ID   DHB12_RAT               Reviewed;         312 AA.
AC   Q6P7R8; Q9Z1B9;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 45.
DE   RecName: Full=Estradiol 17-beta-dehydrogenase 12;
DE            EC=1.1.1.62;
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase 12;
DE            Short=17-beta-HSD 12;
DE   AltName: Full=3-ketoacyl-CoA reductase;
DE            Short=KAR;
DE            EC=1.3.1.-;
GN   Name=Hsd17b12;
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].
RA   Trzyna W.C., Gabbeta V., McHugh K.M.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary anterior lobe;
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: Catalyzes the transformation of estrone (E1) into
CC       estradiol (E2), suggesting a central role in estrogen formation.
CC       Its strong expression in ovary and mammary gland suggest that it
CC       may constitute the major enzyme responsible for the conversion of
CC       E1 to E2 in females. Also has 3-ketoacyl-CoA reductase activity,
CC       reducing both long chain 3-ketoacyl-CoAs and long chain fatty
CC       acyl-CoAs, suggesting a role in long fatty acid elongation (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)(+) = estrone +
CC       NAD(P)H.
CC   -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC       localization for type I membrane proteins (By similarity).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. 17-beta-HSD 3 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD00504.1; Type=Frameshift; Positions=272;
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DR   EMBL; U81186; AAD00504.1; ALT_FRAME; mRNA.
DR   EMBL; BC061543; AAH61543.1; -; mRNA.
DR   IPI; IPI00208645; -.
DR   RefSeq; NP_114455.1; -.
DR   UniGene; Rn.203283; -.
DR   PhosphoSite; Q6P7R8; -.
DR   PRIDE; Q6P7R8; -.
DR   Ensembl; ENSRNOG00000009630; Rattus norvegicus.
DR   GeneID; 84013; -.
DR   KEGG; rno:84013; -.
DR   NMPDR; fig|10116.3.peg.19242; -.
DR   RGD; 708367; Hsd17b12.
DR   HOVERGEN; Q6P7R8; -.
DR   OMA; Q6P7R8; YPEYFLD.
DR   BRENDA; 1.1.1.62; 248.
DR   NextBio; 616547; -.
DR   ArrayExpress; Q6P7R8; -.
DR   GermOnline; ENSRNOG00000009630; Rattus norvegicus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid synthesis; Membrane; NADP;
KW   Oxidoreductase; Steroid biosynthesis; Transmembrane.
FT   CHAIN         1    312       Estradiol 17-beta-dehydrogenase 12.
FT                                /FTId=PRO_0000248370.
FT   TRANSMEM      4     24       Potential.
FT   TRANSMEM    182    202       Potential.
FT   TRANSMEM    271    291       Potential.
FT   NP_BIND      50     79       NADP (By similarity).
FT   MOTIF       308    312       Di-lysine motif (By similarity).
FT   ACT_SITE    202    202       Proton acceptor (By similarity).
FT   BINDING     189    189       Substrate (By similarity).
FT   CONFLICT    236    236       A -> S (in Ref. 1; AAD00504).
SQ   SEQUENCE   312 AA;  34841 MW;  8531943458EFC711 CRC64;
     MERALPAAGF LYWVGASTIA YLTLRASYSL FRAFQVWCVG NQAFVGPRLG EWAVVTGGTD
     GIGKSYAEEL AKRGMKIVLI SRSQDKLKEV SNNIKEKFNV ETRTIAVDFS LDDIYDKIKT
     GLSGLEIGVL VNNVGMSYEY PEYFLEIPDL DNTIKKLINI NVLSICKVTR LVLPGMVERS
     KGVILNISSA SGMLPVPLLT VYSATKAFVD FFSQCLHEEY KSKGIFVQSV LPFFVATKLA
     KIRKPTLDKP SAETFVKSAI KTVGLQTRTT GYVIHAIMGS INSILPRWIY FKTIMGFNKS
     LRNRYLKKTK KN
//