ID   PTGR2_HUMAN             Reviewed;         351 AA.
AC   Q8N8N7; Q3L8A4; Q6MZH8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   07-JUL-2009, entry version 56.
DE   RecName: Full=Prostaglandin reductase 2;
DE            Short=PRG-2;
DE            EC=1.3.1.48;
DE   AltName: Full=15-oxoprostaglandin 13-reductase;
DE   AltName: Full=Zinc-binding alcohol dehydrogenase domain-containing protein 1;
GN   Name=PTGR2; Synonyms=ZADH1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   ALTERNATIVE SPLICING.
RX   PubMed=15004468; DOI=10.1159/000076293;
RA   Zhang L., Zhang F., Huo K.;
RT   "Cloning and characterization of a novel splicing variant of the ZADH1
RT   gene.";
RL   Cytogenet. Genome Res. 103:79-83(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Zheng H., Xie Y., Mao Y.;
RT   "Cloning and characterization of a putative dehydrogenase.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal kidney;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K.,
RA   Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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).
RN   [7]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts
CC       on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-
CC       PGE2-alpha with highest activity towards 15-keto-PGE2.
CC       Overexpression represses transcriptional activity of PPARG and
CC       inhibits adipocyte differentiation (By similarity).
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   -!- COFACTOR: NADPH (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=ZADH1b;
CC         IsoId=Q8N8N7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N8N7-2; Sequence=VSP_013526, VSP_013527;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD
CC       family.
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DR   EMBL; AY346133; AAR05101.1; -; mRNA.
DR   EMBL; AY424308; AAR82927.1; -; mRNA.
DR   EMBL; AK096410; BAC04781.1; -; mRNA.
DR   EMBL; BX641118; CAE46055.1; -; mRNA.
DR   EMBL; CH471061; EAW81132.1; -; Genomic_DNA.
DR   EMBL; BC059364; AAH59364.1; -; mRNA.
DR   IPI; IPI00167515; -.
DR   IPI; IPI00869302; -.
DR   RefSeq; NP_001139626.1; -.
DR   RefSeq; NP_001139627.1; -.
DR   RefSeq; NP_689657.1; -.
DR   UniGene; Hs.632344; -.
DR   PDB; 2VNA; X-ray; 2.17 A; A=1-349.
DR   PDB; 2W4Q; X-ray; 2.00 A; A=1-349.
DR   PDB; 2W98; X-ray; 1.85 A; A/B=1-349.
DR   PDB; 2ZB4; X-ray; 1.63 A; A=1-351.
DR   PDB; 2ZB7; X-ray; 1.80 A; A=1-351.
DR   PDB; 2ZB8; X-ray; 2.00 A; A=1-351.
DR   PDBsum; 2VNA; -.
DR   PDBsum; 2W4Q; -.
DR   PDBsum; 2W98; -.
DR   PDBsum; 2ZB4; -.
DR   PDBsum; 2ZB7; -.
DR   PDBsum; 2ZB8; -.
DR   SMR; Q8N8N7; 1-351.
DR   REPRODUCTION-2DPAGE; IPI00167515; -.
DR   PRIDE; Q8N8N7; -.
DR   Ensembl; ENSG00000140043; Homo sapiens.
DR   GeneID; 145482; -.
DR   KEGG; hsa:145482; -.
DR   UCSC; uc001xow.1; human.
DR   GeneCards; GC14P073389; -.
DR   H-InvDB; HIX0079548; -.
DR   H-InvDB; HIX0079612; -.
DR   HGNC; HGNC:20149; PTGR2.
DR   HPA; HPA000695; -.
DR   MIM; 608642; gene.
DR   PharmGKB; PA134976517; -.
DR   HOGENOM; Q8N8N7; -.
DR   HOVERGEN; Q8N8N7; -.
DR   OMA; Q8N8N7; GLENMGV.
DR   NextBio; 85108; -.
DR   ArrayExpress; Q8N8N7; -.
DR   Bgee; Q8N8N7; -.
DR   CleanEx; HS_PTGR2; -.
DR   GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase 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; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW   NADP; Oxidoreductase.
FT   CHAIN         1    351       Prostaglandin reductase 2.
FT                                /FTId=PRO_0000218070.
FT   NP_BIND     162    168       NADP (Potential).
FT   NP_BIND     188    208       NADP (Potential).
FT   VAR_SEQ     174    180       IGHFLGC -> VNFLRII (in isoform 2).
FT                                /FTId=VSP_013526.
FT   VAR_SEQ     181    351       Missing (in isoform 2).
FT                                /FTId=VSP_013527.
SQ   SEQUENCE   351 AA;  38499 MW;  118ED6D2FB984F3A CRC64;
     MIVQRVVLNS RPGKNGNPVA ENFRMEEVYL PDNINEGQVQ VRTLYLSVDP YMRCRMNEDT
     GTDYITPWQL SQVVDGGGIG IIEESKHTNL TKGDFVTSFY WPWQTKVILD GNSLEKVDPQ
     LVDGHLSYFL GAIGMPGLTS LIGIQEKGHI TAGSNKTMVV SGAAGACGSV AGQIGHFLGC
     SRVVGICGTH EKCILLTSEL GFDAAINYKK DNVAEQLRES CPAGVDVYFD NVGGNISDTV
     ISQMNENSHI ILCGQISQYN KDVPYPPPLS PAIEAIQKER NITRERFLVL NYKDKFEPGI
     LQLSQWFKEG KLKIKETVIN GLENMGAAFQ SMMTGGNIGK QIVCISEEIS L
//