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Reviewed, UniProtKB/Swiss-Prot Q9WUP4 (S5A3_MOUSE)

Last modified November 4, 2008. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 proteinBy similarity. Endoplasmic reticulum membrane; Multi-pass membrane proteinPotential.

Sequence similarities

Belongs to the steroid 5-alpha reductase family.

Ontologies

Keywords

   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   DomainTransmembrane
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microsome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-oxo-5-alpha-steroid 4-dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3303303-oxo-5-alpha-steroid 4-dehydrogenase 3
PRO_0000317704

Regions

Transmembrane17 – 3721 Potential
Transmembrane81 – 10121 Potential
Transmembrane133 – 15321 Potential
Transmembrane170 – 19021 Potential
Transmembrane207 – 22721 Potential
Transmembrane278 – 29821 Potential

Experimental info

Sequence conflict1091G → S in BAE36955, BAE23944, BAC35871 and BAC30537. Ref.2
Sequence conflict2981F → S in BAE36955, BAE23944, BAC35871 and BAC30537. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9WUP4-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 16C3A1CEAB415F41

FASTA33037,966
        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 

« Hide

References

« Hide '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. 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: 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

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.
RefSeqNP_065636.2.
XP_001471752.1.
UniGeneMm.289446

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000029233. Mus musculus. [Contig view]
GeneID100044230.
57357.
KEGGmmu:100044230.
mmu:57357.

Organism-specific databases

MGIMGI:1930252. Srd5a3.

Phylogenomic databases

HOVERGENQ9WUP4.

Gene expression databases

ArrayExpressQ9WUP4.
CleanExMM_SRD5A3.

Family and domain databases

InterProIPR001104. 3-oxo-5_a-steroid_4-DHase_C.
[Graphical view]
PfamPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio457733.
SOURCESearch...

Entry information

Entry nameS5A3_MOUSE
AccessionPrimary (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: November 4, 2008
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents