Reviewed, UniProtKB/Swiss-Prot Q99N99 (S5A2_MOUSE)

Names and origin

Protein names

Recommended name:
    3-oxo-5-alpha-steroid 4-dehydrogenase 2
    EC=1.3.99.5
Alternative name(s):
    Steroid 5-alpha-reductase 2
    5 alpha-SR2
    SR type 2

Gene names

Name:	Srd5a2
Synonyms:	5art2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 + acceptor = a 3-oxo-Delta(4)-steroid + reduced acceptor.
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 process	Differentiation Sexual differentiation
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	androgen biosynthetic process Inferred from mutant phenotype. Source: MGI cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW male genitalia development Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sex determination Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-oxo-5-alpha-steroid 4-dehydrogenase activity Inferred from mutant phenotype. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 254	254	3-oxo-5-alpha-steroid 4-dehydrogenase 2		PRO_0000213678
Regions
	Transmembrane	8 – 28	21	Potential
	Transmembrane	72 – 92	21	Potential
	Transmembrane	146 – 166	21	Potential
	Transmembrane	206 – 226	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q99N99-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 8D25019E8DC4DF47	FASTA	254	28,619
	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

References

	« Hide 'large scale' referencesShow '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: 11884637] [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. , 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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB049456 mRNA. Translation: BAB40179.1. AK138946 mRNA. Translation: BAE23830.1. BC125510 mRNA. Translation: AAI25511.1.
IPI	IPI00118239.
RefSeq	NP_444418.1.
UniGene	Mm.38933
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000038541. Mus musculus. [Contig view]
GeneID	94224.
KEGG	mmu:94224.
Organism-specific databases
MGI	MGI:2150380. Srd5a2.
Phylogenomic databases
HOGENOM	Q99N99.
HOVERGEN	Q99N99.
OMA	Q99N99. EITYRIP.
Enzyme and pathway databases
BRENDA	1.3.99.5. 244.
Gene expression databases
ArrayExpress	Q99N99.
Bgee	Q99N99.
CleanEx	MM_SRD5A2.
GermOnline	ENSMUSG00000038541. Mus musculus.
Family and domain databases
InterPro	IPR016636. 3-oxo-5-alpha-steroid_4-DH. IPR001104. 3-oxo-5_a-steroid_4-DH_C. [Graphical view]
Pfam	PF02544. Steroid_dh. 1 hit. [Graphical view]
PIRSF	PIRSF015596. 5_alpha-SR2. 1 hit.
PROSITE	PS50244. S5A_REDUCTASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	352223.
SOURCE	Search...

Entry information

Entry name

S5A2_MOUSE

Accession

Primary (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:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)