NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=1527072 [NCBI, ExPASy, EBI, Israel, Japan]
Normington K., Russell D.W.;
"Tissue distribution and kinetic characteristics of rat steroid 5 alpha-reductase isozymes. Evidence for distinct physiological functions.";
J. Biol. Chem. 267:19548-19554(1992).

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 + acceptor = a 3-oxo-Delta⁴-steroid + reduced acceptor.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimally active at acidic pHs;
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.
SIMILARITY: Belongs to the steroid 5-alpha reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M95058; AAA42182.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A44104; A44104.

NP_073202.1; -.

3D structure databases

ModBase

P31214.

Organism-specific databases

RGD

621480; Srd5a2.

Gene expression databases

ArrayExpress

P31214; -.

GermOnline

ENSRNOG00000027042; Rattus norvegicus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0003865;	Molecular function: 3-oxo-5-alpha-steroid 4-dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0030154;	Biological process: cell differentiation (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0007530;	Biological process: sex determination (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR016636; 3-oxo-5-alpha-steroid_4-DH.
IPR001104; 3-oxo-5_a-steroid_4-DHase_C.
Graphical view of domain structure.

Pfam

PF02544; Steroid_dh; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF015596; 5_alpha-SR2; 1.

PROSITE

PS50244; S5A_REDUCTASE; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000027042; Rattus norvegicus. [Contig view]

GeneID

64677; -.

KEGG

rno:64677; -.

Phylogenomic databases

HOVERGEN

P31214; -.

Other

NextBio

613680; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Differentiation; Endoplasmic reticulum; Membrane; Microsome; Oxidoreductase; Sexual differentiation; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 254`	`254`	`3-oxo-5-alpha-steroid 4-dehydrogenase 2.`	`PRO_0000213680`
`TRANSMEM`	`8 28`	`21`	`Potential.`
`TRANSMEM`	`72 92`	`21`	`Potential.`
`TRANSMEM`	`146 166`	`21`	`Potential.`
`TRANSMEM`	`206 226`	`21`	`Potential.`

Sequence information

Length: 254 AA [This is the length of the unprocessed precursor]

Molecular weight: 28772 Da [This is the MW of the unprocessed precursor]

CRC64: 8874C533DF3BD123 [This is a checksum on the sequence]

        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

P31214 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools