ID   AKC1H_RAT               Reviewed;         323 AA.
AC   P51652; Q498E4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=Aldo-keto reductase family 1 member C18;
DE            EC=1.1.-.-;
DE   AltName: Full=20-alpha-hydroxysteroid dehydrogenase;
DE            Short=20-alpha-HSD;
DE            EC=1.1.1.149;
DE   AltName: Full=HSD1;
GN   Name=Akr1c18;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 257-269 AND
RP   315-323.
RC   STRAIN=Sprague-Dawley; TISSUE=Corpus luteum;
RX   MEDLINE=94296401; PubMed=8024573; DOI=10.1006/bbrc.1994.1844;
RA   Mao J., Duan W.R., Albarracin C.T., Parmer T.G., Gibori G.;
RT   "Isolation and characterization of a rat luteal cDNA encoding 20
RT   alpha-hydroxysteroid dehydrogenase.";
RL   Biochem. Biophys. Res. Commun. 201:1289-1295(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar Imamichi; TISSUE=Ovary;
RX   MEDLINE=94226624; PubMed=8172618;
RA   Miura R., Shiota K., Noda K., Yagi S., Ogawa T., Takahashi M.;
RT   "Molecular cloning of cDNA for rat ovarian 20 alpha-hydroxysteroid
RT   dehydrogenase (HSD1).";
RL   Biochem. J. 299:561-567(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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   [4]
RP   PROTEIN SEQUENCE OF 233-243; 252-269 AND 315-323.
RC   STRAIN=Sprague-Dawley; TISSUE=Corpus luteum;
RX   MEDLINE=94252249; PubMed=8194472; DOI=10.1210/en.134.6.2453;
RA   Albarracin C.T., Parmer T.G., Duan W.R., Nelson S.E., Gibori G.;
RT   "Identification of a major prolactin-regulated protein as 20 alpha-
RT   hydroxysteroid dehydrogenase: coordinate regulation of its activity,
RT   protein content, and messenger ribonucleic acid expression.";
RL   Endocrinology 134:2453-2460(1994).
RN   [5]
RP   PROTEIN SEQUENCE OF 3-21.
RA   Noda K., Shiota K., Ogawa T., Yagi S., Takahashi M.;
RL   J. Reprod. Dev. 39:169-173(1993).
CC   -!- FUNCTION: Catalyzes the conversion of progesterone into 20-alpha-
CC       dihydroprogesterone (20 alpha-OHP).
CC   -!- CATALYTIC ACTIVITY: 17-alpha,20-alpha-dihydroxypregn-4-en-3-one +
CC       NAD(P)(+) = 17-alpha-hydroxyprogesterone + NAD(P)H.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Corpus luteum (large luteal cells).
CC   -!- DEVELOPMENTAL STAGE: Remains repressed throughout pregnancy and
CC       becomes highly and rapidly expressed before parturition.
CC   -!- INDUCTION: Repressed by prolactin.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
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DR   EMBL; L32601; AAA40601.1; -; mRNA.
DR   EMBL; D14424; BAA03317.1; -; mRNA.
DR   EMBL; BC100248; AAI00249.1; -; mRNA.
DR   IPI; IPI00204302; -.
DR   PIR; JC2330; JC2330.
DR   RefSeq; NP_612519.1; -.
DR   UniGene; Rn.10030; -.
DR   HSSP; P23457; 1LWI.
DR   SMR; P51652; 6-323.
DR   PRIDE; P51652; -.
DR   Ensembl; ENSRNOG00000017531; Rattus norvegicus.
DR   GeneID; 171516; -.
DR   KEGG; rno:171516; -.
DR   RGD; 708428; LOC171516.
DR   HOVERGEN; P51652; -.
DR   OMA; P51652; GTQRYKY.
DR   BRENDA; 1.1.1.149; 248.
DR   NextBio; 622481; -.
DR   ArrayExpress; P51652; -.
DR   GermOnline; ENSRNOG00000017531; Rattus norvegicus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0047006; F:20-alpha-hydroxysteroid dehydrogenase activity; IDA:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0042448; P:progesterone metabolic process; IDA:MGI.
DR   GO; GO:0050810; P:regulation of steroid biosynthetic process; IDA:RGD.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase.
FT   CHAIN         1    323       Aldo-keto reductase family 1 member C18.
FT                                /FTId=PRO_0000124650.
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         54     54       Important for substrate specificity (By
FT                                similarity).
FT   SITE         84     84       Lowers pKa of active site Tyr (By
FT                                similarity).
FT   CONFLICT    242    242       C -> L (in Ref. 4; AA sequence).
SQ   SEQUENCE   323 AA;  37300 MW;  D14270961515195E CRC64;
     MNSKIQKMEL NDGHSIPVLG FGTYATEENL RKKSMESTKI AIDVGFRHID CSHLYQNEEE
     IGQAIVSKIE DGTVKREDIF YTSKLWSTSH RPELVRPSLE NSLRKLNLDY VDLYLIHFPV
     SLKPGDELLP QDEHGNLILD TVDLCDTWEA MEKCKDAGLA KSIGVSNFNR RQLEKILNKP
     GLKHRPVCNQ VECHLYLNQS KLLAYCKMND IVLVAYGALG TQRYKYCINE DTPVLLDDPI
     LCTMAKKYKR TPALIALRYQ LERGIVTLVK SFNEERIREN LQVFDFQLAS DDMEILDNLD
     RNLRYFPANM FKAHPNFPFS DEY
//