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Q99N99 (S5A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Synonyms:5art2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Subcellular location

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

Sequence similarities

Belongs to the steroid 5-alpha reductase family.

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 mutant phenotype PubMed 15249131. Source: MGI

biphenyl metabolic process

Inferred from electronic annotation. Source: Ensembl

bone development

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

dibenzo-p-dioxin metabolic process

Inferred from electronic annotation. Source: Ensembl

female genitalia development

Inferred from electronic annotation. Source: Ensembl

hippocampus development

Inferred from electronic annotation. Source: Ensembl

hypothalamus development

Inferred from electronic annotation. Source: Ensembl

male genitalia development

Inferred from mutant phenotype PubMed 11606430. Source: MGI

male gonad development

Inferred from electronic annotation. Source: Ensembl

phthalate metabolic process

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to follicle-stimulating hormone

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

steroid biosynthetic process

Inferred from mutant phenotype PubMed 11606430. Source: MGI

steroid catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell body fiber

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

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

Inferred from mutant phenotype PubMed 11606430PubMed 15249131. Source: MGI

amide binding

Inferred from electronic annotation. Source: Ensembl

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_0000213678

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q99N99 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8D25019E8DC4DF47

FASTA25428,619
        10         20         30         40         50         60 
MPIVCHQVPV LAGSATLATM GTLILCFGKP ASYGKHSESV SSGVPLLPAR IAWFLQELPS 

        70         80         90        100        110        120 
FVVSVGMLAW QPRSLFGPPG NVLLGLFSAH YFHRTFIYSL LTRGRPLSAV IFLKATAFCI 

       130        140        150        160        170        180 
GNGLLQAYYL VYCAEYPEEW YTDMRFSVGV FFFILGMGIN IHSDCMLRQL RKPGEVIYRI 

       190        200        210        220        230        240 
PQGGLFTYVS GANFLGEIIE WMGYALATWS VPAFAFAFFT LCFLGMQAFY HHRFYLKMFK 

       250 
DYPKSRKALI PFIF 

« Hide

References

« Hide 'large scale' references
[1]"Transcriptional regulation of the mouse steroid 5alpha-reductase type II gene by progesterone in brain."
Takeyama K., Kato S.
Nucleic Acids Res. 30:1387-1393(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Aorta and Vein.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB049456 mRNA. Translation: BAB40179.1.
AK138946 mRNA. Translation: BAE23830.1.
BC125510 mRNA. Translation: AAI25511.1.
CCDSCCDS28968.1.
RefSeqNP_444418.1. NM_053188.2.
UniGeneMm.38933.

3D structure databases

ProteinModelPortalQ99N99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000048862.

PTM databases

PhosphoSiteQ99N99.

Proteomic databases

PRIDEQ99N99.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043458; ENSMUSP00000048862; ENSMUSG00000038541.
GeneID94224.
KEGGmmu:94224.
UCSCuc008dnt.1. mouse.

Organism-specific databases

CTD6716.
MGIMGI:2150380. Srd5a2.

Phylogenomic databases

eggNOGNOG282706.
GeneTreeENSGT00510000046634.
HOGENOMHOG000050133.
HOVERGENHBG003402.
InParanoidQ99N99.
KOK12344.
OMAHHRYYLK.
OrthoDBEOG75QR56.
PhylomeDBQ99N99.
TreeFamTF314668.

Gene expression databases

BgeeQ99N99.
CleanExMM_SRD5A2.
GenevestigatorQ99N99.

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

NextBio352223.
PROQ99N99.
SOURCESearch...

Entry information

Entry nameS5A2_MOUSE
AccessionPrimary (citable) accession number: Q99N99
Secondary accession number(s): Q3UTZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 94 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot