DHB11_HUMAN
ID DHB11_HUMAN Reviewed; 300 AA.
AC Q8NBQ5; Q96HF6; Q9UKU4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Estradiol 17-beta-dehydrogenase 11;
DE EC=1.1.1.62;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 11;
DE Short=17-beta-HSD 11;
DE Short=17bHSD11;
DE Short=17betaHSD11;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase XI;
DE Short=17-beta-HSD XI;
DE Short=17betaHSDXI {ECO:0000303|PubMed:12697717};
DE AltName: Full=Cutaneous T-cell lymphoma-associated antigen HD-CL-03;
DE Short=CTCL-associated antigen HD-CL-03;
DE AltName: Full=Dehydrogenase/reductase SDR family member 8;
DE AltName: Full=Retinal short-chain dehydrogenase/reductase 2;
DE Short=retSDR2;
DE AltName: Full=Short chain dehydrogenase/reductase family 16C member 2;
DE Flags: Precursor;
GN Name=HSD17B11; Synonyms=DHRS8, PAN1B, SDR16C2;
GN ORFNames=PSEC0029, UNQ207/PRO233;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=10800688; DOI=10.1016/s0076-6879(00)16736-9;
RA Haeseleer F., Palczewski K.;
RT "Short-chain dehydrogenases/reductases in retina.";
RL Methods Enzymol. 316:372-383(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RX PubMed=14996095; DOI=10.1111/j.1365-2133.2004.05651.x;
RA Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.;
RT "SEREX identification of new tumour-associated antigens in cutaneous T-cell
RT lymphoma.";
RL Br. J. Dermatol. 150:252-258(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Colon, Kidney, Liver, 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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=9888557; DOI=10.3109/07435809809032667;
RA Li K.X.Z., Smith R.E., Krozowski Z.S.;
RT "Cloning and expression of a novel tissue specific 17beta-hydroxysteroid
RT dehydrogenase.";
RL Endocr. Res. 24:663-667(1998).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=11165019; DOI=10.1016/s0303-7207(00)00417-2;
RA Brereton P., Suzuki T., Sasano H., Li K., Duarte C., Obeyesekere V.,
RA Haeseleer F., Palczewski K., Smith I., Komesaroff P., Krozowski Z.;
RT "Pan1b (17betaHSD11)-enzymatic activity and distribution in the lung.";
RL Mol. Cell. Endocrinol. 171:111-117(2001).
RN [9]
RP ENZYME ACTIVITY IN VITRO, AND TISSUE SPECIFICITY.
RX PubMed=12697717; DOI=10.1210/en.2002-221030;
RA Chai Z., Brereton P., Suzuki T., Sasano H., Obeyesekere V., Escher G.,
RA Saffery R., Fuller P., Enriquez C., Krozowski Z.;
RT "17 beta-hydroxysteroid dehydrogenase type XI localizes to human
RT steroidogenic cells.";
RL Endocrinology 144:2084-2091(2003).
RN [10]
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 [11]
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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-275.
RA Lukacik P., Bunkoczi G., Kavanagh K., Ng S., Von delft F., Bray J.,
RA Edwards A., Arrowsmith C., Sundstrom M., Oppermann U.;
RT "Crystal structure of human 17-beta-hydroxysteroid dehydrogenase type XI.";
RL Submitted (DEC-2004) to the PDB data bank.
CC -!- FUNCTION: Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to
CC androsterone in vitro, suggesting that it may participate in androgen
CC metabolism during steroidogenesis. May act by metabolizing compounds
CC that stimulate steroid synthesis and/or by generating metabolites that
CC inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-
CC dione (4-androste-3,17-dione), and only a slight activity toward
CC testosterone to A-dione. Tumor-associated antigen in cutaneous T-cell
CC lymphoma.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH;
CC Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62;
CC Evidence={ECO:0000269|PubMed:12697717};
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:12697717};
CC -!- INTERACTION:
CC Q8NBQ5; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-1052304, EBI-10827839;
CC Q8NBQ5; Q9NRZ7: AGPAT3; NbExp=3; IntAct=EBI-1052304, EBI-2803601;
CC Q8NBQ5; Q9NRZ5: AGPAT4; NbExp=3; IntAct=EBI-1052304, EBI-1754287;
CC Q8NBQ5; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-1052304, EBI-12109402;
CC Q8NBQ5; Q12981: BNIP1; NbExp=3; IntAct=EBI-1052304, EBI-4402847;
CC Q8NBQ5; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-1052304, EBI-7247651;
CC Q8NBQ5; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-1052304, EBI-10267100;
CC Q8NBQ5; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-1052304, EBI-2680384;
CC Q8NBQ5; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-1052304, EBI-12831978;
CC Q8NBQ5; Q8N5I4: DHRSX; NbExp=3; IntAct=EBI-1052304, EBI-3923585;
CC Q8NBQ5; Q08426: EHHADH; NbExp=3; IntAct=EBI-1052304, EBI-2339219;
CC Q8NBQ5; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-1052304, EBI-711490;
CC Q8NBQ5; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-1052304, EBI-12118888;
CC Q8NBQ5; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-1052304, EBI-11991950;
CC Q8NBQ5; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-1052304, EBI-17231387;
CC Q8NBQ5; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-1052304, EBI-12937691;
CC Q8NBQ5; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-1052304, EBI-12133176;
CC Q8NBQ5; O75427: LRCH4; NbExp=3; IntAct=EBI-1052304, EBI-718707;
CC Q8NBQ5; P11836: MS4A1; NbExp=3; IntAct=EBI-1052304, EBI-2808234;
CC Q8NBQ5; Q99519: NEU1; NbExp=3; IntAct=EBI-1052304, EBI-721517;
CC Q8NBQ5; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-1052304, EBI-1054848;
CC Q8NBQ5; Q9NUU6: OTULINL; NbExp=3; IntAct=EBI-1052304, EBI-6916492;
CC Q8NBQ5; Q04941: PLP2; NbExp=3; IntAct=EBI-1052304, EBI-608347;
CC Q8NBQ5; O60831: PRAF2; NbExp=3; IntAct=EBI-1052304, EBI-2506064;
CC Q8NBQ5; P43378: PTPN9; NbExp=3; IntAct=EBI-1052304, EBI-742898;
CC Q8NBQ5; Q8IV61: RASGRP3; NbExp=3; IntAct=EBI-1052304, EBI-1047876;
CC Q8NBQ5; Q96LZ7: RMDN2; NbExp=3; IntAct=EBI-1052304, EBI-2806908;
CC Q8NBQ5; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-1052304, EBI-10244780;
CC Q8NBQ5; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-1052304, EBI-8652744;
CC Q8NBQ5; O75396: SEC22B; NbExp=3; IntAct=EBI-1052304, EBI-1058865;
CC Q8NBQ5; P05121: SERPINE1; NbExp=3; IntAct=EBI-1052304, EBI-953978;
CC Q8NBQ5; Q6FHJ7: SFRP4; NbExp=3; IntAct=EBI-1052304, EBI-2854879;
CC Q8NBQ5; O95562: SFT2D2; NbExp=3; IntAct=EBI-1052304, EBI-4402330;
CC Q8NBQ5; A0A1P0AYU5: SFXN3; NbExp=3; IntAct=EBI-1052304, EBI-14193895;
CC Q8NBQ5; Q96BI1: SLC22A18; NbExp=3; IntAct=EBI-1052304, EBI-11721845;
CC Q8NBQ5; Q96AG3: SLC25A46; NbExp=3; IntAct=EBI-1052304, EBI-10281975;
CC Q8NBQ5; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-1052304, EBI-10262251;
CC Q8NBQ5; P0DN84: STRIT1; NbExp=3; IntAct=EBI-1052304, EBI-12200293;
CC Q8NBQ5; Q13190: STX5; NbExp=3; IntAct=EBI-1052304, EBI-714206;
CC Q8NBQ5; O15400: STX7; NbExp=3; IntAct=EBI-1052304, EBI-3221827;
CC Q8NBQ5; Q8N2H4: SYS1; NbExp=3; IntAct=EBI-1052304, EBI-13075176;
CC Q8NBQ5; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-1052304, EBI-10171534;
CC Q8NBQ5; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-1052304, EBI-10694905;
CC Q8NBQ5; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1052304, EBI-8638294;
CC Q8NBQ5; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-1052304, EBI-17684533;
CC Q8NBQ5; Q969S6: TMEM203; NbExp=3; IntAct=EBI-1052304, EBI-12274070;
CC Q8NBQ5; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-1052304, EBI-10315004;
CC Q8NBQ5; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-1052304, EBI-12038591;
CC Q8NBQ5; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-1052304, EBI-2852148;
CC Q8NBQ5; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-1052304, EBI-6656213;
CC Q8NBQ5; Q9Y320: TMX2; NbExp=3; IntAct=EBI-1052304, EBI-6447886;
CC Q8NBQ5; Q6ZUI0: TPRG1; NbExp=3; IntAct=EBI-1052304, EBI-17249488;
CC Q8NBQ5; P49638: TTPA; NbExp=3; IntAct=EBI-1052304, EBI-10210710;
CC Q8NBQ5; Q9NYZ1: TVP23B; NbExp=3; IntAct=EBI-1052304, EBI-11343401;
CC Q8NBQ5; Q53HI1: UNC50; NbExp=3; IntAct=EBI-1052304, EBI-7601760;
CC Q8NBQ5; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-1052304, EBI-1059156;
CC Q8NBQ5; O95070: YIF1A; NbExp=3; IntAct=EBI-1052304, EBI-2799703;
CC Q8NBQ5; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-1052304, EBI-751210;
CC Q8NBQ5; Q6UX98: ZDHHC24; NbExp=3; IntAct=EBI-1052304, EBI-10254561;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9EQ06}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q9EQ06}. Note=Redistributed from the endoplasmic
CC reticulum to lipids droplets in the cell upon induction of lipids
CC droplet formation. {ECO:0000250|UniProtKB:Q9EQ06}.
CC -!- TISSUE SPECIFICITY: Present at high level in steroidogenic cells such
CC as syncytiotrophoblasts, sebaceous gland, Leydig cells, and granulosa
CC cells of the dominant follicle and corpus luteum. In lung, it is
CC detected in the ciliated epithelium and in acini of adult trachea, in
CC bronchioles, but not in alveoli. In the eye, it is detected in the
CC nonpigmented epithelium of the ciliary body and, at lower level, in the
CC inner nuclear layer of the retina (at protein level). Widely expressed.
CC Highly expressed in retina, pancreas, kidney, liver, lung, adrenal,
CC small intestine, ovary and heart. {ECO:0000269|PubMed:10800688,
CC ECO:0000269|PubMed:11165019, ECO:0000269|PubMed:12697717,
CC ECO:0000269|PubMed:9888557}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 17-beta-HSD 3 subfamily. {ECO:0000305}.
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DR EMBL; AF126780; AAF06939.1; -; mRNA.
DR EMBL; AF273056; AAM44459.1; -; mRNA.
DR EMBL; AY358553; AAQ88917.1; -; mRNA.
DR EMBL; AK075348; BAC11560.1; -; mRNA.
DR EMBL; AC108516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008650; AAH08650.1; -; mRNA.
DR EMBL; BC014327; AAH14327.1; -; mRNA.
DR EMBL; BC016367; AAH16367.1; -; mRNA.
DR EMBL; BC021673; AAH21673.1; -; mRNA.
DR EMBL; BC036001; AAH36001.1; -; mRNA.
DR CCDS; CCDS3619.1; -.
DR RefSeq; NP_057329.3; NM_016245.4.
DR PDB; 1YB1; X-ray; 1.95 A; A/B=28-275.
DR PDBsum; 1YB1; -.
DR AlphaFoldDB; Q8NBQ5; -.
DR SMR; Q8NBQ5; -.
DR BioGRID; 119349; 394.
DR IntAct; Q8NBQ5; 72.
DR MINT; Q8NBQ5; -.
DR STRING; 9606.ENSP00000351035; -.
DR DrugBank; DB02854; Aetiocholanolone.
DR iPTMnet; Q8NBQ5; -.
DR PhosphoSitePlus; Q8NBQ5; -.
DR SwissPalm; Q8NBQ5; -.
DR BioMuta; HSD17B11; -.
DR DMDM; 296439374; -.
DR EPD; Q8NBQ5; -.
DR jPOST; Q8NBQ5; -.
DR MassIVE; Q8NBQ5; -.
DR MaxQB; Q8NBQ5; -.
DR PaxDb; Q8NBQ5; -.
DR PeptideAtlas; Q8NBQ5; -.
DR PRIDE; Q8NBQ5; -.
DR ProteomicsDB; 72809; -.
DR Antibodypedia; 14449; 197 antibodies from 26 providers.
DR DNASU; 51170; -.
DR Ensembl; ENST00000358290.9; ENSP00000351035.4; ENSG00000198189.11.
DR GeneID; 51170; -.
DR KEGG; hsa:51170; -.
DR UCSC; uc003hqp.3; human.
DR CTD; 51170; -.
DR DisGeNET; 51170; -.
DR GeneCards; HSD17B11; -.
DR HGNC; HGNC:22960; HSD17B11.
DR HPA; ENSG00000198189; Tissue enhanced (intestine, liver).
DR MIM; 612831; gene.
DR neXtProt; NX_Q8NBQ5; -.
DR PharmGKB; PA162391655; -.
DR VEuPathDB; HostDB:ENSG00000198189; -.
DR eggNOG; KOG1201; Eukaryota.
DR HOGENOM; CLU_010194_2_5_1; -.
DR InParanoid; Q8NBQ5; -.
DR OrthoDB; 1373099at2759; -.
DR PhylomeDB; Q8NBQ5; -.
DR TreeFam; TF312837; -.
DR PathwayCommons; Q8NBQ5; -.
DR Reactome; R-HSA-193144; Estrogen biosynthesis.
DR SignaLink; Q8NBQ5; -.
DR SIGNOR; Q8NBQ5; -.
DR BioGRID-ORCS; 51170; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; HSD17B11; human.
DR EvolutionaryTrace; Q8NBQ5; -.
DR GeneWiki; HSD17B11; -.
DR GenomeRNAi; 51170; -.
DR Pharos; Q8NBQ5; Tbio.
DR PRO; PR:Q8NBQ5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8NBQ5; protein.
DR Bgee; ENSG00000198189; Expressed in jejunal mucosa and 200 other tissues.
DR ExpressionAtlas; Q8NBQ5; baseline and differential.
DR Genevisible; Q8NBQ5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; TAS:Reactome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IDA:HGNC-UCL.
DR GO; GO:0006710; P:androgen catabolic process; IDA:HGNC-UCL.
DR GO; GO:0006703; P:estrogen biosynthetic process; TAS:Reactome.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Lipid biosynthesis; Lipid droplet;
KW Lipid metabolism; NADP; Oxidoreductase; Reference proteome; Signal;
KW Steroid biosynthesis.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..300
FT /note="Estradiol 17-beta-dehydrogenase 11"
FT /id="PRO_0000031970"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 23
FT /note="V -> E (in Ref. 6; AAH08650)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="I -> T (in Ref. 4; BAC11560)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="K -> N (in Ref. 6; AAH08650)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="V -> C (in Ref. 6; AAH08650)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="N -> K (in Ref. 6; AAH08650)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="P -> M (in Ref. 6; AAH08650)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="I -> N (in Ref. 6; AAH08650)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="A -> C (in Ref. 6; AAH08650)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="F -> I (in Ref. 6; AAH08650)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="Q -> R (in Ref. 1; AAF06939, 2; AAM44459, 3;
FT AAQ88917, 4; BAC11560 and 6; AAH08650/AAH14327/AAH16367/
FT AAH21673/AAH36001)"
FT /evidence="ECO:0000305"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1YB1"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:1YB1"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:1YB1"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:1YB1"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:1YB1"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 179..205
FT /evidence="ECO:0007829|PDB:1YB1"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:1YB1"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1YB1"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:1YB1"
SQ SEQUENCE 300 AA; 32936 MW; 51DE633A205EBE86 CRC64;
MKFLLDILLL LPLLIVCSLE SFVKLFIPKR RKSVTGEIVL ITGAGHGIGR LTAYEFAKLK
SKLVLWDINK HGLEETAAKC KGLGAKVHTF VVDCSNREDI YSSAKKVKAE IGDVSILVNN
AGVVYTSDLF ATQDPQIEKT FEVNVLAHFW TTKAFLPAMT KNNHGHIVTV ASAAGHVSVP
FLLAYCSSKF AAVGFHKTLT DELAALQITG VKTTCLCPNF VNTGFIKNPS TSLGPTLEPE
EVVNRLMHGI LTEQKMIFIP SSIAFLTTLE RILPERFLAV LKQKISVKFD AVIGYKMKAQ
