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Database: UniProt
Entry: G3PB28_GASAC
LinkDB: G3PB28_GASAC
Original site: G3PB28_GASAC 
ID   G3PB28_GASAC            Unreviewed;       357 AA.
AC   G3PB28;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Prostaglandin reductase 2 {ECO:0000256|ARBA:ARBA00020652};
DE            EC=1.3.1.48 {ECO:0000256|ARBA:ARBA00011981};
DE   AltName: Full=15-oxoprostaglandin 13-reductase {ECO:0000256|ARBA:ARBA00033119};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000014802.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000014802.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000014802.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin
CC         F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374,
CC         ChEBI:CHEBI:133409; Evidence={ECO:0000256|ARBA:ARBA00023548};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590;
CC         Evidence={ECO:0000256|ARBA:ARBA00023548};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-
CC         oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:133408;
CC         Evidence={ECO:0000256|ARBA:ARBA00023544};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586;
CC         Evidence={ECO:0000256|ARBA:ARBA00023544};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=13,14-dihydro-15-oxo-prostaglandin E2 + NAD(+) = 15-
CC         oxoprostaglandin E2 + H(+) + NADH; Xref=Rhea:RHEA:11916,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00023690};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11918;
CC         Evidence={ECO:0000256|ARBA:ARBA00023690};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=13,14-dihydro-15-oxo-prostaglandin E2 + NADP(+) = 15-
CC         oxoprostaglandin E2 + H(+) + NADPH; Xref=Rhea:RHEA:11912,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00023711};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11914;
CC         Evidence={ECO:0000256|ARBA:ARBA00023711};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15-
CC         oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:79072, ChEBI:CHEBI:133411;
CC         Evidence={ECO:0000256|ARBA:ARBA00023543};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594;
CC         Evidence={ECO:0000256|ARBA:ARBA00023543};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC       {ECO:0000256|ARBA:ARBA00010460}.
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DR   AlphaFoldDB; G3PB28; -.
DR   STRING; 69293.ENSGACP00000014802; -.
DR   Ensembl; ENSGACT00000014830.1; ENSGACP00000014802.1; ENSGACG00000011166.1.
DR   eggNOG; KOG1196; Eukaryota.
DR   GeneTree; ENSGT00940000156793; -.
DR   InParanoid; G3PB28; -.
DR   OMA; EEKCRYA; -.
DR   TreeFam; TF324201; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000011166; Expressed in intestinal epithelial cell and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0036132; F:13-prostaglandin reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; IEA:UniProtKB-EC.
DR   CDD; cd08293; PTGR2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR041694; ADH_N_2.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR045010; MDR_fam.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR037399; PTGR2.
DR   PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR   PANTHER; PTHR43205:SF5; PROSTAGLANDIN REDUCTASE 2; 1.
DR   Pfam; PF16884; ADH_N_2; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT   DOMAIN          11..122
FT                   /note="Oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16884"
FT   DOMAIN          178..274
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   357 AA;  38340 MW;  77D44F4BB1E01334 CRC64;
     GYFSRMQVTR VVLNSRPGNN GAPVAENFRL EEATLSADLA DGDVLVRTLC LSVDPYMRCR
     MNEDTGVDYV TPWQLSECVD GGGVGVVESS RCGLCVEGDV VTSFNWPWQT RAVIKGSVLQ
     KVWHGAVDPK LVDGHLSYFL GAVGITGLTA LLGVREKGHV TKGANQTMVV SGAAGACGSI
     AGQIGRLDGC VRVVGICGSD EKCRALVDDL GFSAAINYRQ EDVPARLTEC CPNGIDVYFD
     NVGGSISDAV ITQMNSGSHV ILCGQISQYN KDVPYPPPLS EETKETLRRK NITRERFTVL
     NYMNQAEAAL CELSQRVQSG QINVLETVVN GIENMGDAFC SMMTGGNIGK QIIKISE
//
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