ID   DHB2_MOUSE              Reviewed;         381 AA.
AC   P51658; O08898;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-NOV-2008, entry version 68.
DE   RecName: Full=Estradiol 17-beta-dehydrogenase 2;
DE            EC=1.1.1.62;
DE   AltName: Full=Testosterone 17-beta-dehydrogenase;
DE            EC=1.1.1.63;
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase 2;
DE            Short=17-beta-HSD 2;
GN   Name=Hsd17b2; Synonyms=Edh17b2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=97344259; PubMed=9224647;
RA   Mustonen M.;
RT   "Cloning of mouse 17beta-hydroxysteroid dehydrogenase type 2, and
RT   analysing expression of the mRNAs for types 1, 2, 3, 4 and 5 in mouse
RT   embryos and adult tissues.";
RL   Biochem. J. 325:199-205(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-358.
RC   STRAIN=BALB/c;
RA   Stoffel W., Weiss B.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Capable of catalyzing the interconversion of
CC       testosterone and androstenedione, as well as estradiol and
CC       estrone. Also has 20-alpha-HSD activity. Uses NADH while EDH17B3
CC       uses NADPH (By similarity).
CC   -!- CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)(+) = estrone +
CC       NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: Testosterone + NAD(+) = androst-4-ene-3,17-
CC       dione + NADH.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; Y09517; CAA70706.1; -; mRNA.
DR   EMBL; X95685; CAA64982.1; -; mRNA.
DR   RefSeq; NP_032316.2; -.
DR   UniGene; Mm.276466; -.
DR   HSSP; P14061; 1FDS.
DR   PhosphoSite; P51658; -.
DR   Ensembl; ENSMUSG00000031844; Mus musculus.
DR   GeneID; 15486; -.
DR   KEGG; mmu:15486; -.
DR   MGI; MGI:1096386; Hsd17b2.
DR   HOGENOM; P51658; -.
DR   HOVERGEN; P51658; -.
DR   NextBio; 288350; -.
DR   ArrayExpress; P51658; -.
DR   CleanEx; MM_HSD17B2; -.
DR   GermOnline; ENSMUSG00000031844; Mus musculus.
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:0050327; F:testosterone 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; 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   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Lipid synthesis; Membrane; NAD; Oxidoreductase; Signal-anchor;
KW   Steroid biosynthesis; Transmembrane.
FT   CHAIN         1    381       Estradiol 17-beta-dehydrogenase 2.
FT                                /FTId=PRO_0000054571.
FT   TRANSMEM      4     24       Signal-anchor for type II membrane
FT                                protein (Potential).
FT   NP_BIND      83    112       NAD (By similarity).
FT   ACT_SITE    233    233       Proton acceptor (By similarity).
FT   BINDING     220    220       Substrate (By similarity).
FT   CONFLICT     36     37       QA -> RP (in Ref. 2; CAA64982).
SQ   SEQUENCE   381 AA;  41836 MW;  74A62797947E6086 CRC64;
     MSPFASESAW LCLAAAAVLG GTLLCGCRSG RQLRSQAVCL AGLWGGACLL SLSLLCTLFL
     LSVACFLLLY MSSSDQDLLP VDQKAVLVTG ADSGFGHGLA KHLDKLGFTV FAGVLDKEGP
     GAEELRKHCS ERLSVLQMDV TKPEQIKDAH SKVTEKIQDK GLWAVVNNAG VFHLPIDGEL
     IPMSIYRKCM AVNFFGTVEV TKAFLPLLRK SKGRLVNVSS MGGTVPLQMT SAYAATKAAL
     TMFSTIIRQE LDKWGVKVVT IKPGGFKTNI TGSQDIWDKM EKEILDHFSK DIQENYGQDY
     VHTQKLIIPT LKERSNPDIT PVLRDIQHAI SARNPSSFYY PGRMAYLWVC LAAYCPTSLL
     DYVIKKGFYP QPTPRALRTV H
//