DHB7_RAT
ID DHB7_RAT Reviewed; 334 AA.
AC Q62904;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7 {ECO:0000305};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 7;
DE Short=17-beta-HSD 7;
DE AltName: Full=3-keto-steroid reductase;
DE EC=1.1.1.270 {ECO:0000305|PubMed:6946726};
DE AltName: Full=Dihydrotestosterone oxidoreductase;
DE EC=1.1.1.210 {ECO:0000250|UniProtKB:P56937};
DE AltName: Full=Estradiol 17-beta-dehydrogenase 7;
DE EC=1.1.1.62 {ECO:0000269|PubMed:9658408};
DE AltName: Full=PRL receptor-associated protein {ECO:0000303|PubMed:8663045};
DE Short=PRAP {ECO:0000303|PubMed:8663045};
GN Name=Hsd17b7;
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], PROTEIN SEQUENCE OF 1-18, TISSUE SPECIFICITY,
RP SUBUNIT, AND PHOSPHORYLATION.
RC STRAIN=Sprague-Dawley; TISSUE=Corpus luteum;
RX PubMed=8663045; DOI=10.1074/jbc.271.26.15602;
RA Duan W.R., Linzer D.I.H., Gibori G.;
RT "Cloning and characterization of an ovarian-specific protein that
RT associates with the short form of the prolactin receptor.";
RL J. Biol. Chem. 271:15602-15607(1996).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6946726; DOI=10.1016/0003-9861(81)90474-4;
RA Billheimer J.T., Alcorn M., Gaylor J.L.;
RT "Solubilization and partial purification of a microsomal 3-ketosteroid
RT reductase of cholesterol biosynthesis.";
RL Arch. Biochem. Biophys. 211:430-438(1981).
RN [3]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=9658408; DOI=10.1210/mend.12.7.0134;
RA Nokelainen P., Peltoketo H., Vihko R., Vihko P.;
RT "Expression cloning of a novel estrogenic mouse 17 beta-hydroxysteroid
RT dehydrogenase/17-ketosteroid reductase (m17HSD7), previously described as a
RT prolactin receptor-associated protein (PRAP) in rat.";
RL Mol. Endocrinol. 12:1048-1059(1998).
CC -!- FUNCTION: Bifunctional enzyme involved in steroid-hormone metabolism
CC and cholesterol biosynthesis (PubMed:6946726, PubMed:9658408).
CC Catalyzes the NADP(H)-dependent reduction of estrogens and androgens
CC and regulates the biological potency of these steroids (PubMed:9658408)
CC (By similarity). Converts estrone (E1) to a more potent estrogen,
CC 17beta-estradiol (E2) (PubMed:9658408). Converts dihydrotestosterone
CC (DHT) to an inactive form. Participates also in the post-squalene
CC cholesterol biosynthesis, as a 3-ketosteroid reductase (By similarity).
CC {ECO:0000250|UniProtKB:P56937, ECO:0000269|PubMed:6946726,
CC ECO:0000269|PubMed:9658408}.
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:9658408};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24618;
CC Evidence={ECO:0000305|PubMed:9658408};
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:0000305|PubMed:6946726};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34789;
CC Evidence={ECO:0000305|PubMed:6946726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP(+) = 4alpha-
CC methyl-5alpha-cholest-7-en-3-one + H(+) + NADPH;
CC Xref=Rhea:RHEA:18409, ChEBI:CHEBI:15378, ChEBI:CHEBI:16495,
CC ChEBI:CHEBI:18378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.270; Evidence={ECO:0000305|PubMed:6946726};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18411;
CC Evidence={ECO:0000305|PubMed:6946726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4alpha-methyl-5alpha-cholest-8-en-3-one + H(+) + NADPH =
CC 4alpha-methyl-5alpha-cholest-8-en-3beta-ol + NADP(+);
CC Xref=Rhea:RHEA:46832, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87050, ChEBI:CHEBI:87051;
CC Evidence={ECO:0000250|UniProtKB:P56937};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46833;
CC Evidence={ECO:0000250|UniProtKB:P56937};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-4alpha-methylzymosterol + H(+) + NADPH = 4alpha-
CC methylzymosterol + NADP(+); Xref=Rhea:RHEA:36379, ChEBI:CHEBI:1949,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:136486; EC=1.1.1.270;
CC Evidence={ECO:0000250|UniProtKB:P56937};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36380;
CC Evidence={ECO:0000250|UniProtKB:P56937};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + zymosterone = NADP(+) + zymosterol;
CC Xref=Rhea:RHEA:33459, ChEBI:CHEBI:15378, ChEBI:CHEBI:18252,
CC ChEBI:CHEBI:52386, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P56937};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33460;
CC Evidence={ECO:0000250|UniProtKB:P56937};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-cholest-8-en-3-one + H(+) + NADPH = 5alpha-cholest-8-
CC en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46852, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:87056; Evidence={ECO:0000250|UniProtKB:P56937};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46853;
CC Evidence={ECO:0000250|UniProtKB:P56937};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3beta,17beta-diol + NADP(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:16297,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.210;
CC Evidence={ECO:0000250|UniProtKB:P56937};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16299;
CC Evidence={ECO:0000250|UniProtKB:P56937};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3alpha,17beta-diol + NADP(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:42116,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:O88736};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42118;
CC Evidence={ECO:0000250|UniProtKB:O88736};
CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC {ECO:0000269|PubMed:9658408}.
CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC lanosterol: step 5/6. {ECO:0000250|UniProtKB:P56937}.
CC -!- SUBUNIT: Binds to the short form of prolactin receptor.
CC {ECO:0000269|PubMed:8663045}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P56937}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Most abundant in ovaries of pregnant animals.
CC {ECO:0000269|PubMed:8663045}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:8663045}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. ERG27 subfamily. {ECO:0000305}.
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DR EMBL; U44803; AAC52623.1; -; mRNA.
DR RefSeq; NP_058931.1; NM_017235.3.
DR AlphaFoldDB; Q62904; -.
DR SMR; Q62904; -.
DR STRING; 10116.ENSRNOP00000003812; -.
DR SwissLipids; SLP:000001306; -.
DR GlyGen; Q62904; 3 sites.
DR iPTMnet; Q62904; -.
DR PhosphoSitePlus; Q62904; -.
DR PaxDb; Q62904; -.
DR PRIDE; Q62904; -.
DR GeneID; 29540; -.
DR KEGG; rno:29540; -.
DR UCSC; RGD:2837; rat.
DR CTD; 51478; -.
DR RGD; 2837; Hsd17b7.
DR eggNOG; KOG1478; Eukaryota.
DR HOGENOM; CLU_029944_2_0_1; -.
DR InParanoid; Q62904; -.
DR OMA; ASYEGSK; -.
DR PhylomeDB; Q62904; -.
DR TreeFam; TF105433; -.
DR Reactome; R-RNO-191273; Cholesterol biosynthesis.
DR UniPathway; UPA00769; -.
DR UniPathway; UPA00770; UER00758.
DR PRO; PR:Q62904; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q62904; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0000253; F:3-keto sterol reductase activity; ISS:UniProtKB.
DR GO; GO:0047024; F:5alpha-androstane-3beta,17beta-diol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0102176; F:cycloeucalenone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0005148; F:prolactin receptor binding; IPI:RGD.
DR GO; GO:0008209; P:androgen metabolic process; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0006695; P:cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0048568; P:embryonic organ development; ISO:RGD.
DR GO; GO:0048706; P:embryonic skeletal system development; ISO:RGD.
DR GO; GO:0006703; P:estrogen biosynthetic process; IDA:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:1990637; P:response to prolactin; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR CDD; cd08941; 3KS_SDR_c; 1.
DR InterPro; IPR042829; HSD17B7/Erg27.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NAD; NADP; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..334
FT /note="3-keto-steroid reductase/17-beta-hydroxysteroid
FT dehydrogenase 7"
FT /id="PRO_0000054588"
FT TOPO_DOM 1..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 8..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 334 AA; 37372 MW; 448B546CE8FCBFAC CRC64;
MRKVVLITGA SSGIGLALCG RLLAEDDDLH LCLACRNLSK AGAVRDALLA SHPSAEVSIV
QMDVSNLQSV VRGAEEVKRR FQRLDYLYLN AGIMPNPQLN LKAFFCGIFS RNVIHMFSTA
EGLLTQNDKI TADGFQEVFE TNLFGHFILI RELEPLLCHS DNPSQLIWTS SRNAKKSNFS
LEDIQHAKGQ EPYSSSKYAT DLLNVALNRN FNQKGLYSSV TCPGVVMTNL TYGILPPFVW
TLLLPVIWLL RFFAHAFTVT PYNGAEALVW LFHQKPESLN PLTKYLSGTT GLGTNYVKGQ
KMDVDEDTAE KFYKTLLELE KQVRITIQKS DHHS
