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UniProtKB/Swiss-Prot entry Q9WUP4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name S5A3_MOUSE
Primary accession number Q9WUP4
Secondary accession number Q8BGE3
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 36)
Name and origin of the protein
Protein name 3-oxo-5-alpha-steroid 4-dehydrogenase 3
Synonyms EC 1.3.99.5
Steroid 5-alpha-reductase 3
SR type 3
Steroid 5-alpha-reductase 2-like
Gene name
Name: Srd5a3
Synonyms: Srd5a2l
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
DOI=10.1101/gr.10.12.1928; PubMed=11116088 [NCBI, ExPASy, EBI, Israel, Japan]
Wilsbacher L.D., Sangoram A.M., Antoch M.P., Takahashi J.S.;
"The mouse Clock locus: sequence and comparative analysis of 204 kb from mouse chromosome 5.";
Genome Res. 10:1928-1940(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Cerebellum, Thymus, and Urinary bladder;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF146793; AAD30567.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK040198; BAC30537.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075635; BAC35871.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK139290; BAE23944.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK162527; BAE36955.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC145647; AAI45648.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_065636.2; -.
XP_001471752.1; -.
UniGene Mm.289446
3D structure databases
ModBase Q9WUP4.
Organism-specific databases
MGI MGI:1930252; Srd5a3.
Gene expression databases
ArrayExpress Q9WUP4; -.
CleanEx MM_SRD5A3; -.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR001104; 3-oxo-5_a-steroid_4-DHase_C.
Graphical view of domain structure.
Pfam PF02544; Steroid_dh; 1.
Pfam graphical view of domain structure.
PROSITE PS50244; S5A_REDUCTASE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9WUP4.
Genome annotation databases
Ensembl ENSMUSG00000029233; Mus musculus. [Contig view]
GeneID 100044230; -.
57357; -.
KEGG mmu:100044230; -.
mmu:57357; -.
Phylogenomic databases
HOVERGEN Q9WUP4; -.
Other
SOURCE Srd5a3; Mus musculus.
ProtoNet Q9WUP4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; Membrane; Microsome; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   330  330     3-oxo-5-alpha-steroid 4-dehydrogenase 3. PRO_0000317704
TRANSMEM   17    37  21     Potential. 
TRANSMEM   81   101  21     Potential. 
TRANSMEM   133   153  21     Potential. 
TRANSMEM   170   190  21     Potential. 
TRANSMEM   207   227  21     Potential. 
TRANSMEM   278   298  21     Potential. 
CONFLICT   109   109        G -> S (in Ref. 2; BAE36955/BAE23944/BAC35871/BAC30537). 
CONFLICT   298   298        F -> S (in Ref. 2; BAE36955/BAE23944/BAC35871/BAC30537). 
Sequence information
Length: 330 AA [This is the length of the unprocessed precursor] Molecular weight: 37966 Da [This is the MW of the unprocessed precursor] CRC64: 16C3A1CEAB415F41 [This is a checksum on the sequence]
        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 

Q9WUP4 in FASTA format

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View entry in raw text format (no links)
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