ID   PTGR1_MOUSE             Reviewed;         329 AA.
AC   Q91YR9; Q3TKT6; Q9CPS1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Prostaglandin reductase 1;
DE            Short=PRG-1;
DE            EC=1.3.1.-;
DE   AltName: Full=NADP-dependent leukotriene B4 12-hydroxydehydrogenase;
DE            EC=1.3.1.74;
DE   AltName: Full=15-oxoprostaglandin 13-reductase;
DE            EC=1.3.1.48;
GN   Name=Ptgr1; Synonyms=Ltb4dh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Liver, Testis, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts
CC       on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity
CC       towards PGE1, PGE2 and PGE2-alpha. Catalyzes the conversion of
CC       leukotriene B4 into its biologically less active metabolite, 12-
CC       oxo-leukotriene B4. This is an initial and key step of metabolic
CC       inactivation of leukotriene B4 (By similarity).
CC   -!- CATALYTIC ACTIVITY: n-alkanal + NAD(P)(+) = alk-2-enal + NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: 11-alpha-hydroxy-9,15-dioxoprost-5-enoate +
CC       NAD(P)(+) = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13-
CC       dienoate + NAD(P)H.
CC   -!- SUBUNIT: Monomer or homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD
CC       family.
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DR   EMBL; AK010888; BAB27248.1; -; mRNA.
DR   EMBL; AK011962; BAB27941.1; -; mRNA.
DR   EMBL; AK035425; BAC29060.1; -; mRNA.
DR   EMBL; AK134440; BAE22145.1; -; mRNA.
DR   EMBL; AK166835; BAE39057.1; -; mRNA.
DR   EMBL; BC014865; AAH14865.1; -; mRNA.
DR   IPI; IPI00131887; -.
DR   RefSeq; NP_080244.1; -.
DR   UniGene; Mm.34497; -.
DR   HSSP; P96202; 1PQW.
DR   SMR; Q91YR9; 1-329.
DR   PhosphoSite; Q91YR9; -.
DR   REPRODUCTION-2DPAGE; Q91YR9; -.
DR   PRIDE; Q91YR9; -.
DR   Ensembl; ENSMUSG00000028378; Mus musculus.
DR   GeneID; 67103; -.
DR   KEGG; mmu:67103; -.
DR   MGI; MGI:1914353; Ptgr1.
DR   HOGENOM; Q91YR9; -.
DR   HOVERGEN; Q91YR9; -.
DR   OMA; Q91YR9; WQGEVRQ.
DR   BRENDA; 1.3.1.48; 244.
DR   BRENDA; 1.3.1.74; 244.
DR   NextBio; 323584; -.
DR   ArrayExpress; Q91YR9; -.
DR   Bgee; Q91YR9; -.
DR   GermOnline; ENSMUSG00000028378; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; IEA:EC.
DR   GO; GO:0032440; F:2-alkenal reductase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002085; ADH_SF_Zn.
DR   InterPro; IPR013149; ADH_Zn-bd.
DR   InterPro; IPR014190; B4_12hDH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11695; ADH_Sf_Zn; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   TIGRFAMs; TIGR02825; B4_12hDH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN         1    329       Prostaglandin reductase 1.
FT                                /FTId=PRO_0000218066.
FT   NP_BIND     149    166       NADP (Potential).
FT   BINDING     178    178       NADP (By similarity).
FT   BINDING     193    193       NADP (By similarity).
FT   BINDING     217    217       NADP (By similarity).
FT   BINDING     245    245       NADP (By similarity).
FT   BINDING     321    321       NADP (By similarity).
FT   CONFLICT    298    298       C -> Y (in Ref. 2; AAH14865).
FT   CONFLICT    301    301       Y -> H (in Ref. 2; AAH14865).
SQ   SEQUENCE   329 AA;  35560 MW;  FD0CA4682DB493D8 CRC64;
     MVQAKSWTLK KHFEGFPTDG NFELKTTELP PLNNGEVLLE ALFLSVDPYM RVAAKKLKEG
     DRMMGEQVAR VVESKNSAFP KGTIVAALLG WTSHSISDGN GLTKLPVEWP DKLPLSLALG
     TVGMPGLTAY FGLLDICGVK GGETVMVSAA AGAVGSVVGQ IAKLKGCKVV GTAGSDEKVA
     YLKKLGFDVA FNYKTVKSLE EALRTASPDG YDCYFDNVGG EFSNAVILQM KTFGRIAICG
     AISQYNRTGP CPQGPAPEVV IYQQLRMEGF IVNRWQGEVR QKALTELMNW VSEGKVQCHE
     YVTEGFEKMP AAFMGMLKGE NLGKTIVKA
//