DHR11_BOVIN
ID DHR11_BOVIN Reviewed; 255 AA.
AC Q3ZBV9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BC103081; AAI03082.1; -; mRNA.
DR RefSeq; NP_001030260.1; NM_001035088.2.
DR AlphaFoldDB; Q3ZBV9; -.
DR SMR; Q3ZBV9; -.
DR STRING; 9913.ENSBTAP00000013600; -.
DR PaxDb; Q3ZBV9; -.
DR PeptideAtlas; Q3ZBV9; -.
DR PRIDE; Q3ZBV9; -.
DR GeneID; 510264; -.
DR KEGG; bta:510264; -.
DR CTD; 79154; -.
DR eggNOG; KOG1205; Eukaryota.
DR HOGENOM; CLU_010194_2_10_1; -.
DR InParanoid; Q3ZBV9; -.
DR OrthoDB; 1190834at2759; -.
DR TreeFam; TF324174; -.
DR UniPathway; UPA00769; -.
DR Proteomes; UP000009136; Unplaced.
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:0000253; F:3-keto sterol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102176; F:cycloeucalenone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Lipid metabolism; NADP; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Secreted; Signal; Steroid metabolism.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..255
FT /note="Dehydrogenase/reductase SDR family member 11"
FT /id="PRO_0000045489"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 13..18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 38..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 65..66
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 196..199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
FT BINDING 203
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6UWP2"
SQ SEQUENCE 255 AA; 27811 MW; 6AD331DA1DA09062 CRC64;
MERWRDRLAL VTGASGGIGA AVARALVQQG LKVVGCARTV GNIEELAAEC KSAGYPGTLI
PYRCDLSNEE DILSMFSAVR SQHSGVDICI NNAGLARPDT LLSGSTSGWK EMFNVNVLAL
SICTREACQS MRERKVDDGH IININSMCGH RVPPPAETHF YSATKYAVTA LTEGLRQELR
EARSHIRATC ISPGVVETQF AFKLHDKDPE KAAATYEHMK CLKPEDVAEA VIYVLSTPPH
VQIGDIQMRP TEQVT
