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3BHS_PIG
ID   3BHS_PIG                Reviewed;         373 AA.
AC   Q9N119;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 127.
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 {ECO:0000250|UniProtKB:P14893};
GN   Synonyms=3b-HSD {ECO:0000312|EMBL:AAF37295.2};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1] {ECO:0000312|EMBL:AAF37295.2}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adipose tissue {ECO:0000312|EMBL:AAF37295.2};
RX   PubMed=11683717; DOI=10.1046/j.1365-2052.2001.00775.x;
RA   von Teichman A., Joerg H., Werner P., Brenig B., Stranzinger G.;
RT   "cDNA cloning and physical mapping of porcine 3 beta-hydroxysteroid
RT   dehydrogenase/Delta 5-delta 4 isomerase.";
RL   Anim. Genet. 32:298-302(2001).
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; AF232699; AAF37295.2; -; mRNA.
DR   RefSeq; NP_001004049.1; NM_001004049.2.
DR   AlphaFoldDB; Q9N119; -.
DR   SMR; Q9N119; -.
DR   STRING; 9823.ENSSSCP00000007165; -.
DR   PeptideAtlas; Q9N119; -.
DR   PRIDE; Q9N119; -.
DR   Ensembl; ENSSSCT00000007360; ENSSSCP00000007165; ENSSSCG00000006719.
DR   Ensembl; ENSSSCT00025040671; ENSSSCP00025017317; ENSSSCG00025029902.
DR   Ensembl; ENSSSCT00030043165; ENSSSCP00030019583; ENSSSCG00030031100.
DR   Ensembl; ENSSSCT00035094806; ENSSSCP00035039835; ENSSSCG00035070172.
DR   Ensembl; ENSSSCT00045003183; ENSSSCP00045001999; ENSSSCG00045002042.
DR   Ensembl; ENSSSCT00055002747; ENSSSCP00055002074; ENSSSCG00055001503.
DR   Ensembl; ENSSSCT00060048493; ENSSSCP00060020760; ENSSSCG00060035784.
DR   Ensembl; ENSSSCT00070006206; ENSSSCP00070005059; ENSSSCG00070003287.
DR   GeneID; 445539; -.
DR   KEGG; ssc:445539; -.
DR   CTD; 3283; -.
DR   eggNOG; KOG1430; Eukaryota.
DR   GeneTree; ENSGT00940000155444; -.
DR   HOGENOM; CLU_007383_6_3_1; -.
DR   InParanoid; Q9N119; -.
DR   OMA; SLEDCRG; -.
DR   OrthoDB; 930591at2759; -.
DR   TreeFam; TF343138; -.
DR   BRENDA; 1.1.1.145; 6170.
DR   Reactome; R-SSC-193048; Androgen biosynthesis.
DR   Reactome; R-SSC-193993; Mineralocorticoid biosynthesis.
DR   Reactome; R-SSC-194002; Glucocorticoid biosynthesis.
DR   SABIO-RK; Q9N119; -.
DR   UniPathway; UPA00062; -.
DR   Proteomes; UP000008227; Chromosome 4.
DR   Proteomes; UP000314985; Chromosome 4.
DR   Bgee; ENSSSCG00000006719; Expressed in ovary and 21 other tissues.
DR   ExpressionAtlas; Q9N119; baseline and differential.
DR   Genevisible; Q9N119; SS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion;
KW   Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome;
KW   Steroidogenesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..373
FT                   /note="3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-
FT                   isomerase"
FT                   /id="PRO_0000087786"
FT   TRANSMEM        292..309
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;  41882 MW;  8BD4FEEF0117F6FF CRC64;
     MAGWSCLVTG GGGFLGQRIV HLLLEEKDLQ EIRVLDKVFK PEVREEFSKL QSKIKLTMLE
     GDILDEQCLK GACQGASVVI HTASIIDVVN AVGRETVMKV NVKGTQLLLE ACVQASVPVF
     IHTSSIEVAG PNSYREVIQN ACEEDRLETA WSAPYPLSKK LAEKAVLEAN GWALQNGGTL
     HTCALRPMYI YGEGSPFIFA HMNKALENNG VLTHNSKFSR VNPVYVGNVA WAHILALRAL
     RDPRKALSVQ GQFYYVADDT PPQSYDDLNY TLGKEWGFCL DSRRSLPPSL RYWLAFLLEI
     VSFLLSPIYN YQPPFNRHFV TLCNSVFTVS YKKAQRDLGY EPLFTWEEAK QKTKAWVGSL
     VKQHKEALKT KTH
 
 
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