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DHB1_MOUSE
ID   DHB1_MOUSE              Reviewed;         344 AA.
AC   P51656;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=17-beta-hydroxysteroid dehydrogenase type 1 {ECO:0000305};
DE            Short=17-beta-HSD 1;
DE            EC=1.1.1.51 {ECO:0000269|PubMed:9658408};
DE   AltName: Full=Estradiol 17-beta-dehydrogenase 1 {ECO:0000305};
DE            EC=1.1.1.62 {ECO:0000269|PubMed:9658408};
GN   Name=Hsd17b1 {ECO:0000312|MGI:MGI:105077}; Synonyms=Edh17b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=8612620; DOI=10.1111/j.1432-1033.1996.00482.x;
RA   Nokelainen P., Puranen T., Peltoketo H., Orava M., Vihko P., Vihko R.;
RT   "Molecular cloning of mouse 17 beta-hydroxysteroid dehydrogenase type 1 and
RT   characterization of enzyme activity.";
RL   Eur. J. Biochem. 236:482-490(1996).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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: Favors the reduction of estrogens and androgens. Converts
CC       estrone (E1) to a more potent estrogen, 17beta-estradiol (E2)
CC       (PubMed:9658408). Also has 20-alpha-HSD activity. Uses preferentially
CC       NADH (By similarity). {ECO:0000250|UniProtKB:P14061,
CC       ECO:0000269|PubMed:9658408}.
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:P14061};
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=NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC         NADPH; Xref=Rhea:RHEA:14981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422,
CC         ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.51;
CC         Evidence={ECO:0000269|PubMed:9658408};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14983;
CC         Evidence={ECO:0000305|PubMed:9658408};
CC   -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC       {ECO:0000269|PubMed:9658408}.
CC   -!- SUBUNIT: Homodimer. Exists predominantly as an homodimer but also exits
CC       as monomer. {ECO:0000250|UniProtKB:P14061}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; X89627; CAA61770.1; -; mRNA.
DR   CCDS; CCDS25445.1; -.
DR   PIR; S62652; S62652.
DR   RefSeq; NP_034605.1; NM_010475.1.
DR   AlphaFoldDB; P51656; -.
DR   SMR; P51656; -.
DR   STRING; 10090.ENSMUSP00000019445; -.
DR   BindingDB; P51656; -.
DR   ChEMBL; CHEMBL1914269; -.
DR   SwissLipids; SLP:000001305; -.
DR   PaxDb; P51656; -.
DR   PRIDE; P51656; -.
DR   ProteomicsDB; 277328; -.
DR   Antibodypedia; 16966; 307 antibodies from 33 providers.
DR   DNASU; 15485; -.
DR   Ensembl; ENSMUST00000019445; ENSMUSP00000019445; ENSMUSG00000019301.
DR   GeneID; 15485; -.
DR   KEGG; mmu:15485; -.
DR   UCSC; uc007lnb.1; mouse.
DR   CTD; 3292; -.
DR   MGI; MGI:105077; Hsd17b1.
DR   VEuPathDB; HostDB:ENSMUSG00000019301; -.
DR   eggNOG; KOG1205; Eukaryota.
DR   GeneTree; ENSGT00940000160415; -.
DR   HOGENOM; CLU_010194_2_9_1; -.
DR   InParanoid; P51656; -.
DR   OMA; QMDVTDR; -.
DR   OrthoDB; 1313182at2759; -.
DR   PhylomeDB; P51656; -.
DR   TreeFam; TF105451; -.
DR   Reactome; R-MMU-193144; Estrogen biosynthesis.
DR   UniPathway; UPA00769; -.
DR   BioGRID-ORCS; 15485; 4 hits in 76 CRISPR screens.
DR   ChiTaRS; Hsd17b1; mouse.
DR   PRO; PR:P51656; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P51656; protein.
DR   Bgee; ENSMUSG00000019301; Expressed in cumulus cell and 40 other tissues.
DR   ExpressionAtlas; P51656; baseline and differential.
DR   Genevisible; P51656; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR   GO; GO:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR   GO; GO:0035410; F:dihydrotestosterone 17-beta-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:1903924; F:estradiol binding; ISO:MGI.
DR   GO; GO:0050661; F:NADP binding; ISO:MGI.
DR   GO; GO:0070401; F:NADP+ binding; ISO:MGI.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0005496; F:steroid binding; ISO:MGI.
DR   GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; ISO:MGI.
DR   GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IDA:UniProtKB.
DR   GO; GO:0060348; P:bone development; IEA:Ensembl.
DR   GO; GO:0071248; P:cellular response to metal ion; IEA:Ensembl.
DR   GO; GO:0006703; P:estrogen biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0061370; P:testosterone biosynthetic process; IDA:UniProtKB.
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; NADP; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Steroid biosynthesis.
FT   CHAIN           1..344
FT                   /note="17-beta-hydroxysteroid dehydrogenase type 1"
FT                   /id="PRO_0000054568"
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|UniProtKB:P14061"
FT   BINDING         10..38
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P14061"
FT   BINDING         66
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P14061"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P14061"
FT   BINDING         160
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P14061"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14061"
SQ   SEQUENCE   344 AA;  36785 MW;  0335C473F453C14A CRC64;
     MDPTVVLITG CSSGIGMHLA VRLASDRSQS FKVYATLRDL KAQGPLLEAA RTQGCPPGSL
     EILELDVRDS KSVAAAQACV TEGRVDVLVC NAGRGLFGPL EAHELNAVGA VLDVNVLGTI
     RMLQAFLPDM KRRHSGRVLV TASVGGLMGL PFHEVYCASK FALEGLCESL AILLPLFGVH
     VSLIECGAVH TAFYEKLVGG PGGALERADA QTRHLFAHYL RGYEQALSEA QDPEEVTELF
     LTAMRAPQPA LRYFSTNRFL PLARMRTEDP SGSSYVAAMH QEAFSNLQTQ ENAKAGAQVP
     GVSDTASSAL ICLPECAIPR VASELGWSAS DKPGQDNSCY QQKI
 
 
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