ID   DHR11_HUMAN             Reviewed;         260 AA.
AC   Q6UWP2; A0A0U5BLD0; B2RDZ3; Q9BUC7; Q9H674;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Dehydrogenase/reductase SDR family member 11;
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase {ECO:0000305|PubMed:26920053};
DE   AltName: Full=3-beta-hydroxysteroid 3-dehydrogenase {ECO:0000305|PubMed:26920053};
DE            EC=1.1.1.270 {ECO:0000269|PubMed:26920053};
DE   AltName: Full=Estradiol 17-beta-dehydrogenase {ECO:0000305|PubMed:26920053};
DE            EC=1.1.1.62 {ECO:0000269|PubMed:26920053};
DE   AltName: Full=Short-chain dehydrogenase/reductase family 24C member 1 {ECO:0000303|PubMed:19027726};
DE   Flags: Precursor;
GN   Name=DHRS11; Synonyms=SDR24C1 {ECO:0000303|PubMed:19027726};
GN   ORFNames=UNQ836/PRO1774;
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] (ISOFORM 3), FUNCTION, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=26920053; DOI=10.1016/j.bbrc.2016.01.190;
RA   Endo S., Miyagi N., Matsunaga T., Hara A., Ikari A.;
RT   "Human dehydrogenase/reductase (SDR family) member 11 is a novel type of
RT   17beta-hydroxysteroid dehydrogenase.";
RL   Biochem. Biophys. Res. Commun. 472:231-236(2016).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain cortex, and Small intestine;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
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   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   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 1-256 (ISOFORM 1) IN COMPLEX WITH
RP   NADP AND ACETATE, AND SUBUNIT.
RG   Structural genomics consortium (SGC);
RT   "Structure of the putative human dehydrogenase MGC4172.";
RL   Submitted (OCT-2004) to the PDB data bank.
RN   [9]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA   Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA   Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA   Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA   Adamski J., Oppermann U.;
RT   "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT   nomenclature initiative.";
RL   Chem. Biol. Interact. 178:94-98(2009).
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:0000269|PubMed:26920053}.
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:26920053};
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:26920053};
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:26920053};
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:0000269|PubMed:26920053}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.1 uM for NADPH {ECO:0000269|PubMed:26920053};
CC         KM=0.7 uM for estrone (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=1.3 uM for 5-alpha-androstan-3-alpha-ol-17-one (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=2.2 uM for 5-alpha-androstan-3-beta-ol-17-one (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=11 uM for dehydroepiandrosterone (DHEA) (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=12 uM for DHEA sulfate (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=19 uM for 4-androsten-3-alpha-ol-17-one (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=0.7 uM for 5-beta-pregnan-20-beta-ol-3-one (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=1.1 uM for dehydrolithocholic acid (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=5.2 uM for 5-beta-cholanic acid-3,7-dione (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=5.1 uM for 20-alpha-hydroxyprogesterone (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=44 uM for taurodehydrocholic acid (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=29 uM for dehydrocholic acid (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=102 uM for 5-beta-dihydrotestosterone (DHT) (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=5.2 uM for 5-beta-androstane-3,17-dione (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=4.6 uM for 4-androstene-3,17-dione (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=12 uM for 5-alpha-androstane-3,17-dione (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=2.1 uM for 5-beta-pregnane-21-ol-3,20-dione (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=3.4 uM for progesterone (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=15 uM for 5-beta-pregnane-3,20-dione (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=16 uM for 17-beta-estradiol (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=30 uM for testosterone (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=23 uM for 4-androstene-3-alpha,17-beta-diol (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=11 uM for 5-androstene-3-alpha,17-beta-diol (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=26 uM for 5-alpha-dihydrotestosterone (DHT) (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=9.2 uM for 5-alpha-androstane-3-alpha,17-beta-diol (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=1.1 uM for 5-alpha-androstane-3-beta,17-beta-diol (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=36 uM for 5-beta-androstan-3-beta-ol-17-one (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=12 uM for 5-beta-androstane-3-beta,17-beta-diol (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=22 uM for 3-beta-hydroxyprogesterone (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=36 uM for 5-beta-pregnan-3-beta-ol-20-one (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=14 uM for 5-beta-pregnane-3-beta,20-beta-diol (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=4.7 uM for 5-beta-pregnane-3-beta,21-diol-20-one (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         KM=0.4 uM for isolithocholic acid (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=60 uM for 1-phenyl-1,2-propanedione (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=620 uM for 2,3-hexanedione (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=201 uM for 2,3-heptanedione (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=420 uM for 3,4-hexanedione (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=178 uM for alpha-tetralone (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         KM=740 uM for loxoprofen (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26920053};
CC         Vmax=43 nmol/min/mg enzyme with estrone as substrate (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=42 nmol/min/mg enzyme with 5-alpha-androstan-3-alpha-ol-17-one
CC         as substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=49 nmol/min/mg enzyme with 5-alpha-androstan-3-beta-ol-17-one as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=118 nmol/min/mg enzyme with dehydroepiandrosterone (DHEA) as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=60 nmol/min/mg enzyme with DHEA sulfate as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=43 nmol/min/mg enzyme with 4-androsten-3-alpha-ol-17-one as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=44 nmol/min/mg enzyme with 5-beta-pregnan-20-beta-ol-3-one as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=44 nmol/min/mg enzyme with dehydrolithocholic acid as substrate
CC         (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=85 nmol/min/mg enzyme with 5-beta-cholanic acid-3,7-dione as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=40 nmol/min/mg enzyme with 20-alpha-hydroxyprogesterone as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=200 nmol/min/mg enzyme with taurodehydrocholic acid as substrate
CC         (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=119 nmol/min/mg enzyme with dehydrocholic acid as substrate (at
CC         37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=389 nmol/min/mg enzyme with 5-beta-dihydrotestosterone (DTH) as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=62 nmol/min/mg enzyme with 5-beta-androstane-3,17-dione as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=52 nmol/min/mg enzyme with 4-androstene-3,17-dione as substrate
CC         (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=57 nmol/min/mg enzyme with 5-alpha-androstane-3,17-dione as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=49 nmol/min/mg enzyme with 5-beta-pregnane-21-ol-3,20-dione as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=36 nmol/min/mg enzyme with progesterone as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=123 nmol/min/mg enzyme with 5-beta-pregnane-3,20-dione as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=246 nmol/min/mg enzyme with 17-beta-estradiol as substrate (at
CC         37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=238 nmol/min/mg enzyme with testosterone as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=33 nmol/min/mg enzyme with 4-androstene-3-alpha,17-beta-diol as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=366 nmol/min/mg enzyme with 5-androstene-3-alpha,17-beta-diol as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=117 nmol/min/mg enzyme with 5-alpha-dihydrotestosterone (DHT) as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=40 nmol/min/mg enzyme with
CC         5-alpha-androstane-3-alpha,17-beta-diol as substrate (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=96 nmol/min/mg enzyme with
CC         5-alpha-androstane-3-beta,17-beta-diol as substrate (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=137 nmol/min/mg enzyme with 5-beta-androstan-3-beta-ol-17-one as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=511 nmol/min/mg enzyme with
CC         5-beta-androstane-3-beta,17-beta-diol as substrate (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=364 nmol/min/mg enzyme with 3-beta-hydroxyprogesterone as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=268 nmol/min/mg enzyme with 5-beta-pregnan-3-beta-ol-20-one as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=220 nmol/min/mg enzyme with 5-beta-pregnane-3-beta,20-beta-diol
CC         as substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=96 nmol/min/mg enzyme with 5-beta-pregnane-3-beta,21-diol-20-one
CC         as substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=28 nmol/min/mg enzyme with isolithocholic acid as substrate (at
CC         37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=69 nmol/min/mg enzyme with 1-phenyl-1,2-propanedione as
CC         substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=331 nmol/min/mg enzyme with 2,3-hexanedione as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=86 nmol/min/mg enzyme with 2,3-heptanedione as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=166 nmol/min/mg enzyme with 3,4-hexanedione as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=67 nmol/min/mg enzyme with alpha-tetralone as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:26920053};
CC         Vmax=51 nmol/min/mg enzyme with loxoprofen as substrate (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:26920053};
CC   -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC       {ECO:0000305|PubMed:26920053}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.8}.
CC   -!- INTERACTION:
CC       Q6UWP2-2; Q92796: DLG3; NbExp=3; IntAct=EBI-12225017, EBI-80440;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6UWP2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6UWP2-2; Sequence=VSP_016987;
CC       Name=3;
CC         IsoId=Q6UWP2-3; Sequence=VSP_059104;
CC   -!- TISSUE SPECIFICITY: Isoform 1: Ubiquitously expressed, with highest
CC       levels in testis, small intestine, colon, kidney, brain and heart.
CC       Isoform 3: Expressed in brain, heart and skeletal muscle.
CC       {ECO:0000269|PubMed:26920053}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {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; LC110386; BAU36404.1; -; mRNA.
DR   EMBL; AY358712; AAQ89074.1; -; mRNA.
DR   EMBL; AK026196; BAB15390.1; -; mRNA.
DR   EMBL; AK315735; BAG38090.1; -; mRNA.
DR   EMBL; CR457356; CAG33637.1; -; mRNA.
DR   EMBL; CH471199; EAW57568.1; -; Genomic_DNA.
DR   EMBL; BC002731; AAH02731.2; -; mRNA.
DR   CCDS; CCDS11315.2; -. [Q6UWP2-1]
DR   RefSeq; NP_077284.2; NM_024308.3. [Q6UWP2-1]
DR   RefSeq; XP_005257715.1; XM_005257658.2. [Q6UWP2-3]
DR   PDB; 1XG5; X-ray; 1.53 A; A/B/C/D=1-256.
DR   PDBsum; 1XG5; -.
DR   AlphaFoldDB; Q6UWP2; -.
DR   SMR; Q6UWP2; -.
DR   BioGRID; 122572; 8.
DR   IntAct; Q6UWP2; 1.
DR   STRING; 9606.ENSP00000482704; -.
DR   DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR   iPTMnet; Q6UWP2; -.
DR   PhosphoSitePlus; Q6UWP2; -.
DR   BioMuta; DHRS11; -.
DR   DMDM; 74749397; -.
DR   EPD; Q6UWP2; -.
DR   jPOST; Q6UWP2; -.
DR   MassIVE; Q6UWP2; -.
DR   MaxQB; Q6UWP2; -.
DR   PaxDb; 9606-ENSP00000482704; -.
DR   PeptideAtlas; Q6UWP2; -.
DR   ProteomicsDB; 67507; -. [Q6UWP2-1]
DR   ProteomicsDB; 67508; -. [Q6UWP2-2]
DR   Pumba; Q6UWP2; -.
DR   Antibodypedia; 72789; 213 antibodies from 25 providers.
DR   DNASU; 79154; -.
DR   Ensembl; ENST00000611337.4; ENSP00000477603.1; ENSG00000278535.5. [Q6UWP2-2]
DR   Ensembl; ENST00000618403.5; ENSP00000482704.1; ENSG00000278535.5. [Q6UWP2-1]
DR   Ensembl; ENST00000621143.2; ENSP00000483747.1; ENSG00000275397.2. [Q6UWP2-1]
DR   Ensembl; ENST00000631686.1; ENSP00000488610.1; ENSG00000275397.2. [Q6UWP2-2]
DR   GeneID; 79154; -.
DR   KEGG; hsa:79154; -.
DR   MANE-Select; ENST00000618403.5; ENSP00000482704.1; NM_024308.4; NP_077284.2.
DR   UCSC; uc002hnd.4; human. [Q6UWP2-1]
DR   AGR; HGNC:28639; -.
DR   CTD; 79154; -.
DR   DisGeNET; 79154; -.
DR   GeneCards; DHRS11; -.
DR   HGNC; HGNC:28639; DHRS11.
DR   HPA; ENSG00000278535; Tissue enriched (intestine).
DR   MIM; 616159; gene.
DR   neXtProt; NX_Q6UWP2; -.
DR   OpenTargets; ENSG00000278535; -.
DR   PharmGKB; PA164718841; -.
DR   VEuPathDB; HostDB:ENSG00000278535; -.
DR   eggNOG; KOG1205; Eukaryota.
DR   GeneTree; ENSGT00840000129887; -.
DR   InParanoid; Q6UWP2; -.
DR   OMA; WRWMWET; -.
DR   OrthoDB; 5391013at2759; -.
DR   PhylomeDB; Q6UWP2; -.
DR   TreeFam; TF324174; -.
DR   PathwayCommons; Q6UWP2; -.
DR   SignaLink; Q6UWP2; -.
DR   UniPathway; UPA00769; -.
DR   BioGRID-ORCS; 79154; 11 hits in 1154 CRISPR screens.
DR   ChiTaRS; DHRS11; human.
DR   EvolutionaryTrace; Q6UWP2; -.
DR   GenomeRNAi; 79154; -.
DR   Pharos; Q6UWP2; Tbio.
DR   PRO; PR:Q6UWP2; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q6UWP2; Protein.
DR   Bgee; ENSG00000278535; Expressed in duodenum and 97 other cell types or tissues.
DR   ExpressionAtlas; Q6UWP2; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR   GO; GO:0072555; F:17-beta-ketosteroid reductase activity; IDA:UniProtKB.
DR   GO; GO:0000253; F:3-keto sterol reductase activity; IDA:UniProtKB.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase [NAD(P)] activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   CDD; cd05343; Mgc4172-like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43115; DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR43115:SF4; DEHYDROGENASE_REDUCTASE SDR FAMILY MEMBER 11; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
DR   Genevisible; Q6UWP2; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Lipid metabolism; NADP;
KW   Nucleotide-binding; Oxidoreductase; Reference proteome; Secreted; Signal;
KW   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_0000045490"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         18..23
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   BINDING         43..44
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   BINDING         49
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   BINDING         70..71
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   BINDING         97
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   BINDING         166
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   BINDING         170
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   BINDING         201..204
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   BINDING         208
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0007744|PDB:1XG5"
FT   VAR_SEQ         1..79
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT                   /id="VSP_016987"
FT   VAR_SEQ         196..226
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_059104"
FT   CONFLICT        81
FT                   /note="F -> S (in Ref. 3; BAB15390 and 4; CAG33637)"
FT                   /evidence="ECO:0000305"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   STRAND          13..18
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           22..33
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   STRAND          37..43
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           45..57
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           74..88
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   TURN            106..108
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           111..121
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           123..138
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           152..154
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           164..186
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   STRAND          192..199
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           205..209
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   TURN            210..212
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           214..221
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   HELIX           229..241
FT                   /evidence="ECO:0007829|PDB:1XG5"
FT   STRAND          246..255
FT                   /evidence="ECO:0007829|PDB:1XG5"
SQ   SEQUENCE   260 AA;  28308 MW;  88DFF656874F19F4 CRC64;
     MARPGMERWR DRLALVTGAS GGIGAAVARA LVQQGLKVVG CARTVGNIEE LAAECKSAGY
     PGTLIPYRCD LSNEEDILSM FSAIRSQHSG VDICINNAGL ARPDTLLSGS TSGWKDMFNV
     NVLALSICTR EAYQSMKERN VDDGHIININ SMSGHRVLPL SVTHFYSATK YAVTALTEGL
     RQELREAQTH IRATCISPGV VETQFAFKLH DKDPEKAAAT YEQMKCLKPE DVAEAVIYVL
     STPAHIQIGD IQMRPTEQVT
//