S5A2_RAT
ID S5A2_RAT Reviewed; 254 AA.
AC P31214;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 2;
DE EC=1.3.1.22 {ECO:0000269|PubMed:1527072};
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;
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], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=1527072; DOI=10.1016/s0021-9258(18)41809-1;
RA Normington K., Russell D.W.;
RT "Tissue distribution and kinetic characteristics of rat steroid 5 alpha-
RT reductase isozymes. Evidence for distinct physiological functions.";
RL J. Biol. Chem. 267:19548-19554(1992).
CC -!- FUNCTION: Converts testosterone (T) into 5-alpha-dihydrotestosterone
CC (DHT) and progesterone or corticosterone into their corresponding 5-
CC alpha-3-oxosteroids (PubMed:1527072). It plays a central role in sexual
CC differentiation and androgen physiology (By similarity).
CC {ECO:0000250|UniProtKB:P31213, ECO:0000269|PubMed:1527072}.
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:0000269|PubMed:1527072};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=74 nM for testosterone {ECO:0000269|PubMed:1527072};
CC KM=42 nM for progesterone {ECO:0000269|PubMed:1527072};
CC KM=170 nM for androstenedione {ECO:0000269|PubMed:1527072};
CC KM=376 nM for corticosterone {ECO:0000269|PubMed:1527072};
CC KM=11.2 uM for cortisol {ECO:0000269|PubMed:1527072};
CC Vmax=0.5 nmol/min/mg enzyme {ECO:0000269|PubMed:1527072};
CC pH dependence:
CC Optimally active at acidic pHs. {ECO:0000269|PubMed:1527072};
CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in high levels in the prostate and many
CC other androgen-sensitive tissues. {ECO:0000269|PubMed:1527072}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; M95058; AAA42182.1; -; mRNA.
DR PIR; A44104; A44104.
DR RefSeq; NP_073202.1; NM_022711.4.
DR AlphaFoldDB; P31214; -.
DR SMR; P31214; -.
DR STRING; 10116.ENSRNOP00000009254; -.
DR BindingDB; P31214; -.
DR ChEMBL; CHEMBL5099; -.
DR DrugCentral; P31214; -.
DR PaxDb; P31214; -.
DR Ensembl; ENSRNOT00000008983; ENSRNOP00000009254; ENSRNOG00000027042.
DR GeneID; 64677; -.
DR KEGG; rno:64677; -.
DR UCSC; RGD:621480; rat.
DR CTD; 6716; -.
DR RGD; 621480; Srd5a2.
DR eggNOG; KOG1638; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_065395_1_1_1; -.
DR InParanoid; P31214; -.
DR OMA; SYGKHTE; -.
DR OrthoDB; 1574389at2759; -.
DR PhylomeDB; P31214; -.
DR TreeFam; TF314668; -.
DR BRENDA; 1.3.1.22; 5301.
DR Reactome; R-RNO-193048; Androgen biosynthesis.
DR SABIO-RK; P31214; -.
DR PRO; PR:P31214; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000027042; Expressed in duodenum and 4 other tissues.
DR Genevisible; P31214; RN.
DR GO; GO:0070852; C:cell body fiber; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IDA:RGD.
DR GO; GO:0033218; F:amide binding; IPI:RGD.
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; ISO:RGD.
DR GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; ISS:UniProtKB.
DR GO; GO:0006702; P:androgen biosynthetic process; IDA:RGD.
DR GO; GO:0008209; P:androgen metabolic process; IDA:RGD.
DR GO; GO:0018879; P:biphenyl metabolic process; IEP:RGD.
DR GO; GO:0060348; P:bone development; IEP:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEP:RGD.
DR GO; GO:0030540; P:female genitalia development; IEP:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0021854; P:hypothalamus development; IEP:RGD.
DR GO; GO:0030539; P:male genitalia development; IEP:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0018963; P:phthalate metabolic process; IEP:RGD.
DR GO; GO:0032354; P:response to follicle-stimulating hormone; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IDA:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007548; P:sex differentiation; TAS:RGD.
DR GO; GO:0006694; P:steroid biosynthetic process; IDA:RGD.
DR GO; GO:0006706; P:steroid catabolic process; IDA:RGD.
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 1: Evidence at protein 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_0000213680"
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; 28772 MW; 8874C533DF3BD123 CRC64;
MQIVCHQVPV LAGSATLATM GTLILCLGKP ASYGKHTESV SSGVPFLPAR IAWFLQELPS
FVVSVGMLAW QPRSLFGPPG NVLLALFSAH YFHRTFIYSL LTRGRPFPAV LFLRATAFCI
GNGLLQAYYL VYCAEYPEEW YTDVRFSFGV FLFILGMGIN IHSDYTLRQL RKPGEVIYRI
PRGGLFTYVS GANFLGEIIE WIGYALATWS VPAFAFAFFT LCFLGMQAFY HHRFYLKMFK
DYPKSRKALI PFIF
