DHB11_MOUSE
ID DHB11_MOUSE Reviewed; 298 AA.
AC Q9EQ06; Q3U2P6; Q8BR33; Q8C7S0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
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;
DE AltName: Full=Dehydrogenase/reductase SDR family member 8;
DE Flags: Precursor;
GN Name=Hsd17b11; Synonyms=Dhrs8, Pan1b;
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] (ISOFORM 1), AND ENZYME ACTIVITY IN VITRO.
RC STRAIN=NIH Swiss;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RA Chen W., Napoli J.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Corpora quadrigemina, Dendritic cell, Embryonic stem cell, and
RC Inner ear;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18359291; DOI=10.1016/j.bbrc.2008.03.063;
RA Horiguchi Y., Araki M., Motojima K.;
RT "17beta-Hydroxysteroid dehydrogenase type 13 is a liver-specific lipid
RT droplet-associated protein.";
RL Biochem. Biophys. Res. Commun. 370:235-238(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and 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: 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.
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:11165019};
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:11165019};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000305|PubMed:18359291}. Lipid droplet
CC {ECO:0000269|PubMed:18359291}. Note=Redistributed from the endoplasmic
CC reticulum to lipids droplets in the cell upon induction of lipids
CC droplet formation. {ECO:0000269|PubMed:18359291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EQ06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EQ06-2; Sequence=VSP_015013, VSP_015014;
CC -!- TISSUE SPECIFICITY: Expressed in the liver (at protein level)
CC (PubMed:18359291). Also expressed in the intestine and, at much lower
CC levels, in the kidney (PubMed:18359291). {ECO:0000269|PubMed:18359291}.
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; AF304306; AAG41413.1; -; mRNA.
DR EMBL; AY053570; AAL14859.1; -; mRNA.
DR EMBL; AK049355; BAC33704.1; -; mRNA.
DR EMBL; AK154803; BAE32840.1; -; mRNA.
DR EMBL; AK155174; BAE33094.1; -; mRNA.
DR EMBL; AK155202; BAE33115.1; -; mRNA.
DR EMBL; AK155327; BAE33194.1; -; mRNA.
DR EMBL; AK158327; BAE34459.1; -; mRNA.
DR EMBL; AK170939; BAE42129.1; -; mRNA.
DR EMBL; BC038340; AAH38340.1; -; mRNA.
DR CCDS; CCDS19481.1; -. [Q9EQ06-1]
DR RefSeq; NP_444492.1; NM_053262.3. [Q9EQ06-1]
DR AlphaFoldDB; Q9EQ06; -.
DR SMR; Q9EQ06; -.
DR BioGRID; 227794; 6.
DR IntAct; Q9EQ06; 1.
DR STRING; 10090.ENSMUSP00000031251; -.
DR iPTMnet; Q9EQ06; -.
DR PhosphoSitePlus; Q9EQ06; -.
DR SwissPalm; Q9EQ06; -.
DR EPD; Q9EQ06; -.
DR jPOST; Q9EQ06; -.
DR MaxQB; Q9EQ06; -.
DR PaxDb; Q9EQ06; -.
DR PeptideAtlas; Q9EQ06; -.
DR PRIDE; Q9EQ06; -.
DR ProteomicsDB; 279644; -. [Q9EQ06-1]
DR ProteomicsDB; 279645; -. [Q9EQ06-2]
DR Antibodypedia; 14449; 197 antibodies from 26 providers.
DR DNASU; 114664; -.
DR Ensembl; ENSMUST00000031251; ENSMUSP00000031251; ENSMUSG00000029311. [Q9EQ06-1]
DR Ensembl; ENSMUST00000119025; ENSMUSP00000113455; ENSMUSG00000029311. [Q9EQ06-2]
DR GeneID; 114664; -.
DR KEGG; mmu:114664; -.
DR UCSC; uc008yjy.1; mouse. [Q9EQ06-1]
DR UCSC; uc008yjz.1; mouse. [Q9EQ06-2]
DR CTD; 51170; -.
DR MGI; MGI:2149821; Hsd17b11.
DR VEuPathDB; HostDB:ENSMUSG00000029311; -.
DR eggNOG; KOG1201; Eukaryota.
DR GeneTree; ENSGT00940000160856; -.
DR HOGENOM; CLU_010194_2_5_1; -.
DR InParanoid; Q9EQ06; -.
DR OMA; RTPMIKM; -.
DR OrthoDB; 1373099at2759; -.
DR PhylomeDB; Q9EQ06; -.
DR TreeFam; TF312837; -.
DR Reactome; R-MMU-193144; Estrogen biosynthesis.
DR BioGRID-ORCS; 114664; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Hsd17b13; mouse.
DR PRO; PR:Q9EQ06; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9EQ06; protein.
DR Bgee; ENSMUSG00000029311; Expressed in small intestine Peyer's patch and 258 other tissues.
DR Genevisible; Q9EQ06; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
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; ISO:MGI.
DR GO; GO:0006710; P:androgen catabolic process; ISO:MGI.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
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 Alternative splicing; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid droplet; Lipid metabolism; NADP; Oxidoreductase; Reference proteome;
KW Signal; Steroid biosynthesis.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..298
FT /note="Estradiol 17-beta-dehydrogenase 11"
FT /id="PRO_0000031971"
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 VAR_SEQ 232
FT /note="N -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015013"
FT VAR_SEQ 233..298
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015014"
SQ SEQUENCE 298 AA; 32881 MW; 8ED9279FFBF20EA1 CRC64;
MKYLLDLILL LPLLIVFSIE SLVKLFIPKK KKSVAGEIVL ITGAGHGIGR LTAYEFAKLN
TKLVLWDINK NGIEETAAKC RKLGAQAHPF VVDCSQREEI YSAAKKVKEE VGDVSILVNN
AGVVYTADLF ATQDPQIEKT FEVNVLAHFW TTKAFLPVMM KNNHGHIVTV ASAAGHTVVP
FLLAYCSSKF AAVGFHRALT DELAALGRTG VRTSCLCPNF INTGFIKNPS TNLGPTLEPE
EVVEHLMHGI LTEKQMIFVP SSIALLTVLE RIVPERFLQV LKHRINVKFD AVVGYKDK
