DHR11_CHICK
ID DHR11_CHICK Reviewed; 255 AA.
AC Q71R50;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RA Kato A., Shintani T., Noda M.;
RT "A novel short-chain dehydrogenase/reductase.";
RL Submitted (APR-2001) 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; AF373778; AAQ02772.1; -; mRNA.
DR RefSeq; NP_989838.1; NM_204507.1.
DR AlphaFoldDB; Q71R50; -.
DR SMR; Q71R50; -.
DR STRING; 9031.ENSGALP00000008664; -.
DR PaxDb; Q71R50; -.
DR Ensembl; ENSGALT00000008678; ENSGALP00000008664; ENSGALG00000005403.
DR GeneID; 395172; -.
DR KEGG; gga:395172; -.
DR CTD; 79154; -.
DR VEuPathDB; HostDB:geneid_395172; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00840000129887; -.
DR HOGENOM; CLU_010194_2_10_1; -.
DR InParanoid; Q71R50; -.
DR OMA; WRWMWET; -.
DR OrthoDB; 1190834at2759; -.
DR PhylomeDB; Q71R50; -.
DR TreeFam; TF324174; -.
DR UniPathway; UPA00769; -.
DR PRO; PR:Q71R50; -.
DR Proteomes; UP000000539; Chromosome 19.
DR Bgee; ENSGALG00000005403; Expressed in kidney and 13 other tissues.
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; IEA:Ensembl.
DR GO; GO:0072555; F:17-beta-ketosteroid reductase activity; IEA:Ensembl.
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; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Lipid metabolism; NADP; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Secreted; Signal; Steroid metabolism.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..255
FT /note="Dehydrogenase/reductase SDR family member 11"
FT /id="PRO_0000045492"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
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; 27727 MW; 352DD8E97019B748 CRC64;
MERWTGRVAL VTGASVGIGA AVARALVQHG MKVVGCARSV DKIEKLAAEC QSAGYPGTLI
PYKCDLSNEE EILSMFSAIK TLHQGVDVCI NNAGLARPEP LLSGKTEGWR TMIDVNVMAV
SICTREAYQS MKERNIDDGH IININSMNGH SVVPQSVVHF YSATKYAVTA LTEGLRQELR
EAKTHIRATC ISPGLVETGF AFKLHDNDPE RAAATYESIR CLKAEDMANA VIYVLSAPPH
VQIGDIQMRP TEQIS
