DH12B_XENLA
ID DH12B_XENLA Reviewed; 318 AA.
AC Q8AVY8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Very-long-chain 3-oxoacyl-CoA reductase-B {ECO:0000305};
DE EC=1.1.1.330 {ECO:0000250|UniProtKB:Q53GQ0};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 12-B {ECO:0000250|UniProtKB:Q53GQ0};
DE Short=17-beta-HSD 12-B {ECO:0000250|UniProtKB:Q53GQ0};
DE AltName: Full=3-ketoacyl-CoA reductase {ECO:0000250|UniProtKB:Q53GQ0};
DE Short=KAR {ECO:0000250|UniProtKB:Q53GQ0};
DE AltName: Full=Estradiol 17-beta-dehydrogenase 12-B {ECO:0000250|UniProtKB:Q53GQ0};
DE EC=1.1.1.62 {ECO:0000250|UniProtKB:Q53GQ0};
GN Name=hsd17b12-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the second of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of two carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has
CC a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-
CC hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby,
CC it may participate in the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators. May also catalyze
CC the transformation of estrone (E1) into estradiol (E2) and play a role
CC in estrogen formation. {ECO:0000250|UniProtKB:Q53GQ0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-
CC long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330;
CC Evidence={ECO:0000250|UniProtKB:Q53GQ0};
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:Q53GQ0};
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:Q53GQ0};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q53GQ0}.
CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC {ECO:0000250|UniProtKB:Q53GQ0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q53GQ0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53GQ0}.
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; BC041194; AAH41194.1; -; mRNA.
DR RefSeq; NP_001080055.1; NM_001086586.2.
DR AlphaFoldDB; Q8AVY8; -.
DR SMR; Q8AVY8; -.
DR BioGRID; 97989; 1.
DR DNASU; 379747; -.
DR GeneID; 379747; -.
DR KEGG; xla:379747; -.
DR CTD; 379747; -.
DR Xenbase; XB-GENE-945234; hsd17b12.S.
DR OrthoDB; 913128at2759; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00769; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 379747; Expressed in internal ear and 20 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0102339; F:3-oxo-arachidoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102340; F:3-oxo-behenoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102342; F:3-oxo-cerotoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102341; F:3-oxo-lignoceroyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006633; P:fatty acid 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 Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW NADP; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..318
FT /note="Very-long-chain 3-oxoacyl-CoA reductase-B"
FT /id="PRO_0000248374"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 54..83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 318 AA; 34861 MW; A5D8971F8AE72AD0 CRC64;
MAPESLAEVP GCNCFWYLGV VAATWWGLRA AWCLLNGARV WVLGSGAQVG PTIGKWAVVT
GATDGIGKAY AEELARRGMN IVLISRSPEK LEEAAIHIKQ KFKVETKIIA ADFGKPTEIY
ERIEAGLRDL EIGVLVNNVG ISYEYPEYFL EIPDLENTLD KMININIMSV CQMTRLVLPG
MLGRGKGVVL NISSASGMYP VPLLTVYSAT KAFVDFFSRG LHAEYRSKGV TVQSVLPFFV
ATKLAKIRKP TWDKPSPETY VRSALNTVGL QTQTNGYLPH AITGWISTSL VPVSAAISMG
MKMNKGLRAR FLKKAKQN
