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3BHS_BOVIN
ID   3BHS_BOVIN              Reviewed;         373 AA.
AC   P14893; Q2T9Y8;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase;
DE            Short=3-beta-HSD;
DE   Includes:
DE     RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase;
DE              EC=1.1.1.145;
DE     AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase;
DE     AltName: Full=Progesterone reductase;
DE   Includes:
DE     RecName: Full=Steroid Delta-isomerase;
DE              EC=5.3.3.1;
DE     AltName: Full=Delta-5-3-ketosteroid isomerase;
GN   Name=HSD3B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=2599102; DOI=10.1016/0014-5793(89)81516-9;
RA   Zhao H.-F., Simard J., Labrie C., Breton N., Rheaume E., Luu-The V.,
RA   Labrie F.;
RT   "Molecular cloning, cDNA structure and predicted amino acid sequence of
RT   bovine 3 beta-hydroxy-5-ene steroid dehydrogenase/delta 5-delta 4
RT   isomerase.";
RL   FEBS Lett. 259:153-157(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Adrenal gland;
RX   PubMed=1868086; DOI=10.1021/bi00247a003;
RA   Rutherfurd K.J., Chen S., Shively J.E.;
RT   "Isolation and amino acid sequence analysis of bovine adrenal 3 beta-
RT   hydroxysteroid dehydrogenase/steroid isomerase.";
RL   Biochemistry 30:8108-8116(1991).
CC   -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the
CC       oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the
CC       oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system
CC       plays a crucial role in the biosynthesis of all classes of hormonal
CC       steroids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)-
CC         steroid + H(+) + NADH; Xref=Rhea:RHEA:24076, ChEBI:CHEBI:1722,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:47907, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.145;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid;
CC         Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909;
CC         EC=5.3.3.1;
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein. Mitochondrion membrane; Single-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR   EMBL; X17614; CAA35615.1; -; mRNA.
DR   EMBL; BC111203; AAI11204.2; -; mRNA.
DR   PIR; S07102; DEBOHS.
DR   RefSeq; NP_776768.1; NM_174343.3.
DR   AlphaFoldDB; P14893; -.
DR   STRING; 9913.ENSBTAP00000010992; -.
DR   PaxDb; P14893; -.
DR   Ensembl; ENSBTAT00000087114; ENSBTAP00000061218; ENSBTAG00000006769.
DR   GeneID; 281824; -.
DR   KEGG; bta:281824; -.
DR   CTD; 3283; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006769; -.
DR   eggNOG; KOG1430; Eukaryota.
DR   GeneTree; ENSGT00940000155444; -.
DR   HOGENOM; CLU_007383_6_3_1; -.
DR   InParanoid; P14893; -.
DR   OMA; SLEDCRG; -.
DR   OrthoDB; 930591at2759; -.
DR   TreeFam; TF343138; -.
DR   Reactome; R-BTA-193048; Androgen biosynthesis.
DR   Reactome; R-BTA-193993; Mineralocorticoid biosynthesis.
DR   Reactome; R-BTA-194002; Glucocorticoid biosynthesis.
DR   UniPathway; UPA00062; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000006769; Expressed in diaphragm and 57 other tissues.
DR   ExpressionAtlas; P14893; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102294; F:cholesterol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008207; P:C21-steroid hormone metabolic process; IBA:GO_Central.
DR   GO; GO:0021766; P:hippocampus development; IBA:GO_Central.
DR   GO; GO:0051412; P:response to corticosterone; IBA:GO_Central.
DR   GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Isomerase; Membrane;
KW   Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase;
KW   Reference proteome; Steroidogenesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..373
FT                   /note="3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-
FT                   isomerase"
FT                   /id="PRO_0000087771"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  42220 MW;  B9BDB817E7B5A1D1 CRC64;
     MAGWSCLVTG GGGFLGQRII CLLVEEKDLQ EIRVLDKVFR PEVREEFSKL QSKIKLTLLE
     GDILDEQCLK GACQGTSVVI HTASVIDVRN AVPRETIMNV NVKGTQLLLE ACVQASVPVF
     IHTSTIEVAG PNSYREIIQD GREEEHHESA WSSPYPYSKK LAEKAVLGAN GWALKNGGTL
     YTCALRPMYI YGEGSPFLSA YMHGALNNNG ILTNHCKFSR VNPVYVGNVA WAHILALRAL
     RDPKKVPNIQ GQFYYISDDT PHQSYDDLNY TLSKEWGFCL DSRMSLPISL QYWLAFLLEI
     VSFLLSPIYK YNPCFNRHLV TLSNSVFTFS YKKAQRDLGY EPLYTWEEAK QKTKEWIGSL
     VKQHKETLKT KIH
 
 
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