ID   DHB11_PONAB             Reviewed;         300 AA.
AC   Q5NVG2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Dehydrogenase/reductase SDR family member 8;
DE   Flags: Precursor;
GN   Name=HSD17B11; Synonyms=DHRS8;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR926074; CAI29701.1; -; mRNA.
DR   RefSeq; NP_001127691.1; NM_001134219.1.
DR   AlphaFoldDB; Q5NVG2; -.
DR   SMR; Q5NVG2; -.
DR   STRING; 9601.ENSPPYP00000016651; -.
DR   GeneID; 100174773; -.
DR   KEGG; pon:100174773; -.
DR   CTD; 51170; -.
DR   eggNOG; KOG1201; Eukaryota.
DR   InParanoid; Q5NVG2; -.
DR   OrthoDB; 1373099at2759; -.
DR   Proteomes; UP000001595; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..300
FT                   /note="Estradiol 17-beta-dehydrogenase 11"
FT                   /id="PRO_0000031972"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..64
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  32992 MW;  982412E8EEE44083 CRC64;
     MKFLLDVLLL LPLLIVCSLE SFVKLFIPKR RKSVTGEIVL ITGAGHGIGR LTAYEFAKLK
     SKLVLWDINK HGLEETAAKC KGLGAKVHTF VVDCSNREDI YSAAKKVKAE IGDVSILVNN
     AGVVYTSDLF ATQDPQIEKT FEVNVLAHFW TTKAFLPAMM KNNHGHIVTV ASAAGHVSVP
     FLLAYCSSKF AAVGFHKTLT DELAALQITG VKTTCLCPNF VNTGFIKNPS TSLGPTLEPE
     EVVNRLMHGI LTEQKMIFIP SSIAFLTTLE RILPERFLAV LKRKISVKFD AVIGYRMKAQ