDADS DPELLPGWEK SKTSTGRTFY VDHNTQTTQW EHPQRSHKKP
     HQKIDLPFGW IQIKNENGTI LYVNQRNQKK TYVDPRLAFR MKKNRRVFDA VSTSMDVLQG
     RNLSGGIALI TGATSGIGFE TARALALHGA LVIMGCHDIV KGSIAAKKIT KEEPLAKIDV
     IEVDLSSLKS IACLADEVLK KYRQLHVIIC NAGVLGLPWR LTTDELEYTF TVNYIGHFYL
     VKLLTELLIS SSPARVVVIS SESHRFPTTD GSSFNVENIL PSKQQFIPME AYNQSKLCGI
     LFSNEFNRKY SCYGVTSNAV HPGNLLPTSL CRNSWFYTIL FLLARPFAKS TVQGAATTTF
     CAAARELNGV GGSYFNNCQR CDPSPESQNE ELARALWKYT ESLLSCRTIR LLPQ
//
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