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P31214 (S5A2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-oxo-5-alpha-steroid 4-dehydrogenase 2

EC=1.3.1.22
Alternative name(s):
5 alpha-SR2
SR type 2
Steroid 5-alpha-reductase 2
Short name=S5AR 2
Gene names
Name:Srd5a2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts testosterone (T) into 5-alpha-dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology By similarity.

Catalytic activity

A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + NADPH. Ref.1

Subcellular location

Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Tissue specificity

Expressed in high levels in the prostate and many other androgen-sensitive tissues. Ref.1

Sequence similarities

Belongs to the steroid 5-alpha reductase family.

Biophysicochemical properties

Kinetic parameters:

KM=74 nM for testosterone Ref.1

KM=42 nM for progesterone

KM=170 nM for androstenedione

KM=376 nM for corticosterone

KM=11.2 µM for cortisol

Vmax=0.5 nmol/min/mg enzyme

pH dependence:

Optimally active at acidic pHs.

Ontologies

Keywords
   Biological processDifferentiation
Sexual differentiation
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   DomainTransmembrane
Transmembrane helix
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen biosynthetic process

Inferred from direct assay PubMed 12606426. Source: RGD

androgen metabolic process

Inferred from direct assay PubMed 20954080. Source: RGD

biphenyl metabolic process

Inferred from expression pattern PubMed 16938428. Source: RGD

bone development

Inferred from expression pattern PubMed 15012600. Source: RGD

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

dibenzo-p-dioxin metabolic process

Inferred from expression pattern PubMed 11222880. Source: RGD

female genitalia development

Inferred from expression pattern PubMed 9142501. Source: RGD

hippocampus development

Inferred from expression pattern PubMed 21047951. Source: RGD

hypothalamus development

Inferred from expression pattern PubMed 15804399. Source: RGD

male genitalia development

Inferred from expression pattern PubMed 9142501. Source: RGD

male gonad development

Inferred from expression pattern PubMed 12606426. Source: RGD

phthalate metabolic process

Inferred from expression pattern PubMed 20954080. Source: RGD

response to drug

Inferred from expression pattern PubMed 18978642. Source: RGD

response to follicle-stimulating hormone

Inferred from expression pattern PubMed 12630924. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 16425201. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 17940878. Source: RGD

response to organic substance

Inferred from direct assay PubMed 12443045. Source: RGD

response to peptide hormone

Inferred from direct assay PubMed 12630924. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 16076027. Source: RGD

response to testosterone

Inferred from expression pattern PubMed 16595696. Source: RGD

sex differentiation

Traceable author statement Ref.1. Source: RGD

steroid biosynthetic process

Inferred from direct assay Ref.1PubMed 7662592. Source: RGD

steroid catabolic process

Inferred from direct assay Ref.1. Source: RGD

   Cellular_componentcell body fiber

Inferred from direct assay PubMed 15305365. Source: RGD

cytoplasm

Inferred from direct assay PubMed 15305365. Source: RGD

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuronal cell body

Inferred from direct assay PubMed 15305365. Source: RGD

   Molecular_function3-oxo-5-alpha-steroid 4-dehydrogenase activity

Inferred from direct assay Ref.1PubMed 7662592. Source: RGD

amide binding

Inferred from physical interaction PubMed 9328210. Source: RGD

cholestenone 5-alpha-reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2542543-oxo-5-alpha-steroid 4-dehydrogenase 2
PRO_0000213680

Regions

Transmembrane8 – 2821Helical; Potential
Transmembrane72 – 9221Helical; Potential
Transmembrane146 – 16621Helical; Potential
Transmembrane206 – 22621Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
P31214 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 8874C533DF3BD123

FASTA25428,772
        10         20         30         40         50         60 
MQIVCHQVPV LAGSATLATM GTLILCLGKP ASYGKHTESV SSGVPFLPAR IAWFLQELPS 

        70         80         90        100        110        120 
FVVSVGMLAW QPRSLFGPPG NVLLALFSAH YFHRTFIYSL LTRGRPFPAV LFLRATAFCI 

       130        140        150        160        170        180 
GNGLLQAYYL VYCAEYPEEW YTDVRFSFGV FLFILGMGIN IHSDYTLRQL RKPGEVIYRI 

       190        200        210        220        230        240 
PRGGLFTYVS GANFLGEIIE WIGYALATWS VPAFAFAFFT LCFLGMQAFY HHRFYLKMFK 

       250 
DYPKSRKALI PFIF 

« Hide

References

[1]"Tissue distribution and kinetic characteristics of rat steroid 5 alpha-reductase isozymes. Evidence for distinct physiological functions."
Normington K., Russell D.W.
J. Biol. Chem. 267:19548-19554(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95058 mRNA. Translation: AAA42182.1.
PIRA44104.
RefSeqNP_073202.1. NM_022711.4.
UniGeneRn.9938.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000009254.

Chemistry

BindingDBP31214.
ChEMBLCHEMBL5099.

Proteomic databases

PRIDEP31214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000008983; ENSRNOP00000009254; ENSRNOG00000027042.
GeneID64677.
KEGGrno:64677.
UCSCRGD:621480. rat.

Organism-specific databases

CTD6716.
RGD621480. Srd5a2.

Phylogenomic databases

eggNOGNOG282706.
GeneTreeENSGT00510000046634.
HOGENOMHOG000050133.
HOVERGENHBG003402.
InParanoidP31214.
KOK12344.
OMAGYGKYSE.
OrthoDBEOG75QR56.
PhylomeDBP31214.
TreeFamTF314668.

Gene expression databases

GenevestigatorP31214.

Family and domain databases

InterProIPR016636. 3-oxo-5-alpha-steroid_4-DH.
IPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamPF02544. Steroid_dh. 1 hit.
[Graphical view]
PIRSFPIRSF015596. 5_alpha-SR2. 1 hit.
PROSITEPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio613680.
PROP31214.

Entry information

Entry nameS5A2_RAT
AccessionPrimary (citable) accession number: P31214
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families