ID   DHB12_ANAPL             Reviewed;         312 AA.
AC   O57314;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 42.
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;
GN   Name=HSD17B12; Synonyms=SPM2;
OS   Anas platyrhynchos (Domestic duck) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Anseriformes; Anatidae; Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Forebrain;
RA   Kimura N., Kurosawa N., Kondo K., Tsukada Y.;
RT   "Molecular cloning of SPM2 from duckling brain: a putative brain
RT   specific steroid dehydrogenase and its induction by imprinting
RT   stimuli.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transformation of estrone (E1) into
CC       estradiol (E2), suggesting a central role in estrogen formation
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)(+) = estrone +
CC       NAD(P)H.
CC   -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. 17-beta-HSD 3 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB009304; BAA23765.1; -; mRNA.
DR   HOVERGEN; O57314; -.
DR   BRENDA; 1.1.1.62; 3217.
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_0000054577.
FT   TRANSMEM     33     53       Potential.
FT   TRANSMEM    181    201       Potential.
FT   TRANSMEM    274    294       Potential.
FT   NP_BIND      48     77       NADP (By similarity).
FT   ACT_SITE    201    201       Proton acceptor (By similarity).
FT   BINDING     188    188       Substrate (By similarity).
SQ   SEQUENCE   312 AA;  33896 MW;  744D8F44491A9262 CRC64;
     MLPAAGLLWW VGALGALYAA VRGALGLLGA LRVWGIGAGR AALGPGLGAW AVVTGATDGI
     GKAYAKELAK RGMKVALISR SKEKLDQVAG EITEQYGVET KVIVADFGER EDIYDRIRAG
     LEGLEIGVLV NNVGISYSYP EYFIDVPDLD KTIDKMININ IMSVCKMTRL VLPGMLERSK
     GVILNISSAA GMYPTPLLTL YSASKAFVDY FSRGLHAEYK SKGIIVQSVM PYYVATKMSK
     ISKPSFDKPT PETYVRAAIG TVGLQSQTNG CLPHAFMGWV FSILPTSTVM NLLMKTNKQI
     RARFLKKKMK EK
//