DHB7_MOUSE
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 03-AUG-2022, entry version 171.
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; 4.
DR IntAct; O88736; 1.
DR STRING; 10090.ENSMUSP00000027989; -.
DR SwissLipids; SLP:000001215; -.
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; O88736; -.
DR PeptideAtlas; O88736; -.
DR PRIDE; O88736; -.
DR ProteomicsDB; 279355; -.
DR Antibodypedia; 34324; 170 antibodies from 26 providers.
DR DNASU; 15490; -.
DR Ensembl; ENSMUST00000027989; ENSMUSP00000027989; ENSMUSG00000026675.
DR GeneID; 15490; -.
DR KEGG; mmu:15490; -.
DR UCSC; uc007dlp.1; mouse.
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; RRGTQPY; -.
DR OrthoDB; 1413827at2759; -.
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 75 CRISPR screens.
DR PRO; PR:O88736; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O88736; protein.
DR Bgee; ENSMUSG00000026675; Expressed in vestibular epithelium and 231 other tissues.
DR ExpressionAtlas; O88736; baseline and differential.
DR Genevisible; O88736; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
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:0102176; F:cycloeucalenone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase 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 GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR CDD; cd08941; 3KS_SDR_c; 1.
DR InterPro; IPR042829; HSD17B7/Erg27.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
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
