ID   DHB7_MOUSE              Reviewed;         334 AA.
AC   O88736; Q8K5C9; Q921L1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 72.
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;
GN   Name=Hsd17b7;
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=Mammary gland;
RX   MEDLINE=98322544; PubMed=9658408; DOI=10.1210/me.12.7.1048;
RA   Nokelainen P., Peltoketo H., Vihko R., Vihko P.;
RT   "Expression cloning of a novel estrogenic mouse 17 beta-hydroxysteroid
RT   dehydrogenase/17-ketosteroid reductase (m17HSD7), previously described
RT   as a prolactin receptor-associated protein (PRAP) in rat.";
RL   Mol. Endocrinol. 12:1048-1059(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nokelainen P., Vihko P.;
RT   "Characterization of mouse 17beta-hydroxysteroid dehydrogenase type 7
RT   gene.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [5]
RP   NUCLEOTIDE SEQUENCE OF 1-301.
RA   Ohnesorg T., Adamski J.;
RT   "Characterization of mouse gene for 17-beta-hydroxysteroid
RT   dehydrogenase type 7.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Most abundant in ovaries of pregnant animals.
CC       Present also in nonpregnant animals in ovaries, mammary gland,
CC       liver, kidney and testis.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. ERG27 subfamily.
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DR   EMBL; Y15733; CAA75742.1; -; mRNA.
DR   EMBL; AJ291459; CAC88119.1; -; Genomic_DNA.
DR   EMBL; AJ291460; CAC88119.1; JOINED; Genomic_DNA.
DR   EMBL; AJ291461; CAC88119.1; JOINED; Genomic_DNA.
DR   EMBL; AJ291463; CAC88119.1; JOINED; Genomic_DNA.
DR   EMBL; AJ291465; CAC88119.1; JOINED; Genomic_DNA.
DR   EMBL; AJ291466; CAC88119.1; JOINED; Genomic_DNA.
DR   EMBL; AJ291464; CAC88119.1; JOINED; Genomic_DNA.
DR   EMBL; AJ291462; CAC88119.1; JOINED; Genomic_DNA.
DR   EMBL; AK028380; BAC25918.1; -; mRNA.
DR   EMBL; AK050211; BAC34124.1; -; mRNA.
DR   EMBL; BC011464; AAH11464.1; -; mRNA.
DR   EMBL; AF367475; AAM21211.1; -; Genomic_DNA.
DR   IPI; IPI00316067; -.
DR   RefSeq; NP_034606.3; -.
DR   UniGene; Mm.12882; -.
DR   PRIDE; O88736; -.
DR   Ensembl; ENSMUSG00000026675; Mus musculus.
DR   GeneID; 15490; -.
DR   KEGG; mmu:15490; -.
DR   MGI; MGI:1330808; Hsd17b7.
DR   HOGENOM; O88736; -.
DR   HOVERGEN; O88736; -.
DR   OMA; O88736; FDIWNSA.
DR   BRENDA; 1.1.1.270; 244.
DR   BRENDA; 1.1.1.62; 244.
DR   NextBio; 288362; -.
DR   ArrayExpress; O88736; -.
DR   Bgee; O88736; -.
DR   CleanEx; MM_HSD17B7; -.
DR   GermOnline; ENSMUSG00000026675; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000253; F:3-keto sterol reductase activity; IDA:MGI.
DR   GO; GO:0050576; F:3-keto-steroid reductase activity; IEA:EC.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IDA:MGI.
DR   GO; GO:0055114; P:oxidation reduction; 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   PROSITE; PS00061; ADH_SHORT; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Lipid synthesis; Membrane; NAD; NADP;
KW   Oxidoreductase; Steroid biosynthesis; Transmembrane.
FT   CHAIN         1    334       3-keto-steroid reductase.
FT                                /FTId=PRO_0000054587.
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    127    127       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    178    178       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    229    229       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    160    160       A -> V (in Ref. 2 and 4).
SQ   SEQUENCE   334 AA;  37317 MW;  E05F0716465BC160 CRC64;
     MRKVVLITGA SSGIGLALCG RLLAEDDDLH LCLACRNLSK ARAVRDTLLA SHPSAEVSIV
     QMDVSSLQSV VRGAEEVKQK FQRLDYLYLN AGILPNPQFN LKAFFCGIFS RNVIHMFTTA
     EGILTQNDSV TADGLQEVFE TNLFGHFILI RELEPLLCHA DNPSQLIWTS SRNAKKANFS
     LEDIQHSKGP EPYSSSKYAT DLLNVALNRN FNQKGLYSSV MCPGVVMTNM TYGILPPFIW
     TLLLPIMWLL RFFVNALTVT PYNGAEALVW LFHQKPESLN PLTKYASATS GFGTNYVTGQ
     KMDIDEDTAE KFYEVLLELE KRVRTTVQKS DHPS
//