ID DHB7_HUMAN Reviewed; 341 AA. AC P56937; Q5T246; Q7Z4V9; Q8WWS2; Q9UF00; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 208. 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:11165030, ECO:0000269|PubMed:12829805, ECO:0000269|PubMed:20659585}; DE AltName: Full=Dihydrotestosterone oxidoreductase; DE EC=1.1.1.210 {ECO:0000269|PubMed:12574203, ECO:0000269|PubMed:12732193, ECO:0000269|PubMed:19772289}; DE AltName: Full=Estradiol 17-beta-dehydrogenase 7; DE EC=1.1.1.62 {ECO:0000269|PubMed:12574203, ECO:0000269|PubMed:12732193, ECO:0000269|PubMed:19772289}; DE AltName: Full=Short chain dehydrogenase/reductase family 37C member 1; GN Name=HSD17B7; Synonyms=17HSD7 {ECO:0000303|PubMed:12732193}, SDR37C1; GN ORFNames=UNQ2563/PRO6243; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). RX PubMed=10544267; DOI=10.1016/s0014-5793(99)01366-6; RA Krazeisen A., Breitling R., Imai K., Fritz S., Moeller G., Adamski J.; RT "Determination of cDNA, gene structure and chromosomal localization of the RT novel human 17beta-hydroxysteroid dehydrogenase type 7."; RL FEBS Lett. 460:373-379(1999). RN [2] RP SEQUENCE REVISION. RA Krazeisen A., Breitling R., Imai K., Fritz S., Moeller G., Adamski J.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3), CATALYTIC RP ACTIVITY, FUNCTION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RC TISSUE=Placenta; 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Zhou Y., Yu L., Zhao S.Y.; RT "Cloning of a new human cDNA homologous to Rattus norvegicus ovarian- RT specific protein."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin, and Urinary bladder; 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 [11] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=11165030; DOI=10.1016/s0303-7207(00)00416-0; RA Breitling R., Krazeisen A., Moeller G., Adamski J.; RT "17beta-hydroxysteroid dehydrogenase type 7--an ancient 3-ketosteroid RT reductase of cholesterogenesis."; RL Mol. Cell. Endocrinol. 171:199-204(2001). RN [12] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=12574203; DOI=10.1210/jc.2002-020236; RA Haerkoenen P., Toern S., Kurkela R., Porvari K., Pulkka A., Lindfors A., RA Isomaa V., Vihko P.; RT "Sex hormone metabolism in prostate cancer cells during transition to an RT androgen-independent state."; RL J. Clin. Endocrinol. Metab. 88:705-712(2003). RN [13] 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 [14] RP ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=19772289; DOI=10.1021/jm900921c; RA Bellavance E., Luu-The V., Poirier D.; RT "Potent and selective steroidal inhibitors of 17beta-hydroxysteroid RT dehydrogenase type 7, an enzyme that catalyzes the reduction of the key RT hormones estrone and dihydrotestosterone."; RL J. Med. Chem. 52:7488-7502(2009). RN [15] 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). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Bifunctional enzyme involved in steroid-hormone metabolism CC and cholesterol biosynthesis (PubMed:12574203, PubMed:12732193, CC PubMed:12829805, PubMed:20659585, PubMed:19772289, PubMed:11165030). CC Catalyzes the NADP(H)-dependent reduction of estrogens and androgens CC and regulates the biological potency of these steroids. Converts CC estrone (E1) to a more potent estrogen, 17beta-estradiol (E2) CC (PubMed:12574203, PubMed:12732193, PubMed:19772289). Converts CC dihydrotestosterone (DHT) to its inactive form 5a-androstane-3b,17b- CC diol (PubMed:12574203, PubMed:12732193, PubMed:19772289). Converts CC moderately progesterone to 3beta-hydroxypregn-4-ene-20-one, leading to CC its inactivation (PubMed:12574203, PubMed:12732193). Additionally, CC participates in the post-squalene cholesterol biosynthesis, as a 3- CC ketosteroid reductase (PubMed:12829805, PubMed:20659585, CC PubMed:11165030). {ECO:0000269|PubMed:11165030, CC ECO:0000269|PubMed:12574203, ECO:0000269|PubMed:12732193, CC ECO:0000269|PubMed:12829805, ECO:0000269|PubMed:19772289, CC ECO:0000269|PubMed:20659585}. CC -!- FUNCTION: [Isoform 3]: Does not have enzymatic activities toward E1 and CC DHT. {ECO:0000269|PubMed:12732193}. 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:12574203, ECO:0000269|PubMed:12732193, CC ECO:0000269|PubMed:19772289}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24618; CC Evidence={ECO:0000305|PubMed:12574203, ECO:0000305|PubMed:12732193}; 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:11165030, ECO:0000269|PubMed:12829805}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33460; CC Evidence={ECO:0000305|PubMed:11165030, 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:0000269|PubMed:11165030}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46853; CC Evidence={ECO:0000305|PubMed:11165030}; 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:12574203, ECO:0000269|PubMed:12732193, CC ECO:0000269|PubMed:19772289}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16299; CC Evidence={ECO:0000269|PubMed:12732193, ECO:0000305|PubMed:12574203}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + NADPH + progesterone = 3beta-hydroxypregn-4-ene-20-one CC + NADP(+); Xref=Rhea:RHEA:46216, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17026, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:85899; Evidence={ECO:0000269|PubMed:12574203, CC ECO:0000269|PubMed:12732193}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46217; CC Evidence={ECO:0000305|PubMed:12574203, ECO:0000305|PubMed:12732193}; CC -!- ACTIVITY REGULATION: Estradiol 17-beta-dehydrogenase and CC dihydrotestosterone oxidoreductase activities are selectively inhibited CC by 4-methyl-4-aza-5alpha-androstane derivatives, such as 17beta-[(N- CC Heptyl)methylamino]-4-aza-5r-androstan-3-one and 17beta-(N- CC Decylformamido)-4-aza-5r-androstan-3-one. CC {ECO:0000269|PubMed:19772289}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.25 uM for estrone {ECO:0000269|PubMed:12732193}; CC KM=2.6 uM for 17beta-hydroxy-5alpha-androstan-3-one CC {ECO:0000269|PubMed:12732193}; CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis. CC {ECO:0000269|PubMed:12574203, ECO:0000269|PubMed:12732193, CC ECO:0000269|PubMed:19772289}. CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from CC lanosterol: step 5/6. {ECO:0000269|PubMed:11165030, CC 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}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P56937-1; Sequence=Displayed; CC Name=2; CC IsoId=P56937-2; Sequence=VSP_006029; CC Name=3; CC IsoId=P56937-3; Sequence=VSP_012766; CC -!- TISSUE SPECIFICITY: Highly expressed in adrenal gland, liver, lung and CC thymus. Expressed in breast, ovaries, pituitary gland, pregnant uterus, CC prostate, kidney, lymph node, small intestine, spinal cord and trachea. CC Weakly expressed in all other tissues tested. CC {ECO:0000269|PubMed:12732193}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in eye ciliary epithelial CC cells and neuroendocrine cells. {ECO:0000269|PubMed:12732193}. CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q62904}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. ERG27 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF098786; AAF09266.2; -; mRNA. DR EMBL; AF162767; AAF14537.1; -; Genomic_DNA. DR EMBL; AF162759; AAF14537.1; JOINED; Genomic_DNA. DR EMBL; AF162760; AAF14537.1; JOINED; Genomic_DNA. DR EMBL; AF162761; AAF14537.1; JOINED; Genomic_DNA. DR EMBL; AF162762; AAF14537.1; JOINED; Genomic_DNA. DR EMBL; AF162763; AAF14537.1; JOINED; Genomic_DNA. DR EMBL; AF162764; AAF14537.1; JOINED; Genomic_DNA. DR EMBL; AF162765; AAF14537.1; JOINED; Genomic_DNA. DR EMBL; AF162766; AAF14537.1; JOINED; Genomic_DNA. DR EMBL; AJ249179; CAC20418.1; -; mRNA. DR EMBL; AJ250550; CAC88111.1; -; Genomic_DNA. DR EMBL; AJ250551; CAC88111.1; JOINED; Genomic_DNA. DR EMBL; AJ250552; CAC88111.1; JOINED; Genomic_DNA. DR EMBL; AJ250553; CAC88111.1; JOINED; Genomic_DNA. DR EMBL; AJ250554; CAC88111.1; JOINED; Genomic_DNA. DR EMBL; AJ250555; CAC88111.1; JOINED; Genomic_DNA. DR EMBL; AJ250556; CAC88111.1; JOINED; Genomic_DNA. DR EMBL; AJ250557; CAC88111.1; JOINED; Genomic_DNA. DR EMBL; AJ250558; CAC88111.1; JOINED; Genomic_DNA. DR EMBL; AF145023; AAP97275.1; -; mRNA. DR EMBL; AY358962; AAQ89321.1; -; mRNA. DR EMBL; AK290741; BAF83430.1; -; mRNA. DR EMBL; BT007075; AAP35738.1; -; mRNA. DR EMBL; AL392003; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL445197; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW90716.1; -; Genomic_DNA. DR EMBL; BC007068; AAH07068.1; -; mRNA. DR EMBL; BC065246; AAH65246.1; -; mRNA. DR CCDS; CCDS1242.1; -. [P56937-1] DR RefSeq; NP_001291441.1; NM_001304512.1. DR RefSeq; NP_001291442.1; NM_001304513.1. DR RefSeq; NP_057455.1; NM_016371.3. [P56937-1] DR AlphaFoldDB; P56937; -. DR SMR; P56937; -. DR BioGRID; 119563; 37. DR IntAct; P56937; 14. DR STRING; 9606.ENSP00000254521; -. DR BindingDB; P56937; -. DR ChEMBL; CHEMBL5999; -. DR DrugBank; DB00157; NADH. DR SwissLipids; SLP:000001214; -. DR GlyCosmos; P56937; 3 sites, No reported glycans. DR GlyGen; P56937; 3 sites. DR iPTMnet; P56937; -. DR PhosphoSitePlus; P56937; -. DR SwissPalm; P56937; -. DR BioMuta; HSD17B7; -. DR DMDM; 8134404; -. DR EPD; P56937; -. DR jPOST; P56937; -. DR MassIVE; P56937; -. DR MaxQB; P56937; -. DR PaxDb; 9606-ENSP00000254521; -. DR PeptideAtlas; P56937; -. DR ProteomicsDB; 56957; -. [P56937-1] DR ProteomicsDB; 56958; -. [P56937-2] DR ProteomicsDB; 56959; -. [P56937-3] DR Pumba; P56937; -. DR Antibodypedia; 34324; 184 antibodies from 26 providers. DR DNASU; 51478; -. DR Ensembl; ENST00000254521.8; ENSP00000254521.3; ENSG00000132196.16. [P56937-1] DR GeneID; 51478; -. DR KEGG; hsa:51478; -. DR MANE-Select; ENST00000254521.8; ENSP00000254521.3; NM_016371.4; NP_057455.1. DR UCSC; uc001gci.4; human. [P56937-1] DR AGR; HGNC:5215; -. DR CTD; 51478; -. DR DisGeNET; 51478; -. DR GeneCards; HSD17B7; -. DR HGNC; HGNC:5215; HSD17B7. DR HPA; ENSG00000132196; Tissue enhanced (liver). DR MIM; 606756; gene. DR neXtProt; NX_P56937; -. DR OpenTargets; ENSG00000132196; -. DR PharmGKB; PA29483; -. DR VEuPathDB; HostDB:ENSG00000132196; -. DR eggNOG; KOG1478; Eukaryota. DR GeneTree; ENSGT00390000013340; -. DR HOGENOM; CLU_029944_2_0_1; -. DR InParanoid; P56937; -. DR OMA; WHNIDGY; -. DR OrthoDB; 2787383at2759; -. DR PhylomeDB; P56937; -. DR TreeFam; TF105433; -. DR BioCyc; MetaCyc:HS05604-MONOMER; -. DR BRENDA; 1.1.1.270; 2681. DR BRENDA; 1.1.1.62; 2681. DR PathwayCommons; P56937; -. DR Reactome; R-HSA-191273; Cholesterol biosynthesis. DR SABIO-RK; P56937; -. DR SignaLink; P56937; -. DR UniPathway; UPA00769; -. DR UniPathway; UPA00770; UER00758. DR BioGRID-ORCS; 51478; 28 hits in 1125 CRISPR screens. DR GeneWiki; HSD17B7; -. DR GenomeRNAi; 51478; -. DR Pharos; P56937; Tchem. DR PRO; PR:P56937; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P56937; Protein. DR Bgee; ENSG00000132196; Expressed in adrenal tissue and 105 other cell types or tissues. DR ExpressionAtlas; P56937; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0000253; F:3-keto sterol reductase activity; IDA:UniProtKB. 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:0008209; P:androgen metabolic process; IDA:UniProtKB. DR GO; GO:0006695; P:cholesterol biosynthetic process; IDA:UniProtKB. DR GO; GO:0006703; P:estrogen biosynthetic process; IDA:UniProtKB. 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; P56937; HS. PE 1: Evidence at protein level; KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; KW Lipid biosynthesis; Lipid metabolism; Membrane; NAD; NADP; Oxidoreductase; KW Reference proteome; Steroid biosynthesis; Transmembrane; KW Transmembrane helix. FT CHAIN 1..341 FT /note="3-keto-steroid reductase/17-beta-hydroxysteroid FT dehydrogenase 7" FT /id="PRO_0000054586" 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..341 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 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 VAR_SEQ 112..119 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10544267" FT /id="VSP_006029" FT VAR_SEQ 215..249 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12732193" FT /id="VSP_012766" FT CONFLICT 52..53 FT /note="HP -> PT (in Ref. 1; AAF14537)" FT /evidence="ECO:0000305" FT CONFLICT 61 FT /note="Q -> P (in Ref. 1; AAF14537)" FT /evidence="ECO:0000305" FT CONFLICT 86 FT /note="C -> R (in Ref. 3; CAC88111)" FT /evidence="ECO:0000305" FT CONFLICT 105 FT /note="F -> L (in Ref. 3; CAC88111)" FT /evidence="ECO:0000305" FT CONFLICT 135 FT /note="L -> F (in Ref. 4; AAP97275)" FT /evidence="ECO:0000305" FT CONFLICT 273..276 FT /note="HQKP -> PPKA (in Ref. 4; AAP97275)" FT /evidence="ECO:0000305" FT CONFLICT 288..295 FT /note="ATTGFGRN -> GTTALEEI (in Ref. 4; AAP97275)" FT /evidence="ECO:0000305" SQ SEQUENCE 341 AA; 38206 MW; FE4892B2602F549B CRC64; MRKVVLITGA SSGIGLALCK RLLAEDDELH LCLACRNMSK AEAVCAALLA SHPTAEVTIV QVDVSNLQSV FRASKELKQR FQRLDCIYLN AGIMPNPQLN IKALFFGLFS RKVIHMFSTA EGLLTQGDKI TADGLQEVFE TNVFGHFILI RELEPLLCHS DNPSQLIWTS SRSARKSNFS LEDFQHSKGK EPYSSSKYAT DLLSVALNRN FNQQGLYSNV ACPGTALTNL TYGILPPFIW TLLMPAILLL RFFANAFTLT PYNGTEALVW LFHQKPESLN PLIKYLSATT GFGRNYIMTQ KMDLDEDTAE KFYQKLLELE KHIRVTIQKT DNQARLSGSC L //