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   27-MAR-2024, entry version 180.
DE   RecName: Full=3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7 {ECO:0000305};
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase 7;
DE            Short=17-beta-HSD 7;
DE   AltName: Full=3-keto-steroid reductase;
DE            EC=1.1.1.270 {ECO:0000269|PubMed:20659585};
DE   AltName: Full=Dihydrotestosterone oxidoreductase;
DE            EC=1.1.1.210 {ECO:0000269|PubMed:12732193};
DE   AltName: Full=Estradiol 17-beta-dehydrogenase 7;
DE            EC=1.1.1.62 {ECO:0000269|PubMed:9658408};
GN   Name=Hsd17b7; Synonyms=17hsd7 {ECO:0000303|PubMed:9658408};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Mammary gland;
RX   PubMed=9658408; DOI=10.1210/mend.12.7.0134;
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 as a
RT   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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT   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 dehydrogenase
RT   type 7.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, and Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12732193; DOI=10.1016/s0006-291x(03)00694-6;
RA   Toern S., Nokelainen P., Kurkela R., Pulkka A., Menjivar M., Ghosh S.,
RA   Coca-Prados M., Peltoketo H., Isomaa V., Vihko P.;
RT   "Production, purification, and functional analysis of recombinant human and
RT   mouse 17beta-hydroxysteroid dehydrogenase type 7.";
RL   Biochem. Biophys. Res. Commun. 305:37-45(2003).
RN   [8]
RP   CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12829805; DOI=10.1210/me.2002-0436;
RA   Marijanovic Z., Laubner D., Moeller G., Gege C., Husen B., Adamski J.,
RA   Breitling R.;
RT   "Closing the gap: identification of human 3-ketosteroid reductase, the last
RT   unknown enzyme of mammalian cholesterol biosynthesis.";
RL   Mol. Endocrinol. 17:1715-1725(2003).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18669642; DOI=10.1210/me.2008-0165;
RA   Shehu A., Mao J., Gibori G.B., Halperin J., Le J., Devi Y.S., Merrill B.,
RA   Kiyokawa H., Gibori G.;
RT   "Prolactin receptor-associated protein/17beta-hydroxysteroid dehydrogenase
RT   type 7 gene (Hsd17b7) plays a crucial role in embryonic development and
RT   fetal survival.";
RL   Mol. Endocrinol. 22:2268-2277(2008).
RN   [10]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=20659585; DOI=10.1016/j.bbalip.2010.07.006;
RA   Taramino S., Teske B., Oliaro-Bosso S., Bard M., Balliano G.;
RT   "Divergent interactions involving the oxidosqualene cyclase and the
RT   steroid-3-ketoreductase in the sterol biosynthetic pathway of mammals and
RT   yeasts.";
RL   Biochim. Biophys. Acta 1801:1232-1237(2010).
CC   -!- FUNCTION: Bifunctional enzyme involved in steroid-hormone metabolism
CC       and cholesterol biosynthesis (PubMed:9658408, PubMed:12732193,
CC       PubMed:12829805, PubMed:20659585). Catalyzes the NADP(H)-dependent
CC       reduction of estrogens and androgens and regulates the biological
CC       potency of these steroids. Converts estrone (E1)to a more potent
CC       estrogen, 17beta-estradiol (E2) (PubMed:9658408, PubMed:12732193).
CC       Converts moderately dihydrotestosterone (DHT) to their inactive forms
CC       5a-androstane-3beta,17b-diol and 5alpha-androstane-3alpha,17beta-diol
CC       (PubMed:12732193). Does not metabolize progesterone (PubMed:12732193).
CC       Additionally, participates in the post-squalene cholesterol
CC       biosynthesis, as a 3-ketosteroid reductase (PubMed:12829805,
CC       PubMed:20659585). {ECO:0000269|PubMed:12732193,
CC       ECO:0000269|PubMed:12829805, ECO:0000269|PubMed:20659585,
CC       ECO:0000269|PubMed:9658408}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62;
CC         Evidence={ECO:0000269|PubMed:12732193, ECO:0000269|PubMed:9658408};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24618;
CC         Evidence={ECO:0000305|PubMed:12732193, ECO:0000305|PubMed:9658408};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3beta-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) +
CC         NADPH; Xref=Rhea:RHEA:34787, ChEBI:CHEBI:15378, ChEBI:CHEBI:36836,
CC         ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.270; Evidence={ECO:0000269|PubMed:12829805,
CC         ECO:0000269|PubMed:20659585};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34789;
CC         Evidence={ECO:0000305|PubMed:12829805, ECO:0000305|PubMed:20659585};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-4alpha-methylzymosterol + H(+) + NADPH = 4alpha-
CC         methylzymosterol + NADP(+); Xref=Rhea:RHEA:36379, ChEBI:CHEBI:1949,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:136486; EC=1.1.1.270;
CC         Evidence={ECO:0000269|PubMed:20659585};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36380;
CC         Evidence={ECO:0000305|PubMed:20659585};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + zymosterone = NADP(+) + zymosterol;
CC         Xref=Rhea:RHEA:33459, ChEBI:CHEBI:15378, ChEBI:CHEBI:18252,
CC         ChEBI:CHEBI:52386, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000269|PubMed:12829805};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33460;
CC         Evidence={ECO:0000305|PubMed:12829805};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4alpha-methyl-5alpha-cholest-8-en-3-one + H(+) + NADPH =
CC         4alpha-methyl-5alpha-cholest-8-en-3beta-ol + NADP(+);
CC         Xref=Rhea:RHEA:46832, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:87050, ChEBI:CHEBI:87051;
CC         Evidence={ECO:0000305|PubMed:20659585};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46833;
CC         Evidence={ECO:0000305|PubMed:20659585};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP(+) = 4alpha-
CC         methyl-5alpha-cholest-7-en-3-one + H(+) + NADPH;
CC         Xref=Rhea:RHEA:18409, ChEBI:CHEBI:15378, ChEBI:CHEBI:16495,
CC         ChEBI:CHEBI:18378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.270; Evidence={ECO:0000250|UniProtKB:Q62904};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18411;
CC         Evidence={ECO:0000250|UniProtKB:Q62904};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-cholest-8-en-3-one + H(+) + NADPH = 5alpha-cholest-8-
CC         en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46852, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:87056; Evidence={ECO:0000250|UniProtKB:P56937};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46853;
CC         Evidence={ECO:0000250|UniProtKB:P56937};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-androstane-3alpha,17beta-diol + NADP(+) = 17beta-
CC         hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:42116,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000269|PubMed:12732193};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42118;
CC         Evidence={ECO:0000305|PubMed:12732193};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-androstane-3beta,17beta-diol + NADP(+) = 17beta-
CC         hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:16297,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.210;
CC         Evidence={ECO:0000269|PubMed:12732193};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16299;
CC         Evidence={ECO:0000305|PubMed:12732193};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.28 uM for estrone {ECO:0000269|PubMed:9658408};
CC         KM=12.87 uM for 17beta-estradiol {ECO:0000269|PubMed:9658408};
CC         KM=1.19 uM for estrone {ECO:0000269|PubMed:12732193};
CC         Vmax=556 pmol/min/mg enzyme with estrone as substrate
CC         {ECO:0000269|PubMed:9658408};
CC         Vmax=616 pmol/min/mg enzyme with 17beta-estradiol as substrate
CC         {ECO:0000269|PubMed:9658408};
CC   -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC       {ECO:0000269|PubMed:12732193, ECO:0000269|PubMed:9658408}.
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC       lanosterol: step 5/6. {ECO:0000269|PubMed:12829805}.
CC   -!- SUBUNIT: Binds to the short form of prolactin receptor.
CC       {ECO:0000250|UniProtKB:Q62904}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12829805}; Single-pass membrane protein
CC       {ECO:0000255}. Note=Colocalizes with HMGCR in a wide range of tissues
CC       during embryonic development. {ECO:0000269|PubMed:12829805}.
CC   -!- TISSUE SPECIFICITY: Most abundant in ovaries of pregnant animals.
CC       Present also in nonpregnant animals in ovaries, mammary gland liver,
CC       kidney and testis. {ECO:0000269|PubMed:9658408}.
CC   -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q62904}.
CC   -!- DISRUPTION PHENOTYPE: Death at embryonic day 10.5. Embryonic lethality
CC       is caused by severe brain malformation and heart defect.
CC       {ECO:0000269|PubMed:18669642}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. ERG27 subfamily. {ECO:0000305}.
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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; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF367475; AAM21211.1; -; Genomic_DNA.
DR   CCDS; CCDS35766.1; -.
DR   RefSeq; NP_034606.3; NM_010476.3.
DR   AlphaFoldDB; O88736; -.
DR   SMR; O88736; -.
DR   BioGRID; 200436; 5.
DR   IntAct; O88736; 1.
DR   STRING; 10090.ENSMUSP00000027989; -.
DR   SwissLipids; SLP:000001215; -.
DR   GlyCosmos; O88736; 4 sites, No reported glycans.
DR   GlyGen; O88736; 4 sites.
DR   iPTMnet; O88736; -.
DR   PhosphoSitePlus; O88736; -.
DR   SwissPalm; O88736; -.
DR   EPD; O88736; -.
DR   jPOST; O88736; -.
DR   MaxQB; O88736; -.
DR   PaxDb; 10090-ENSMUSP00000027989; -.
DR   PeptideAtlas; O88736; -.
DR   ProteomicsDB; 279355; -.
DR   Pumba; O88736; -.
DR   Antibodypedia; 34324; 184 antibodies from 26 providers.
DR   DNASU; 15490; -.
DR   Ensembl; ENSMUST00000027989.13; ENSMUSP00000027989.7; ENSMUSG00000026675.13.
DR   GeneID; 15490; -.
DR   KEGG; mmu:15490; -.
DR   UCSC; uc007dlp.1; mouse.
DR   AGR; MGI:1330808; -.
DR   CTD; 51478; -.
DR   MGI; MGI:1330808; Hsd17b7.
DR   VEuPathDB; HostDB:ENSMUSG00000026675; -.
DR   eggNOG; KOG1478; Eukaryota.
DR   GeneTree; ENSGT00390000013340; -.
DR   HOGENOM; CLU_029944_2_0_1; -.
DR   InParanoid; O88736; -.
DR   OMA; WHNIDGY; -.
DR   OrthoDB; 2787383at2759; -.
DR   TreeFam; TF105433; -.
DR   BRENDA; 1.1.1.270; 3474.
DR   BRENDA; 1.1.1.62; 3474.
DR   Reactome; R-MMU-191273; Cholesterol biosynthesis.
DR   UniPathway; UPA00769; -.
DR   UniPathway; UPA00770; UER00758.
DR   BioGRID-ORCS; 15490; 5 hits in 80 CRISPR screens.
DR   PRO; PR:O88736; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; O88736; Protein.
DR   Bgee; ENSMUSG00000026675; Expressed in vestibular epithelium and 234 other cell types or tissues.
DR   ExpressionAtlas; O88736; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0000253; F:3-keto sterol reductase activity; IDA:MGI.
DR   GO; GO:0047024; F:5alpha-androstane-3beta,17beta-diol dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase [NAD(P)] activity; IDA:UniProtKB.
DR   GO; GO:0005148; F:prolactin receptor binding; ISO:MGI.
DR   GO; GO:0008209; P:androgen metabolic process; IDA:UniProtKB.
DR   GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IDA:MGI.
DR   GO; GO:0048568; P:embryonic organ development; IMP:UniProtKB.
DR   GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI.
DR   GO; GO:0006703; P:estrogen biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   CDD; cd08941; 3KS_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR042829; HSD17B7/Erg27.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR44442; 3-KETO-STEROID REDUCTASE; 1.
DR   PANTHER; PTHR44442:SF1; 3-KETO-STEROID REDUCTASE_17-BETA-HYDROXYSTEROID DEHYDROGENASE 7; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   Genevisible; O88736; MM.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; NAD; NADP; Oxidoreductase; Reference proteome;
KW   Steroid biosynthesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..334
FT                   /note="3-keto-steroid reductase/17-beta-hydroxysteroid
FT                   dehydrogenase 7"
FT                   /id="PRO_0000054587"
FT   TOPO_DOM        1..229
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..334
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         8..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        160
FT                   /note="A -> V (in Ref. 2; CAC88119 and 4; BC011464)"
FT                   /evidence="ECO:0000305"
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
//