S5A2_MOUSE
ID S5A2_MOUSE Reviewed; 254 AA.
AC Q99N99; Q3UTZ9;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 2;
DE EC=1.3.1.22 {ECO:0000250|UniProtKB:P31213};
DE AltName: Full=5 alpha-SR2;
DE AltName: Full=SR type 2;
DE AltName: Full=Steroid 5-alpha-reductase 2;
DE Short=S5AR 2;
GN Name=Srd5a2; Synonyms=5art2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=11884637; DOI=10.1093/nar/30.6.1387;
RA Takeyama K., Kato S.;
RT "Transcriptional regulation of the mouse steroid 5alpha-reductase type II
RT gene by progesterone in brain.";
RL Nucleic Acids Res. 30:1387-1393(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Converts testosterone (T) into 5-alpha-dihydrotestosterone
CC (DHT) and progesterone or corticosterone into their corresponding 5-
CC alpha-3-oxosteroids. It plays a central role in sexual differentiation
CC and androgen physiology. {ECO:0000250|UniProtKB:P31213}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid +
CC H(+) + NADPH; Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.22;
CC Evidence={ECO:0000250|UniProtKB:P31213};
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; AB049456; BAB40179.1; -; mRNA.
DR EMBL; AK138946; BAE23830.1; -; mRNA.
DR EMBL; BC125510; AAI25511.1; -; mRNA.
DR CCDS; CCDS28968.1; -.
DR RefSeq; NP_444418.1; NM_053188.2.
DR AlphaFoldDB; Q99N99; -.
DR SMR; Q99N99; -.
DR STRING; 10090.ENSMUSP00000048862; -.
DR PhosphoSitePlus; Q99N99; -.
DR PaxDb; Q99N99; -.
DR PRIDE; Q99N99; -.
DR ProteomicsDB; 256828; -.
DR Antibodypedia; 72759; 236 antibodies from 26 providers.
DR DNASU; 94224; -.
DR Ensembl; ENSMUST00000043458; ENSMUSP00000048862; ENSMUSG00000038541.
DR GeneID; 94224; -.
DR KEGG; mmu:94224; -.
DR UCSC; uc008dnt.1; mouse.
DR CTD; 6716; -.
DR MGI; MGI:2150380; Srd5a2.
DR VEuPathDB; HostDB:ENSMUSG00000038541; -.
DR eggNOG; KOG1638; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_065395_1_1_1; -.
DR InParanoid; Q99N99; -.
DR OMA; SYGKHTE; -.
DR OrthoDB; 1574389at2759; -.
DR PhylomeDB; Q99N99; -.
DR TreeFam; TF314668; -.
DR Reactome; R-MMU-193048; Androgen biosynthesis.
DR BioGRID-ORCS; 94224; 4 hits in 76 CRISPR screens.
DR PRO; PR:Q99N99; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99N99; protein.
DR Bgee; ENSMUSG00000038541; Expressed in adrenal gland and 44 other tissues.
DR Genevisible; Q99N99; MM.
DR GO; GO:0070852; C:cell body fiber; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IMP:MGI.
DR GO; GO:0033218; F:amide binding; ISO:MGI.
DR GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009917; F:sterol 5-alpha reductase activity; ISO:MGI.
DR GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; ISS:UniProtKB.
DR GO; GO:0006702; P:androgen biosynthetic process; IMP:MGI.
DR GO; GO:0008209; P:androgen metabolic process; ISO:MGI.
DR GO; GO:0018879; P:biphenyl metabolic process; IEA:Ensembl.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEA:Ensembl.
DR GO; GO:0030540; P:female genitalia development; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
DR GO; GO:0030539; P:male genitalia development; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; ISO:MGI.
DR GO; GO:0018963; P:phthalate metabolic process; IEA:Ensembl.
DR GO; GO:0032354; P:response to follicle-stimulating hormone; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006694; P:steroid biosynthetic process; IMP:MGI.
DR GO; GO:0006706; P:steroid catabolic process; ISO:MGI.
DR GO; GO:0061370; P:testosterone biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR016636; 3-oxo-5-alpha-steroid_4-DH.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039357; SRD5A/TECR.
DR PANTHER; PTHR10556; PTHR10556; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PIRSF; PIRSF015596; 5_alpha-SR2; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 2: Evidence at transcript level;
KW Differentiation; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Microsome; NADP; Oxidoreductase; Reference proteome;
KW Sexual differentiation; Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="3-oxo-5-alpha-steroid 4-dehydrogenase 2"
FT /id="PRO_0000213678"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 254 AA; 28619 MW; 8D25019E8DC4DF47 CRC64;
MPIVCHQVPV LAGSATLATM GTLILCFGKP ASYGKHSESV SSGVPLLPAR IAWFLQELPS
FVVSVGMLAW QPRSLFGPPG NVLLGLFSAH YFHRTFIYSL LTRGRPLSAV IFLKATAFCI
GNGLLQAYYL VYCAEYPEEW YTDMRFSVGV FFFILGMGIN IHSDCMLRQL RKPGEVIYRI
PQGGLFTYVS GANFLGEIIE WMGYALATWS VPAFAFAFFT LCFLGMQAFY HHRFYLKMFK
DYPKSRKALI PFIF
