ID A0A0V0RI81_9BILA Unreviewed; 416 AA.
AC A0A0V0RI81;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=WW domain-containing oxidoreductase {ECO:0000256|ARBA:ARBA00016094};
GN Name=WWOX {ECO:0000313|EMBL:KRX14172.1};
GN ORFNames=T07_13376 {ECO:0000313|EMBL:KRX14172.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX14172.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX14172.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX14172.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX14172.1}.
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DR EMBL; JYDL01000169; KRX14172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0RI81; -.
DR STRING; 6336.A0A0V0RI81; -.
DR Proteomes; UP000054630; 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; 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:UP000054630};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 11..44
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 52..85
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
SQ SEQUENCE 416 AA; 47295 MW; 54770C759CFD22A2 CRC64;
MLGFAESDSE DELPSGWEER TTLDNRVYYV NHFEKSVQWN HPRTDRRKTV PAELPKNWKR
IVIEENKILY ENQVTGFKTY ADPRLAAAFE ETGEEEEEQL PRQRFDARTK ALQVLHGIDL
SNKTVMITGG TSGIGLEVVK AMLFHGANVI IACRNISRAR DTVAKLHTDR RCVKVEFIHC
DLASMSSVRR CAETFLASNW KLNVLILNAA TLEYSYSVTE DGLERTFSVN YLGQFYLTTF
LLKKLQNSTP ARIVITTGES HRLYALFSAN YHNLDEDELI SRITLTPENK DSYSGIIAYS
ISKLCLTMFA FYLNEKFSKQ HIFCNAVHPG NLVPTRLYRR YCCISALVWL LKPFTKSADQ
AASTIVFAAF SPDLNNIGGV YLNSCWFCSP SATSTNRTLQ RRLWNVSNEI LNSIGA
//
