DHB11_MACFA
ID DHB11_MACFA Reviewed; 300 AA.
AC Q4JK73;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
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;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu H., Labrie F., Luu-The V.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9EQ06}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q9EQ06}. Note=Redistributed from the endoplasmic
CC reticulum to lipids droplets in the cell upon induction of lipids
CC droplet formation. {ECO:0000250|UniProtKB:Q9EQ06}.
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; DQ078724; AAY84570.1; -; mRNA.
DR RefSeq; NP_001271762.1; NM_001284833.1.
DR AlphaFoldDB; Q4JK73; -.
DR SMR; Q4JK73; -.
DR STRING; 9541.XP_005555426.1; -.
DR GeneID; 102131126; -.
DR CTD; 51170; -.
DR eggNOG; KOG1201; Eukaryota.
DR OrthoDB; 1373099at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW NADP; Oxidoreductase; Reference proteome; Signal; Steroid biosynthesis.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..300
FT /note="Estradiol 17-beta-dehydrogenase 11"
FT /id="PRO_0000042582"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40..67
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 300 AA; 32920 MW; 25B38CCF2A8A5D8D CRC64;
MKILLDLLLL LPLLIVCCLE SFVKLFIPKR RKSVAGEIVL ITGAGHGIGR LTAYEFAKLK
SKLVLWDINK HGLEETAAKC KGLGAKVYTF VVDCSNREDI YSSAKKVKAE IGDVSILVNN
AGVVYTSDLF ATQDAQIEKT FEVNILAHFW TTKAFLPAMM KNNHGHVVTV ASAAGHISVP
FLLAYCSSKF SAVGFHKALT DELAALQITG VKTTCLCPNF VNTGFIKNPS TSLGPALEPE
EVVNRLMNGI LTEQKMIFSP SSIAFLTILE RILPERFLAV LKRKINIKFD AVIGYKMKAQ