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S5A2_PIG
ID   S5A2_PIG                Reviewed;         254 AA.
AC   O18765;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 2;
DE            EC=1.3.1.22 {ECO:0000250|UniProtKB:P31213};
DE   AltName: Full=5 alpha-SR2;
DE   AltName: Full=SR type 2;
DE   AltName: Full=Steroid 5-alpha-reductase 2;
DE            Short=S5AR 2;
GN   Name=SRD5A2; Synonyms=ST5AR2;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Epididymis;
RA   Lacroix D.A., Men T., Houde A., Murphy B.D.;
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts testosterone (T) into 5-alpha-dihydrotestosterone
CC       (DHT) and progesterone or corticosterone into their corresponding 5-
CC       alpha-3-oxosteroids. It plays a central role in sexual differentiation
CC       and androgen physiology (By similarity).
CC       {ECO:0000250|UniProtKB:P31213}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid +
CC         H(+) + NADPH; Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.3.1.22;
CC         Evidence={ECO:0000250|UniProtKB:P31213};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AF008440; AAB69279.2; -; mRNA.
DR   RefSeq; NP_999153.1; NM_213988.1.
DR   AlphaFoldDB; O18765; -.
DR   SMR; O18765; -.
DR   STRING; 9823.ENSSSCP00000009087; -.
DR   PaxDb; O18765; -.
DR   PeptideAtlas; O18765; -.
DR   Ensembl; ENSSSCT00030046625; ENSSSCP00030021001; ENSSSCG00030033689.
DR   Ensembl; ENSSSCT00040065105; ENSSSCP00040027543; ENSSSCG00040048320.
DR   Ensembl; ENSSSCT00045015342; ENSSSCP00045010660; ENSSSCG00045009063.
DR   Ensembl; ENSSSCT00055036688; ENSSSCP00055029157; ENSSSCG00055018745.
DR   Ensembl; ENSSSCT00060032689; ENSSSCP00060014019; ENSSSCG00060024102.
DR   GeneID; 397048; -.
DR   KEGG; ssc:397048; -.
DR   CTD; 6716; -.
DR   eggNOG; KOG1638; Eukaryota.
DR   HOGENOM; CLU_065395_3_0_1; -.
DR   InParanoid; O18765; -.
DR   OMA; SYGKHTE; -.
DR   OrthoDB; 1574389at2759; -.
DR   Reactome; R-SSC-193048; Androgen biosynthesis.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; O18765; SS.
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:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0009917; F:sterol 5-alpha reductase activity; IEA:Ensembl.
DR   GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; ISS:UniProtKB.
DR   GO; GO:0006702; P:androgen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0061370; P:testosterone biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR016636; 3-oxo-5-alpha-steroid_4-DH.
DR   InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR   InterPro; IPR039357; SRD5A/TECR.
DR   PANTHER; PTHR10556; PTHR10556; 1.
DR   Pfam; PF02544; Steroid_dh; 1.
DR   PIRSF; PIRSF015596; 5_alpha-SR2; 1.
DR   PROSITE; PS50244; S5A_REDUCTASE; 1.
PE   2: Evidence at transcript level;
KW   Differentiation; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW   Microsome; NADP; Oxidoreductase; Reference proteome;
KW   Sexual differentiation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..254
FT                   /note="3-oxo-5-alpha-steroid 4-dehydrogenase 2"
FT                   /id="PRO_0000213679"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   254 AA;  28536 MW;  F647B3D46AB98A29 CRC64;
     MPVRCQQSPV LAGSATLAAL GALALYFAEP SGYGKYTESL TPAAIRLPAR AAWFLQELPS
     FVVPAGILAG QPRSLFGPPA TVLLGLFCAH YFHRTFVYSL LTRGRPFPVV FLFRGFVFCM
     GNGLLQGYYL VYCAEYPAEW YTDIRFSLGV FLFILGMGIN IHSDYILRQL RKPGEVIYKI
     PQGGLFTYVS GANFLGEIIE WIGYALATWS LPALAFAFFS LCFLGLRAFH HHRFYVKMFE
     DYPKSRKALI PFIF
 
 
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