ID   PGFS2_BOVIN             Reviewed;         323 AA.
AC   P52897;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Prostaglandin F synthase 2;
DE            Short=PGF synthase 2;
DE            Short=PGFS2;
DE            Short=PGF 2;
DE            EC=1.1.1.188;
DE   AltName: Full=Prostaglandin F synthase II;
DE            Short=PGFSII;
DE   AltName: Full=Prostaglandin-D2 11 reductase 2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=92231889; PubMed=1339268; DOI=10.1016/S0006-291X(05)80323-7;
RA   Kuchinke W., Barski O., Watanabe K., Hayaishi O.;
RT   "A lung type prostaglandin F synthase is expressed in bovine liver:
RT   cDNA sequence and expression in E. coli.";
RL   Biochem. Biophys. Res. Commun. 183:1238-1246(1992).
CC   -!- FUNCTION: Catalyzes the reduction of PGD(2) and PGH(2) to PGF(2
CC       alpha) and a stereoisomer, respectively. It has a broad substrate
CC       specificity and reduces also other carbonyl compounds.
CC   -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha,15-
CC       trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-9-
CC       alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH.
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
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DR   EMBL; M86544; AAA30730.1; -; mRNA.
DR   IPI; IPI00701050; -.
DR   PIR; E75572; JH0575.
DR   RefSeq; XP_001250623.1; -.
DR   UniGene; Bt.64820; -.
DR   UniGene; Bt.66508; -.
DR   UniGene; Bt.67184; -.
DR   UniGene; Bt.91770; -.
DR   HSSP; P52895; 1J96.
DR   SMR; P52897; 2-323.
DR   Ensembl; ENSBTAG00000022570; Bos taurus.
DR   GeneID; 782922; -.
DR   KEGG; bta:782922; -.
DR   HOVERGEN; P52897; -.
DR   BRENDA; 1.1.1.188; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047017; F:prostaglandin-F synthase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001395; Aldo/ket_red.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732; Aldo/ket_red; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   ProDom; PD000288; Aldo/ket_red; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Fatty acid biosynthesis; Lipid synthesis; NADP;
KW   Oxidoreductase; Prostaglandin biosynthesis.
FT   CHAIN         1    323       Prostaglandin F synthase 2.
FT                                /FTId=PRO_0000124647.
FT   NP_BIND      13     22       NADP (Potential).
FT   NP_BIND     217    280       NADP (By similarity).
FT   ACT_SITE     55     55       Proton donor (By similarity).
FT   BINDING     117    117       Substrate (By similarity).
FT   SITE         84     84       Lowers pKa of active site Tyr (By
FT                                similarity).
SQ   SEQUENCE   323 AA;  36742 MW;  21A5BE0668D07A2C CRC64;
     MDPKSQRVKF NDGHFIPVLG FGTYAPEEVP KSEALEATKF AIEVGFRHVD SAHLYQNEEQ
     VGQAIRSKIA DGTVKREDIF YTSKLWCNSL QPELVRPALE KSLQNLQLDY VDLYIIHSPV
     SLKPGNKFVP KDESGKLIFD SVDLCHTWEA LEKCKDAGLT KSIGVSNFNH KQLEKILNKP
     GLKYKPVCNQ VECHPYLNQS KLLEFCKSHD IVLVAYAALG AQLLSEWVNS NNPVLLEDPV
     LCAIAKKHKQ TPALVALRYQ VQRGVVVLAK SFNKKRIKEN MQVFDFELTP EDMKAIDGLN
     RNTRYYDFQQ GIGHPEYPFS EEY
//