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Dehydrogenase/reductase SDR family member 11 (17-beta-hydroxysteroid dehydrogenase) (3-beta-hydroxysteroid 3-dehydrogenase) (EC 1.1.1.270) (Estradiol 17-beta-dehydrogenase) (EC 1.1.1.62) (Short-chain dehydrogenase/reductase family 24C member 1)

 DHR11_HUMAN             Reviewed;         260 AA.
Q6UWP2; A0A0U5BLD0; B2RDZ3; Q9BUC7; Q9H674;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 128.
RecName: Full=Dehydrogenase/reductase SDR family member 11;
AltName: Full=17-beta-hydroxysteroid dehydrogenase {ECO:0000305|PubMed:26920053};
AltName: Full=3-beta-hydroxysteroid 3-dehydrogenase {ECO:0000305|PubMed:26920053};
EC=1.1.1.270 {ECO:0000269|PubMed:26920053};
AltName: Full=Estradiol 17-beta-dehydrogenase {ECO:0000305|PubMed:26920053};
EC=1.1.1.62 {ECO:0000269|PubMed:26920053};
AltName: Full=Short-chain dehydrogenase/reductase family 24C member 1 {ECO:0000303|PubMed:19027726};
Flags: Precursor;
Name=DHRS11; Synonyms=SDR24C1 {ECO:0000303|PubMed:19027726};
ORFNames=UNQ836/PRO1774;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, CATALYTIC ACTIVITY,
ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
SPECIFICITY.
PubMed=26920053; DOI=10.1016/j.bbrc.2016.01.190;
Endo S., Miyagi N., Matsunaga T., Hara A., Ikari A.;
"Human dehydrogenase/reductase (SDR family) member 11 is a novel type
of 17beta-hydroxysteroid dehydrogenase.";
Biochem. Biophys. Res. Commun. 472:231-236(2016).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain cortex, and Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 1-256 (ISOFORM 1) IN COMPLEX
WITH NADP AND ACETATE, AND SUBUNIT.
Structural genomics consortium (SGC);
"Structure of the putative human dehydrogenase MGC4172.";
Submitted (OCT-2004) to the PDB data bank.
[9]
GENE FAMILY, AND NOMENCLATURE.
PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M.,
Thornton J.M., Adamski J., Oppermann U.;
"The SDR (short-chain dehydrogenase/reductase and related enzymes)
nomenclature initiative.";
Chem. Biol. Interact. 178:94-98(2009).
-!- FUNCTION: Catalyzes the conversion of the 17-keto group of
estrone, 4- and 5-androstenes and 5-alpha-androstanes into their
17-beta-hydroxyl metabolites and the conversion of the 3-keto
group of 3-, 3,17- and 3,20- diketosteroids into their 3-hydroxyl
metabolites. Exhibits reductive 3-beta-hydroxysteroid
dehydrogenase activity toward 5-beta-androstanes, 5-beta-
pregnanes, 4-pregnenes and bile acids. May also reduce endogenous
and exogenous alpha-dicarbonyl compounds and xenobiotic alicyclic
ketones. {ECO:0000269|PubMed:26920053}.
-!- CATALYTIC ACTIVITY: A 3-beta-hydroxysteroid + NADP(+) = a 3-
oxosteroid + NADPH. {ECO:0000269|PubMed:26920053}.
-!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone +
NAD(P)H. {ECO:0000269|PubMed:26920053}.
-!- ENZYME REGULATION: Inhibited by flavonoids including apigenin,
luteolin, genistein, kaempferol and quercetin and also by
carbenoxolone, zearalenone, glycyrrhetinic, curcumin and
flufenamic acid. {ECO:0000269|PubMed:26920053}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.1 uM for NADPH {ECO:0000269|PubMed:26920053};
KM=0.7 uM for estrone (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=1.3 uM for 5-alpha-androstan-3-alpha-ol-17-one (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=2.2 uM for 5-alpha-androstan-3-beta-ol-17-one (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=11 uM for dehydroepiandrosterone (DHEA) (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=12 uM for DHEA sulfate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=19 uM for 4-androsten-3-alpha-ol-17-one (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=0.7 uM for 5-beta-pregnan-20-beta-ol-3-one (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=1.1 uM for dehydrolithocholic acid (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=5.2 uM for 5-beta-cholanic acid-3,7-dione (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=5.1 uM for 20-alpha-hydroxyprogesterone (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=44 uM for taurodehydrocholic acid (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=29 uM for dehydrocholic acid (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=102 uM for 5-beta-dihydrotestosterone (DHT) (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=5.2 uM for 5-beta-androstane-3,17-dione (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=4.6 uM for 4-androstene-3,17-dione (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=12 uM for 5-alpha-androstane-3,17-dione (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=2.1 uM for 5-beta-pregnane-21-ol-3,20-dione (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=3.4 uM for progesterone (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=15 uM for 5-beta-pregnane-3,20-dione (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=16 uM for 17-beta-estradiol (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=30 uM for testosterone (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=23 uM for 4-androstene-3-alpha,17-beta-diol (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=11 uM for 5-androstene-3-alpha,17-beta-diol (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=26 uM for 5-alpha-dihydrotestosterone (DHT) (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=9.2 uM for 5-alpha-androstane-3-alpha,17-beta-diol (at 37
degrees Celsius) {ECO:0000269|PubMed:26920053};
KM=1.1 uM for 5-alpha-androstane-3-beta,17-beta-diol (at 37
degrees Celsius) {ECO:0000269|PubMed:26920053};
KM=36 uM for 5-beta-androstan-3-beta-ol-17-one (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=12 uM for 5-beta-androstane-3-beta,17-beta-diol (at 37
degrees Celsius) {ECO:0000269|PubMed:26920053};
KM=22 uM for 3-beta-hydroxyprogesterone (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=36 uM for 5-beta-pregnan-3-beta-ol-20-one (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=14 uM for 5-beta-pregnane-3-beta,20-beta-diol (at 37 degrees
Celsius) {ECO:0000269|PubMed:26920053};
KM=4.7 uM for 5-beta-pregnane-3-beta,21-diol-20-one (at 37
degrees Celsius) {ECO:0000269|PubMed:26920053};
KM=0.4 uM for isolithocholic acid (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=60 uM for 1-phenyl-1,2-propanedione (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=620 uM for 2,3-hexanedione (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=201 uM for 2,3-heptanedione (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=420 uM for 3,4-hexanedione (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=178 uM for alpha-tetralone (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
KM=740 uM for loxoprofen (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=43 nmol/min/mg enzyme with estrone as substrate (at 37
degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=42 nmol/min/mg enzyme with 5-alpha-androstan-3-alpha-ol-17-
one as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=49 nmol/min/mg enzyme with 5-alpha-androstan-3-beta-ol-17-
one as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=118 nmol/min/mg enzyme with dehydroepiandrosterone (DHEA)
as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=60 nmol/min/mg enzyme with DHEA sulfate as substrate (at 37
degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=43 nmol/min/mg enzyme with 4-androsten-3-alpha-ol-17-one as
substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=44 nmol/min/mg enzyme with 5-beta-pregnan-20-beta-ol-3-one
as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=44 nmol/min/mg enzyme with dehydrolithocholic acid as
substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=85 nmol/min/mg enzyme with 5-beta-cholanic acid-3,7-dione
as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=40 nmol/min/mg enzyme with 20-alpha-hydroxyprogesterone as
substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=200 nmol/min/mg enzyme with taurodehydrocholic acid as
substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=119 nmol/min/mg enzyme with dehydrocholic acid as substrate
(at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=389 nmol/min/mg enzyme with 5-beta-dihydrotestosterone
(DTH) as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=62 nmol/min/mg enzyme with 5-beta-androstane-3,17-dione as
substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=52 nmol/min/mg enzyme with 4-androstene-3,17-dione as
substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=57 nmol/min/mg enzyme with 5-alpha-androstane-3,17-dione as
substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=49 nmol/min/mg enzyme with 5-beta-pregnane-21-ol-3,20-dione
as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=36 nmol/min/mg enzyme with progesterone as substrate (at 37
degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=123 nmol/min/mg enzyme with 5-beta-pregnane-3,20-dione as
substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=246 nmol/min/mg enzyme with 17-beta-estradiol as substrate
(at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=238 nmol/min/mg enzyme with testosterone as substrate (at
37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=33 nmol/min/mg enzyme with 4-androstene-3-alpha,17-beta-
diol as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=366 nmol/min/mg enzyme with 5-androstene-3-alpha,17-beta-
diol as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=117 nmol/min/mg enzyme with 5-alpha-dihydrotestosterone
(DHT) as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=40 nmol/min/mg enzyme with 5-alpha-androstane-3-alpha,17-
beta-diol as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=96 nmol/min/mg enzyme with 5-alpha-androstane-3-beta,17-
beta-diol as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=137 nmol/min/mg enzyme with 5-beta-androstan-3-beta-ol-17-
one as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=511 nmol/min/mg enzyme with 5-beta-androstane-3-beta,17-
beta-diol as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=364 nmol/min/mg enzyme with 3-beta-hydroxyprogesterone as
substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=268 nmol/min/mg enzyme with 5-beta-pregnan-3-beta-ol-20-one
as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=220 nmol/min/mg enzyme with 5-beta-pregnane-3-beta,20-beta-
diol as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=96 nmol/min/mg enzyme with 5-beta-pregnane-3-beta,21-diol-
20-one as substrate (at 37 degrees Celsius)
{ECO:0000269|PubMed:26920053};
Vmax=28 nmol/min/mg enzyme with isolithocholic acid as substrate
(at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=69 nmol/min/mg enzyme with 1-phenyl-1,2-propanedione as
substrate (at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=331 nmol/min/mg enzyme with 2,3-hexanedione as substrate
(at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=86 nmol/min/mg enzyme with 2,3-heptanedione as substrate
(at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=166 nmol/min/mg enzyme with 3,4-hexanedione as substrate
(at 37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=67 nmol/min/mg enzyme with alpha-tetralone as substrate (at
37 degrees Celsius) {ECO:0000269|PubMed:26920053};
Vmax=51 nmol/min/mg enzyme with loxoprofen as substrate (at 37
degrees Celsius) {ECO:0000269|PubMed:26920053};
-!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
{ECO:0000305|PubMed:26920053}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.8}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q6UWP2-1; Sequence=Displayed;
Name=2;
IsoId=Q6UWP2-2; Sequence=VSP_016987;
Name=3;
IsoId=Q6UWP2-3; Sequence=VSP_059104;
-!- TISSUE SPECIFICITY: Isoform 1: Ubiquitously expressed, with
highest levels in testis, small intestine, colon, kidney, brain
and heart. Isoform 3: Expressed in brain, heart and skeletal
muscle. {ECO:0000269|PubMed:26920053}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
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EMBL; LC110386; BAU36404.1; -; mRNA.
EMBL; AY358712; AAQ89074.1; -; mRNA.
EMBL; AK026196; BAB15390.1; -; mRNA.
EMBL; AK315735; BAG38090.1; -; mRNA.
EMBL; CR457356; CAG33637.1; -; mRNA.
EMBL; CH471199; EAW57568.1; -; Genomic_DNA.
EMBL; BC002731; AAH02731.2; -; mRNA.
CCDS; CCDS11315.2; -. [Q6UWP2-1]
RefSeq; NP_077284.2; NM_024308.3. [Q6UWP2-1]
RefSeq; XP_005257715.1; XM_005257658.2.
UniGene; Hs.462859; -.
PDB; 1XG5; X-ray; 1.53 A; A/B/C/D=1-256.
PDBsum; 1XG5; -.
ProteinModelPortal; Q6UWP2; -.
SMR; Q6UWP2; -.
BioGrid; 122572; 5.
IntAct; Q6UWP2; 1.
STRING; 9606.ENSP00000251312; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
iPTMnet; Q6UWP2; -.
PhosphoSitePlus; Q6UWP2; -.
BioMuta; DHRS11; -.
DMDM; 74749397; -.
EPD; Q6UWP2; -.
MaxQB; Q6UWP2; -.
PaxDb; Q6UWP2; -.
PeptideAtlas; Q6UWP2; -.
PRIDE; Q6UWP2; -.
Ensembl; ENST00000611337; ENSP00000477603; ENSG00000278535. [Q6UWP2-2]
Ensembl; ENST00000618403; ENSP00000482704; ENSG00000278535. [Q6UWP2-1]
Ensembl; ENST00000621143; ENSP00000483747; ENSG00000275397. [Q6UWP2-1]
Ensembl; ENST00000631686; ENSP00000488610; ENSG00000275397. [Q6UWP2-2]
GeneID; 79154; -.
KEGG; hsa:79154; -.
UCSC; uc002hnd.4; human. [Q6UWP2-1]
CTD; 79154; -.
EuPathDB; HostDB:ENSG00000278535.4; -.
GeneCards; DHRS11; -.
HGNC; HGNC:28639; DHRS11.
HPA; HPA041226; -.
HPA; HPA048236; -.
HPA; HPA053623; -.
MIM; 616159; gene.
neXtProt; NX_Q6UWP2; -.
OpenTargets; ENSG00000278535; -.
PharmGKB; PA164718841; -.
eggNOG; ENOG410IUBV; Eukaryota.
eggNOG; COG4221; LUCA.
GeneTree; ENSGT00840000129887; -.
HOVERGEN; HBG105262; -.
InParanoid; Q6UWP2; -.
OMA; NAGITTH; -.
OrthoDB; EOG091G0J8P; -.
PhylomeDB; Q6UWP2; -.
TreeFam; TF324174; -.
UniPathway; UPA00769; -.
ChiTaRS; DHRS11; human.
EvolutionaryTrace; Q6UWP2; -.
GenomeRNAi; 79154; -.
PRO; PR:Q6UWP2; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000278535; -.
ExpressionAtlas; Q6UWP2; baseline and differential.
Genevisible; Q6UWP2; HS.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; IDA:UniProtKB.
GO; GO:0072555; F:17-beta-ketosteroid reductase activity; IDA:UniProtKB.
GO; GO:0000253; F:3-keto sterol reductase activity; IDA:UniProtKB.
GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:UniProtKB.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0006703; P:estrogen biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006694; P:steroid biosynthetic process; IDA:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Lipid metabolism; NADP; Nucleotide-binding; Oxidoreductase;
Reference proteome; Secreted; Signal; Steroid metabolism.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 260 Dehydrogenase/reductase SDR family member
11.
/FTId=PRO_0000045490.
NP_BIND 18 23 NADP. {ECO:0000244|PDB:1XG5}.
NP_BIND 43 44 NADP. {ECO:0000244|PDB:1XG5}.
NP_BIND 70 71 NADP. {ECO:0000244|PDB:1XG5}.
NP_BIND 201 204 NADP. {ECO:0000244|PDB:1XG5}.
ACT_SITE 166 166 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 49 49 NADP. {ECO:0000244|PDB:1XG5}.
BINDING 97 97 NADP; via carbonyl oxygen.
{ECO:0000244|PDB:1XG5}.
BINDING 151 151 Substrate. {ECO:0000244|PDB:1XG5}.
BINDING 166 166 NADP. {ECO:0000244|PDB:1XG5}.
BINDING 166 166 Substrate. {ECO:0000244|PDB:1XG5}.
BINDING 170 170 NADP. {ECO:0000244|PDB:1XG5}.
BINDING 208 208 NADP. {ECO:0000244|PDB:1XG5}.
VAR_SEQ 1 79 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.4}.
/FTId=VSP_016987.
VAR_SEQ 196 226 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_059104.
CONFLICT 81 81 F -> S (in Ref. 3; BAB15390 and 4;
CAG33637). {ECO:0000305}.
HELIX 7 9 {ECO:0000244|PDB:1XG5}.
STRAND 13 18 {ECO:0000244|PDB:1XG5}.
HELIX 22 33 {ECO:0000244|PDB:1XG5}.
STRAND 37 43 {ECO:0000244|PDB:1XG5}.
HELIX 45 57 {ECO:0000244|PDB:1XG5}.
STRAND 61 68 {ECO:0000244|PDB:1XG5}.
HELIX 74 88 {ECO:0000244|PDB:1XG5}.
STRAND 92 96 {ECO:0000244|PDB:1XG5}.
TURN 106 108 {ECO:0000244|PDB:1XG5}.
HELIX 111 121 {ECO:0000244|PDB:1XG5}.
HELIX 123 138 {ECO:0000244|PDB:1XG5}.
STRAND 145 149 {ECO:0000244|PDB:1XG5}.
HELIX 152 154 {ECO:0000244|PDB:1XG5}.
HELIX 161 163 {ECO:0000244|PDB:1XG5}.
HELIX 164 186 {ECO:0000244|PDB:1XG5}.
STRAND 192 199 {ECO:0000244|PDB:1XG5}.
HELIX 205 209 {ECO:0000244|PDB:1XG5}.
TURN 210 212 {ECO:0000244|PDB:1XG5}.
HELIX 214 221 {ECO:0000244|PDB:1XG5}.
HELIX 229 241 {ECO:0000244|PDB:1XG5}.
STRAND 246 255 {ECO:0000244|PDB:1XG5}.
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


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