DHB1_RAT
ID DHB1_RAT Reviewed; 344 AA.
AC P51657;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Estradiol 17-beta-dehydrogenase 1;
DE EC=1.1.1.62;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase type 1;
DE Short=17-beta-HSD 1;
GN Name=Hsd17b1; Synonyms=Edh17b1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=7925110; DOI=10.1210/endo.135.4.7925110;
RA Ghersevich S., Nokelainen P., Poutanen M., Orava M., Autio-Harmainen H.,
RA Rajaniemi H., Vihko R.;
RT "Rat 17 beta-hydroxysteroid dehydrogenase type 1: primary structure and
RT regulation of enzyme expression in rat ovary by diethylstilbestrol and
RT gonadotropins in vivo.";
RL Endocrinology 135:1477-1487(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8612487; DOI=10.1210/endo.137.5.8612487;
RA Akinola L.A., Poutanen M., Vihko R.;
RT "Cloning of rat 17 beta-hydroxysteroid dehydrogenase type 2 and
RT characterization of tissue distribution and catalytic activity of rat type
RT 1 and type 2 enzymes.";
RL Endocrinology 137:1572-1579(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9524272; DOI=10.1016/s0378-1119(97)00669-0;
RA Akinola L.A., Poutanen M., Peltoketo H., Vihko R., Vihko P.;
RT "Characterization of rat 17 beta-hydroxysteroid dehydrogenase type 1 gene
RT and mRNA transcripts.";
RL Gene 208:229-238(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Favors the reduction of estrogens and androgens. Uses
CC preferentially NADH.
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:0000269|PubMed:7925110};
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:0000269|PubMed:7925110};
CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; X78811; CAA55389.1; -; mRNA.
DR EMBL; X97754; CAA66349.1; -; mRNA.
DR EMBL; X98038; CAA66657.1; -; Genomic_DNA.
DR EMBL; BC086365; AAH86365.1; -; mRNA.
DR PIR; S57901; S57901.
DR RefSeq; NP_036983.1; NM_012851.2.
DR AlphaFoldDB; P51657; -.
DR SMR; P51657; -.
DR STRING; 10116.ENSRNOP00000026878; -.
DR BindingDB; P51657; -.
DR ChEMBL; CHEMBL1914267; -.
DR PaxDb; P51657; -.
DR PRIDE; P51657; -.
DR Ensembl; ENSRNOT00000026878; ENSRNOP00000026878; ENSRNOG00000019830.
DR GeneID; 25322; -.
DR KEGG; rno:25322; -.
DR CTD; 3292; -.
DR RGD; 2836; Hsd17b1.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000160415; -.
DR HOGENOM; CLU_010194_2_9_1; -.
DR InParanoid; P51657; -.
DR OMA; QMDVTDR; -.
DR OrthoDB; 1313182at2759; -.
DR PhylomeDB; P51657; -.
DR Reactome; R-RNO-193144; Estrogen biosynthesis.
DR UniPathway; UPA00769; -.
DR PRO; PR:P51657; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000019830; Expressed in ovary and 18 other tissues.
DR Genevisible; P51657; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; ISO:RGD.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:RGD.
DR GO; GO:1903924; F:estradiol binding; ISO:RGD.
DR GO; GO:0050661; F:NADP binding; ISO:RGD.
DR GO; GO:0070401; F:NADP+ binding; ISO:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0005496; F:steroid binding; ISO:RGD.
DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IDA:RGD.
DR GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; ISO:RGD.
DR GO; GO:0060348; P:bone development; IEP:RGD.
DR GO; GO:0071248; P:cellular response to metal ion; IEP:RGD.
DR GO; GO:0006703; P:estrogen biosynthetic process; IDA:RGD.
DR GO; GO:0061370; P:testosterone biosynthetic process; IDA:RGD.
DR InterPro; IPR011348; 17beta_DH.
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 PIRSF; PIRSF000095; 17beta-HSD; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis.
FT CHAIN 1..344
FT /note="Estradiol 17-beta-dehydrogenase 1"
FT /id="PRO_0000054569"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 3..32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 344 AA; 36967 MW; CB5FC139FBB3995E CRC64;
MDSTVVLITG CSSGIGLHLA VRLASDRSQS FKVYATLRDL KSQGPLLEAA RAQGCPPGSL
EILELDVRDS ESVAAARACV TEGRVDVLVC NAGRGLFGPL EAHELNAVGA VLDVNVLGTI
RMLQAFLPDM KRRHSGRVLV TASVGGLMGL PFHEVYCASK FALEGLCESL AILLPLFGVH
VSLIECGAVH TAFHEKLEGG PGGALERADA QTRHLFAHYQ RGYEQALSEA QDPEEVTELF
LTAMRAPQPA LRYFSTNRFL PLARMRTEDP SGSSYVEAMH REAFSDLQVQ EGAKAGAQVS
GDPDTPPRAL ICLPECAIPR VTAELGWSAS DKPGQNKSCY QQKI
