Reviewed, UniProtKB/Swiss-Prot Q9WUP4 (S5A3_MOUSE)

Names and origin

Protein names

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

Gene names

Name:	Srd5a3
Synonyms:	Srd5a2l

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	330 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) 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
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	lipid metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction 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 electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 330	330	3-oxo-5-alpha-steroid 4-dehydrogenase 3		PRO_0000317704
Regions
	Transmembrane	17 – 37	21	Potential
	Transmembrane	81 – 101	21	Potential
	Transmembrane	133 – 153	21	Potential
	Transmembrane	170 – 190	21	Potential
	Transmembrane	207 – 227	21	Potential
	Transmembrane	278 – 298	21	Potential
Experimental info
	Sequence conflict	109	1	G → S in BAE36955. Ref.2
	Sequence conflict	109	1	G → S in BAE23944. Ref.2
	Sequence conflict	109	1	G → S in BAC35871. Ref.2
	Sequence conflict	109	1	G → S in BAC30537. Ref.2
	Sequence conflict	298	1	F → S in BAE36955. Ref.2
	Sequence conflict	298	1	F → S in BAE23944. Ref.2
	Sequence conflict	298	1	F → S in BAC35871. Ref.2
	Sequence conflict	298	1	F → S in BAC30537. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9WUP4-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 16C3A1CEAB415F41	FASTA	330	37,966
	10 20 30 40 50 60 MAGWAGFELS ALNPLRTLWL ALAAAFLFAL LLQLAPARLL PSCALFQDLL RYGKTKQSGS 70 80 90 100 110 120 RRPAVCRAFD VPKRYFSHFY VISVVWNGSL LWLLSQSLFL GAPFPNWLGA LLRTLGATQF 130 140 150 160 170 180 QALEMESKAS RMPAAELALS AFLVLVFLWV HSLRRLFECF YVSVFSNAAI HVVQYCFGLV 190 200 210 220 230 240 YYVLVGLTVL SQVPMDDKNV YVLGKNLLIQ ARWFHILGMV MFFWSSAHQY KCHVILSNLR 250 260 270 280 290 300 RNKKGVVIHC QHRIPFGDWF EYVSSANYLA ELMIYISMAV TFGLHNLTWW LVVTYVFFSQ 310 320 330 ALSAFFNHKF YRSTFVSYPK HRKAFLPFLF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mouse Clock locus: sequence and comparative analysis of 204 kb from mouse chromosome 5." Wilsbacher L.D., Sangoram A.M., Antoch M.P., Takahashi J.S. Genome Res. 10:1928-1940(2000) [PubMed: 11116088] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv.
[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: Cerebellum, Thymus and Urinary bladder.
[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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF146793 Genomic DNA. Translation: AAD30567.1. AK040198 mRNA. Translation: BAC30537.1. AK075635 mRNA. Translation: BAC35871.1. AK139290 mRNA. Translation: BAE23944.1. AK162527 mRNA. Translation: BAE36955.1. BC145647 mRNA. Translation: AAI45648.1.
IPI	IPI00885969.
RefSeq	NP_065636.2. XP_001471752.1.
UniGene	Mm.289446
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000029233. Mus musculus. [Contig view]
GeneID	100044230. 57357.
KEGG	mmu:100044230. mmu:57357.
Organism-specific databases
MGI	MGI:1930252. Srd5a3.
Phylogenomic databases
HOVERGEN	Q9WUP4.
Enzyme and pathway databases
BRENDA	1.3.99.5. 244.
Gene expression databases
ArrayExpress	Q9WUP4.
Bgee	Q9WUP4.
CleanEx	MM_SRD5A3.
Family and domain databases
InterPro	IPR001104. 3-oxo-5_a-steroid_4-DH_C. [Graphical view]
Pfam	PF02544. Steroid_dh. 1 hit. [Graphical view]
PROSITE	PS50244. S5A_REDUCTASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	457733.
SOURCE	Search...

Entry information

Entry name

S5A3_MOUSE

Accession

Primary (citable) accession number: Q9WUP4
Secondary accession number(s): Q8BGE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)