DHR11_MOUSE
ID DHR11_MOUSE Reviewed; 260 AA.
AC Q3U0B3; Q5SXB3; Q8R249;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Dehydrogenase/reductase SDR family member 11;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase {ECO:0000305};
DE AltName: Full=3-beta-hydroxysteroid 3-dehydrogenase {ECO:0000305};
DE EC=1.1.1.270 {ECO:0000250|UniProtKB:Q6UWP2};
DE AltName: Full=Estradiol 17-beta-dehydrogenase {ECO:0000305};
DE EC=1.1.1.62 {ECO:0000250|UniProtKB:Q6UWP2};
DE AltName: Full=Short-chain dehydrogenase/reductase family 24C member 1 {ECO:0000250|UniProtKB:Q6UWP2};
DE Flags: Precursor;
GN Name=Dhrs11; Synonyms=Sdr24c1 {ECO:0000250|UniProtKB:Q6UWP2};
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 [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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).
CC -!- FUNCTION: Catalyzes the conversion of the 17-keto group of estrone,
CC 4- and 5-androstenes and 5-alpha-androstanes into their 17-beta-
CC hydroxyl metabolites and the conversion of the 3-keto group of 3-,
CC 3,17- and 3,20- diketosteroids into their 3-hydroxyl metabolites.
CC Exhibits reductive 3-beta-hydroxysteroid dehydrogenase activity toward
CC 5-beta-androstanes, 5-beta-pregnanes, 4-pregnenes and bile acids. May
CC also reduce endogenous and exogenous alpha-dicarbonyl compounds and
CC xenobiotic alicyclic ketones. {ECO:0000250|UniProtKB:Q6UWP2}.
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:0000250|UniProtKB:Q6UWP2};
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:0000250|UniProtKB:Q6UWP2};
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:0000250|UniProtKB:Q6UWP2};
CC -!- ACTIVITY REGULATION: Inhibited by flavonoids including apigenin,
CC luteolin, genistein, kaempferol and quercetin and also by
CC carbenoxolone, zearalenone, glycyrrhetinic, curcumin and flufenamic
CC acid. {ECO:0000250|UniProtKB:Q6UWP2}.
CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC {ECO:0000250|UniProtKB:Q6UWP2}.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AK157041; BAE33942.1; -; mRNA.
DR EMBL; AL596083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022224; AAH22224.2; -; mRNA.
DR CCDS; CCDS36261.1; -.
DR RefSeq; NP_808232.2; NM_177564.5.
DR AlphaFoldDB; Q3U0B3; -.
DR SMR; Q3U0B3; -.
DR STRING; 10090.ENSMUSP00000043467; -.
DR iPTMnet; Q3U0B3; -.
DR PhosphoSitePlus; Q3U0B3; -.
DR CPTAC; non-CPTAC-3438; -.
DR CPTAC; non-CPTAC-3784; -.
DR EPD; Q3U0B3; -.
DR jPOST; Q3U0B3; -.
DR MaxQB; Q3U0B3; -.
DR PaxDb; Q3U0B3; -.
DR PeptideAtlas; Q3U0B3; -.
DR PRIDE; Q3U0B3; -.
DR ProteomicsDB; 279382; -.
DR Antibodypedia; 72789; 194 antibodies from 25 providers.
DR DNASU; 192970; -.
DR Ensembl; ENSMUST00000047560; ENSMUSP00000043467; ENSMUSG00000034449.
DR GeneID; 192970; -.
DR KEGG; mmu:192970; -.
DR UCSC; uc007kqs.2; mouse.
DR CTD; 79154; -.
DR MGI; MGI:2652816; Dhrs11.
DR VEuPathDB; HostDB:ENSMUSG00000034449; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00840000129887; -.
DR HOGENOM; CLU_010194_2_10_1; -.
DR InParanoid; Q3U0B3; -.
DR OMA; WRWMWET; -.
DR OrthoDB; 1190834at2759; -.
DR PhylomeDB; Q3U0B3; -.
DR TreeFam; TF324174; -.
DR UniPathway; UPA00769; -.
DR BioGRID-ORCS; 192970; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q3U0B3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3U0B3; protein.
DR Bgee; ENSMUSG00000034449; Expressed in fetal liver hematopoietic progenitor cell and 176 other tissues.
DR ExpressionAtlas; Q3U0B3; baseline and differential.
DR Genevisible; Q3U0B3; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; ISO:MGI.
DR GO; GO:0072555; F:17-beta-ketosteroid reductase activity; ISO:MGI.
DR GO; GO:0000253; F:3-keto sterol reductase activity; ISO:MGI.
DR GO; GO:0102176; F:cycloeucalenone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006694; P:steroid biosynthetic process; ISO:MGI.
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 Lipid metabolism; NADP; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Secreted; Signal; Steroid metabolism.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..260
FT /note="Dehydrogenase/reductase SDR family member 11"
FT /id="PRO_0000045491"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 18..23
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 43..44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 70..71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 97
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 170
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 201..204
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
SQ SEQUENCE 260 AA; 28274 MW; D26E6B4F4877EB86 CRC64;
MTRAGMERWR DRLALVTGAS GGIGAAVARA LVQQGLKVVG CARTVGNIEE LAAECKSAGY
PGTLIPYRCD LSNEEDILSM FSAVRSQHSG VDICINNAGM ARPDTLLSGS TSGWKDMFNV
NVLALSICTR EAYQSMKERN IDDGHIININ SMCGHRVPPQ SVIHFYSATK YAVTALTEGL
RQELLEAQTH IRATCISPGL VETQFAFKLH DKDPGEAAAT YEHIKCLRPE DVAEAVIYVL
STPPHVQVGD IQMRPTEQVT
