ID   DHB7_RAT                Reviewed;         334 AA.
AC   Q62904;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   04-NOV-2008, entry version 65.
DE   RecName: Full=3-keto-steroid reductase;
DE            EC=1.1.1.270;
DE   AltName: Full=Estradiol 17-beta-dehydrogenase 7;
DE            EC=1.1.1.62;
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase 7;
DE            Short=17-beta-HSD 7;
DE   AltName: Full=PRL receptor-associated protein;
DE            Short=PRAP;
GN   Name=Hsd17b7;
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 1-18.
RC   STRAIN=Sprague-Dawley; TISSUE=Corpus luteum;
RX   MEDLINE=96279080; PubMed=8663045; DOI=10.1074/jbc.271.26.15602;
RA   Duan W.R., Linzer D.I.H., Gibori G.;
RT   "Cloning and characterization of an ovarian-specific protein that
RT   associates with the short form of the prolactin receptor.";
RL   J. Biol. Chem. 271:15602-15607(1996).
CC   -!- FUNCTION: Responsible for the reduction of the keto group on the
CC       C-3 of sterols.
CC   -!- CATALYTIC ACTIVITY: 4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol
CC       + NADP(+) = 4-alpha-methyl-5-alpha-cholest-7-en-3-one + NADPH.
CC   -!- CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)(+) = estrone +
CC       NAD(P)H.
CC   -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol
CC       from lanosterol: step 5/6.
CC   -!- SUBUNIT: Binds to the short form of prolactin receptor.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Most abundant in ovaries of pregnant animals.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. ERG27 subfamily.
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DR   EMBL; U44803; AAC52623.1; -; mRNA.
DR   RefSeq; NP_058931.1; -.
DR   UniGene; Rn.7040; -.
DR   Ensembl; ENSRNOG00000002826; Rattus norvegicus.
DR   GeneID; 29540; -.
DR   KEGG; rno:29540; -.
DR   RGD; 2837; Hsd17b7.
DR   HOVERGEN; Q62904; -.
DR   NextBio; 609535; -.
DR   ArrayExpress; Q62904; -.
DR   GermOnline; ENSRNOG00000002826; Rattus norvegicus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050576; F:3-keto-steroid reductase activity; IEA:EC.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DHase_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DHase.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PROSITE; PS00061; ADH_SHORT; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Lipid synthesis; Membrane;
KW   NAD; NADP; Oxidoreductase; Steroid biosynthesis; Transmembrane.
FT   CHAIN         1    334       3-keto-steroid reductase.
FT                                /FTId=PRO_0000054588.
FT   TOPO_DOM      1    229       Extracellular (Potential).
FT   TRANSMEM    230    250       Potential.
FT   TOPO_DOM    251    334       Cytoplasmic (Potential).
FT   NP_BIND       8     15       NAD (Potential).
FT   ACT_SITE    193    193       Proton acceptor (By similarity).
FT   BINDING     171    171       Substrate (By similarity).
FT   CARBOHYD     37     37       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    178    178       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    229    229       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   334 AA;  37372 MW;  448B546CE8FCBFAC CRC64;
     MRKVVLITGA SSGIGLALCG RLLAEDDDLH LCLACRNLSK AGAVRDALLA SHPSAEVSIV
     QMDVSNLQSV VRGAEEVKRR FQRLDYLYLN AGIMPNPQLN LKAFFCGIFS RNVIHMFSTA
     EGLLTQNDKI TADGFQEVFE TNLFGHFILI RELEPLLCHS DNPSQLIWTS SRNAKKSNFS
     LEDIQHAKGQ EPYSSSKYAT DLLNVALNRN FNQKGLYSSV TCPGVVMTNL TYGILPPFVW
     TLLLPVIWLL RFFAHAFTVT PYNGAEALVW LFHQKPESLN PLTKYLSGTT GLGTNYVKGQ
     KMDVDEDTAE KFYKTLLELE KQVRITIQKS DHHS
//