Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-oxo-5-alpha-steroid 4-dehydrogenase 2

Gene

Srd5a2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Kineticsi

  1. KM=74 nM for testosterone1 Publication
  2. KM=42 nM for progesterone1 Publication
  3. KM=170 nM for androstenedione1 Publication
  4. KM=376 nM for corticosterone1 Publication
  5. KM=11.2 µM for cortisol1 Publication

Vmax=0.5 nmol/min/mg enzyme1 Publication

pH dependencei

Optimally active at acidic pHs.1 Publication

GO - Molecular functioni

  1. 3-oxo-5-alpha-steroid 4-dehydrogenase activity Source: RGD
  2. amide binding Source: RGD
  3. cholestenone 5-alpha-reductase activity Source: UniProtKB-EC

GO - Biological processi

  1. androgen biosynthetic process Source: RGD
  2. androgen metabolic process Source: RGD
  3. biphenyl metabolic process Source: RGD
  4. bone development Source: RGD
  5. cell differentiation Source: UniProtKB-KW
  6. dibenzo-p-dioxin metabolic process Source: RGD
  7. female genitalia development Source: RGD
  8. hippocampus development Source: RGD
  9. hypothalamus development Source: RGD
  10. male genitalia development Source: RGD
  11. male gonad development Source: RGD
  12. phthalate metabolic process Source: RGD
  13. response to drug Source: RGD
  14. response to follicle-stimulating hormone Source: RGD
  15. response to nutrient levels Source: RGD
  16. response to organic cyclic compound Source: RGD
  17. response to organic substance Source: RGD
  18. response to peptide hormone Source: RGD
  19. response to steroid hormone Source: RGD
  20. response to testosterone Source: RGD
  21. sex differentiation Source: RGD
  22. steroid biosynthetic process Source: RGD
  23. steroid catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Differentiation, Sexual differentiation

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Srd5a2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 6

Organism-specific databases

RGDi621480. Srd5a2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei8 – 2821HelicalSequence AnalysisAdd
BLAST
Transmembranei72 – 9221HelicalSequence AnalysisAdd
BLAST
Transmembranei146 – 16621HelicalSequence AnalysisAdd
BLAST
Transmembranei206 – 22621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell body fiber Source: RGD
  2. cytoplasm Source: RGD
  3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
  5. neuronal cell body Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2542543-oxo-5-alpha-steroid 4-dehydrogenase 2PRO_0000213680Add
BLAST

Proteomic databases

PRIDEiP31214.

Expressioni

Tissue specificityi

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

Gene expression databases

ExpressionAtlasiP31214. baseline.
GenevestigatoriP31214.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009254.

Family & Domainsi

Sequence similaritiesi

Belongs to the steroid 5-alpha reductase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG282706.
GeneTreeiENSGT00510000046634.
HOGENOMiHOG000050133.
HOVERGENiHBG003402.
InParanoidiP31214.
KOiK12344.
OMAiHHRYYLK.
OrthoDBiEOG75QR56.
PhylomeDBiP31214.
TreeFamiTF314668.

Family and domain databases

InterProiIPR016636. 3-oxo-5-alpha-steroid_4-DH.
IPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015596. 5_alpha-SR2. 1 hit.
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31214-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQIVCHQVPV LAGSATLATM GTLILCLGKP ASYGKHTESV SSGVPFLPAR
60 70 80 90 100
IAWFLQELPS FVVSVGMLAW QPRSLFGPPG NVLLALFSAH YFHRTFIYSL
110 120 130 140 150
LTRGRPFPAV LFLRATAFCI GNGLLQAYYL VYCAEYPEEW YTDVRFSFGV
160 170 180 190 200
FLFILGMGIN IHSDYTLRQL RKPGEVIYRI PRGGLFTYVS GANFLGEIIE
210 220 230 240 250
WIGYALATWS VPAFAFAFFT LCFLGMQAFY HHRFYLKMFK DYPKSRKALI

PFIF
Length:254
Mass (Da):28,772
Last modified:July 1, 1993 - v1
Checksum:i8874C533DF3BD123
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95058 mRNA. Translation: AAA42182.1.
PIRiA44104.
RefSeqiNP_073202.1. NM_022711.4.
UniGeneiRn.9938.

Genome annotation databases

EnsembliENSRNOT00000008983; ENSRNOP00000009254; ENSRNOG00000027042.
GeneIDi64677.
KEGGirno:64677.
UCSCiRGD:621480. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95058 mRNA. Translation: AAA42182.1.
PIRiA44104.
RefSeqiNP_073202.1. NM_022711.4.
UniGeneiRn.9938.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009254.

Chemistry

BindingDBiP31214.
ChEMBLiCHEMBL5099.

Proteomic databases

PRIDEiP31214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008983; ENSRNOP00000009254; ENSRNOG00000027042.
GeneIDi64677.
KEGGirno:64677.
UCSCiRGD:621480. rat.

Organism-specific databases

CTDi6716.
RGDi621480. Srd5a2.

Phylogenomic databases

eggNOGiNOG282706.
GeneTreeiENSGT00510000046634.
HOGENOMiHOG000050133.
HOVERGENiHBG003402.
InParanoidiP31214.
KOiK12344.
OMAiHHRYYLK.
OrthoDBiEOG75QR56.
PhylomeDBiP31214.
TreeFamiTF314668.

Miscellaneous databases

NextBioi613680.
PROiP31214.

Gene expression databases

ExpressionAtlasiP31214. baseline.
GenevestigatoriP31214.

Family and domain databases

InterProiIPR016636. 3-oxo-5-alpha-steroid_4-DH.
IPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015596. 5_alpha-SR2. 1 hit.
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiS5A2_RAT
AccessioniPrimary (citable) accession number: P31214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: January 7, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.