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Q99N99

- S5A2_MOUSE

UniProt

Q99N99 - S5A2_MOUSE

Protein

3-oxo-5-alpha-steroid 4-dehydrogenase 2

Gene

Srd5a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Converts testosterone (T) into 5-alpha-dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology By similarity.By similarity

    Catalytic activityi

    A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + NADPH.

    GO - Molecular functioni

    1. 3-oxo-5-alpha-steroid 4-dehydrogenase activity Source: MGI
    2. amide binding Source: Ensembl
    3. cholestenone 5-alpha-reductase activity Source: UniProtKB-EC

    GO - Biological processi

    1. androgen biosynthetic process Source: MGI
    2. biphenyl metabolic process Source: Ensembl
    3. bone development Source: Ensembl
    4. cell differentiation Source: UniProtKB-KW
    5. dibenzo-p-dioxin metabolic process Source: Ensembl
    6. female genitalia development Source: Ensembl
    7. hippocampus development Source: Ensembl
    8. hypothalamus development Source: Ensembl
    9. male genitalia development Source: MGI
    10. male gonad development Source: Ensembl
    11. phthalate metabolic process Source: Ensembl
    12. response to drug Source: Ensembl
    13. response to follicle-stimulating hormone Source: Ensembl
    14. response to nutrient levels Source: Ensembl
    15. response to peptide hormone Source: Ensembl
    16. response to testosterone Source: Ensembl
    17. steroid biosynthetic process Source: MGI
    18. steroid catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Differentiation, Sexual differentiation

    Keywords - Ligandi

    NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-oxo-5-alpha-steroid 4-dehydrogenase 2 (EC:1.3.1.22)
    Alternative name(s):
    5 alpha-SR2
    SR type 2
    Steroid 5-alpha-reductase 2
    Short name:
    S5AR 2
    Gene namesi
    Name:Srd5a2
    Synonyms:5art2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:2150380. Srd5a2.

    Subcellular locationi

    GO - Cellular componenti

    1. cell body fiber Source: Ensembl
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. neuronal cell body Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2542543-oxo-5-alpha-steroid 4-dehydrogenase 2PRO_0000213678Add
    BLAST

    Proteomic databases

    PRIDEiQ99N99.

    PTM databases

    PhosphoSiteiQ99N99.

    Expressioni

    Gene expression databases

    BgeeiQ99N99.
    CleanExiMM_SRD5A2.
    GenevestigatoriQ99N99.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000048862.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99N99.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei72 – 9221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei146 – 16621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei206 – 22621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the steroid 5-alpha reductase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG282706.
    GeneTreeiENSGT00510000046634.
    HOGENOMiHOG000050133.
    HOVERGENiHBG003402.
    InParanoidiQ99N99.
    KOiK12344.
    OMAiHHRYYLK.
    OrthoDBiEOG75QR56.
    PhylomeDBiQ99N99.
    TreeFamiTF314668.

    Family and domain databases

    InterProiIPR016636. 3-oxo-5-alpha-steroid_4-DH.
    IPR001104. 3-oxo-5_a-steroid_4-DH_C.
    [Graphical view]
    PfamiPF02544. Steroid_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015596. 5_alpha-SR2. 1 hit.
    PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99N99-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPIVCHQVPV LAGSATLATM GTLILCFGKP ASYGKHSESV SSGVPLLPAR    50
    IAWFLQELPS FVVSVGMLAW QPRSLFGPPG NVLLGLFSAH YFHRTFIYSL 100
    LTRGRPLSAV IFLKATAFCI GNGLLQAYYL VYCAEYPEEW YTDMRFSVGV 150
    FFFILGMGIN IHSDCMLRQL RKPGEVIYRI PQGGLFTYVS GANFLGEIIE 200
    WMGYALATWS VPAFAFAFFT LCFLGMQAFY HHRFYLKMFK DYPKSRKALI 250
    PFIF 254
    Length:254
    Mass (Da):28,619
    Last modified:June 1, 2001 - v1
    Checksum:i8D25019E8DC4DF47
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB049456 mRNA. Translation: BAB40179.1.
    AK138946 mRNA. Translation: BAE23830.1.
    BC125510 mRNA. Translation: AAI25511.1.
    CCDSiCCDS28968.1.
    RefSeqiNP_444418.1. NM_053188.2.
    UniGeneiMm.38933.

    Genome annotation databases

    EnsembliENSMUST00000043458; ENSMUSP00000048862; ENSMUSG00000038541.
    GeneIDi94224.
    KEGGimmu:94224.
    UCSCiuc008dnt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB049456 mRNA. Translation: BAB40179.1 .
    AK138946 mRNA. Translation: BAE23830.1 .
    BC125510 mRNA. Translation: AAI25511.1 .
    CCDSi CCDS28968.1.
    RefSeqi NP_444418.1. NM_053188.2.
    UniGenei Mm.38933.

    3D structure databases

    ProteinModelPortali Q99N99.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000048862.

    PTM databases

    PhosphoSitei Q99N99.

    Proteomic databases

    PRIDEi Q99N99.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000043458 ; ENSMUSP00000048862 ; ENSMUSG00000038541 .
    GeneIDi 94224.
    KEGGi mmu:94224.
    UCSCi uc008dnt.1. mouse.

    Organism-specific databases

    CTDi 6716.
    MGIi MGI:2150380. Srd5a2.

    Phylogenomic databases

    eggNOGi NOG282706.
    GeneTreei ENSGT00510000046634.
    HOGENOMi HOG000050133.
    HOVERGENi HBG003402.
    InParanoidi Q99N99.
    KOi K12344.
    OMAi HHRYYLK.
    OrthoDBi EOG75QR56.
    PhylomeDBi Q99N99.
    TreeFami TF314668.

    Miscellaneous databases

    NextBioi 352223.
    PROi Q99N99.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99N99.
    CleanExi MM_SRD5A2.
    Genevestigatori Q99N99.

    Family and domain databases

    InterProi IPR016636. 3-oxo-5-alpha-steroid_4-DH.
    IPR001104. 3-oxo-5_a-steroid_4-DH_C.
    [Graphical view ]
    Pfami PF02544. Steroid_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015596. 5_alpha-SR2. 1 hit.
    PROSITEi PS50244. S5A_REDUCTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Transcriptional regulation of the mouse steroid 5alpha-reductase type II gene by progesterone in brain."
      Takeyama K., Kato S.
      Nucleic Acids Res. 30:1387-1393(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Aorta and Vein.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.

    Entry informationi

    Entry nameiS5A2_MOUSE
    AccessioniPrimary (citable) accession number: Q99N99
    Secondary accession number(s): Q3UTZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3