Q99N99 (S5A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Srd5a2
Synonyms:	5art2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
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 + 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 process	Differentiation Sexual differentiation
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane Transmembrane helix
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen biosynthetic process Inferred from mutant phenotype PubMed 15249131. Source: MGI biphenyl metabolic process Inferred from electronic annotation. Source: Compara bone development Inferred from electronic annotation. Source: Compara cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW dibenzo-p-dioxin metabolic process Inferred from electronic annotation. Source: Compara female genitalia development Inferred from electronic annotation. Source: Compara hippocampus development Inferred from electronic annotation. Source: Compara hypothalamus development Inferred from electronic annotation. Source: Compara male genitalia development Inferred from mutant phenotype PubMed 11606430. Source: MGI male gonad development Inferred from electronic annotation. Source: Compara phthalate metabolic process Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to follicle-stimulating hormone stimulus Inferred from electronic annotation. Source: Compara response to nutrient levels Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara response to testosterone stimulus Inferred from electronic annotation. Source: Compara steroid catabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cell body fiber Inferred from electronic annotation. Source: Compara endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW neuronal cell body Inferred from electronic annotation. Source: Compara
Molecular_function	3-oxo-5-alpha-steroid 4-dehydrogenase activity Inferred from mutant phenotype PubMed 11606430PubMed 15249131. Source: MGI amide binding Inferred from electronic annotation. Source: Compara cholestenone 5-alpha-reductase activity Inferred from electronic annotation. Source: EC
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	Helical; Potential
	Transmembrane	72 – 92	21	Helical; Potential
	Transmembrane	146 – 166	21	Helical; Potential
	Transmembrane	206 – 226	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q99N99 [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] [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. , 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.
IPI	IPI00118239.
RefSeq	NP_444418.1. NM_053188.2.
UniGene	Mm.38933.
3D structure databases
ProteinModelPortal	Q99N99.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000048862.
PTM databases
PhosphoSite	Q99N99.
Proteomic databases
PRIDE	Q99N99.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000043458; ENSMUSP00000048862; ENSMUSG00000038541.
GeneID	94224.
KEGG	mmu:94224.
UCSC	uc008dnt.1. mouse.
Organism-specific databases
CTD	6716.
MGI	MGI:2150380. Srd5a2.
Phylogenomic databases
eggNOG	NOG282706.
GeneTree	ENSGT00510000046634.
HOGENOM	HOG000050133.
HOVERGEN	HBG003402.
InParanoid	Q99N99.
KO	K12344.
OMA	FAFFTLC.
OrthoDB	EOG469QVK.
Gene expression databases
ArrayExpress	Q99N99.
Bgee	Q99N99.
CleanEx	MM_SRD5A2.
Genevestigator	Q99N99.
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
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:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program