ID S5A3_MOUSE Reviewed; 330 AA. AC Q9WUP4; Q8BGE3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 16-JUN-2009, entry version 41. DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3; DE EC=1.3.99.5; DE AltName: Full=Steroid 5-alpha-reductase 3; DE AltName: Full=SR type 3; DE AltName: Full=Steroid 5-alpha-reductase 2-like; GN Name=Srd5a3; Synonyms=Srd5a2l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; RX MEDLINE=20568483; PubMed=11116088; DOI=10.1101/gr.10.12.1928; RA Wilsbacher L.D., Sangoram A.M., Antoch M.P., Takahashi J.S.; RT "The mouse Clock locus: sequence and comparative analysis of 204 kb RT from mouse chromosome 5."; RL Genome Res. 10:1928-1940(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Thymus, and Urinary bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Converts testosterone (T) into 5-alpha- CC dihydrotestosterone (DHT) (By similarity). CC -!- CATALYTIC ACTIVITY: A 3-oxo-5-alpha-steroid + acceptor = a 3-oxo- CC Delta(4)-steroid + reduced acceptor. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane CC protein (By similarity). Endoplasmic reticulum membrane; Multi- CC pass membrane protein (Potential). CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF146793; AAD30567.1; -; Genomic_DNA. DR EMBL; AK040198; BAC30537.1; -; mRNA. DR EMBL; AK075635; BAC35871.1; -; mRNA. DR EMBL; AK139290; BAE23944.1; -; mRNA. DR EMBL; AK162527; BAE36955.1; -; mRNA. DR EMBL; BC145647; AAI45648.1; -; mRNA. DR IPI; IPI00885969; -. DR RefSeq; NP_065636.2; -. DR RefSeq; XP_001471752.1; -. DR UniGene; Mm.289446; -. DR Ensembl; ENSMUSG00000029233; Mus musculus. DR GeneID; 100044230; -. DR GeneID; 57357; -. DR KEGG; mmu:100044230; -. DR KEGG; mmu:57357; -. DR MGI; MGI:1930252; Srd5a3. DR HOVERGEN; Q9WUP4; -. DR BRENDA; 1.3.99.5; 244. DR NextBio; 457733; -. DR ArrayExpress; Q9WUP4; -. DR Bgee; Q9WUP4; -. DR CleanEx; MM_SRD5A3; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell. DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IEA:EC. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR Pfam; PF02544; Steroid_dh; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. PE 2: Evidence at transcript level; KW Endoplasmic reticulum; Membrane; Microsome; Oxidoreductase; KW Transmembrane. FT CHAIN 1 330 3-oxo-5-alpha-steroid 4-dehydrogenase 3. FT /FTId=PRO_0000317704. FT TRANSMEM 17 37 Potential. FT TRANSMEM 81 101 Potential. FT TRANSMEM 133 153 Potential. FT TRANSMEM 170 190 Potential. FT TRANSMEM 207 227 Potential. FT TRANSMEM 278 298 Potential. FT CONFLICT 109 109 G -> S (in Ref. 2; BAE36955/BAE23944/ FT BAC35871/BAC30537). FT CONFLICT 298 298 F -> S (in Ref. 2; BAE36955/BAE23944/ FT BAC35871/BAC30537). SQ SEQUENCE 330 AA; 37966 MW; 16C3A1CEAB415F41 CRC64; MAGWAGFELS ALNPLRTLWL ALAAAFLFAL LLQLAPARLL PSCALFQDLL RYGKTKQSGS RRPAVCRAFD VPKRYFSHFY VISVVWNGSL LWLLSQSLFL GAPFPNWLGA LLRTLGATQF QALEMESKAS RMPAAELALS AFLVLVFLWV HSLRRLFECF YVSVFSNAAI HVVQYCFGLV YYVLVGLTVL SQVPMDDKNV YVLGKNLLIQ ARWFHILGMV MFFWSSAHQY KCHVILSNLR RNKKGVVIHC QHRIPFGDWF EYVSSANYLA ELMIYISMAV TFGLHNLTWW LVVTYVFFSQ ALSAFFNHKF YRSTFVSYPK HRKAFLPFLF //