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P63300

- SELW_MOUSE

UniProt

P63300 - SELW_MOUSE

Protein

Selenoprotein W

Gene

Sepw1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency.3 Publications

    GO - Molecular functioni

    1. antioxidant activity Source: UniProtKB-KW
    2. oxidoreductase activity Source: UniProtKB
    3. selenium binding Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. oxidation-reduction process Source: GOC

    Keywords - Molecular functioni

    Antioxidant

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Selenoprotein W
    Short name:
    SelW
    Gene namesi
    Name:Sepw1
    Synonyms:Selw
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1100878. Sepw1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101C → S: Disrupts redox reaction.
    Mutagenesisi13 – 131U → C: Increased sensitivity to hydrogen peroxide-induced toxicity. 1 Publication
    Mutagenesisi13 – 131U → S: Impairs protection against hydrogen peroxide-induced toxicity. 1 Publication
    Mutagenesisi37 – 371C → S: Impairs protection against hydrogen peroxide-induced toxicity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 8887Selenoprotein WPRO_0000097680Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki10 ↔ 13Cysteinyl-selenocysteine (Cys-Sec); redox-activeBy similarity
    Modified residuei37 – 371S-glutathionyl cysteineBy similarity

    Keywords - PTMi

    Glutathionylation

    Proteomic databases

    PaxDbiP63300.
    PRIDEiP63300.

    PTM databases

    PhosphoSiteiP63300.

    Expressioni

    Tissue specificityi

    In the embryo, expressed in the developing nervous system and in mesoderm-derived tissues such as heart and limbs. In the adult, predominantly expressed in brain, skeletal muscle and heart.2 Publications

    Developmental stagei

    Expression is first detected in the newly implanted embryo. Levels increase gradually during embryonic development with a steady increase during the second week and a dramatic increase by the end of gestation. Expression increases gradually in proliferating myotubes but is low in terminally differentiated myobutubes.1 Publication

    Inductioni

    Down-regulated by hydrogen peroxide. Increased levels are detected after treatment with L-buthionine sulfoxide (BSO) before exposure to hydrogen peroxide.1 Publication

    Gene expression databases

    BgeeiP63300.
    CleanExiMM_SEPW1.
    GenevestigatoriP63300.

    Interactioni

    Subunit structurei

    Interacts with DPYSL2, PRDX1, YWHAB, YWHAG, HSP70 and HSP90.2 Publications

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000038943.

    Structurei

    Secondary structure

    1
    88
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi15 – 2915
    Beta strandi34 – 385
    Beta strandi49 – 524
    Beta strandi55 – 595
    Turni60 – 634
    Helixi70 – 8718

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NPBNMR-A1-88[»]
    ProteinModelPortaliP63300.
    SMRiP63300. Positions 1-88.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63300.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SelWTH family. SELW subfamily.Curated

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiNOG84296.
    GeneTreeiENSGT00530000064138.
    HOGENOMiHOG000286957.
    HOVERGENiHBG059755.
    InParanoidiP63300.
    OMAiKKRGDGY.
    OrthoDBiEOG7QRQXF.
    PhylomeDBiP63300.
    TreeFamiTF326627.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR011893. Selenoprotein_Rdx-typ.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF10262. Rdx. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.
    TIGRFAMsiTIGR02174. CXXU_selWTH. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P63300-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALAVRVVYC GAUGYKPKYL QLKEKLEHEF PGCLDICGEG TPQVTGFFEV   50
    TVAGKLVHSK KRGDGYVDTE SKFRKLVTAI KAALAQCQ 88
    Length:88
    Mass (Da):9,687
    Last modified:February 26, 2008 - v3
    Checksum:i03E297B668D3D7E0
    GO

    Non-standard residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-standard residuei13 – 131Selenocysteine

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67890 mRNA. Translation: AAC53317.1.
    AF241527 mRNA. Translation: AAF64481.1.
    AF015284 mRNA. Translation: AAB69860.1.
    AK002870 mRNA. Translation: BAC55247.1.
    AK028124 mRNA. Translation: BAC55256.1.
    BC052719 mRNA. Translation: AAH52719.2.
    CCDSiCCDS39778.1.
    RefSeqiNP_033182.1. NM_009156.2.
    UniGeneiMm.42829.

    Genome annotation databases

    EnsembliENSMUST00000044355; ENSMUSP00000038943; ENSMUSG00000041571.
    GeneIDi20364.
    KEGGimmu:20364.
    UCSCiuc009fgp.1. mouse.

    Keywords - Coding sequence diversityi

    Selenocysteine

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67890 mRNA. Translation: AAC53317.1 .
    AF241527 mRNA. Translation: AAF64481.1 .
    AF015284 mRNA. Translation: AAB69860.1 .
    AK002870 mRNA. Translation: BAC55247.1 .
    AK028124 mRNA. Translation: BAC55256.1 .
    BC052719 mRNA. Translation: AAH52719.2 .
    CCDSi CCDS39778.1.
    RefSeqi NP_033182.1. NM_009156.2.
    UniGenei Mm.42829.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NPB NMR - A 1-88 [» ]
    ProteinModelPortali P63300.
    SMRi P63300. Positions 1-88.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000038943.

    PTM databases

    PhosphoSitei P63300.

    Proteomic databases

    PaxDbi P63300.
    PRIDEi P63300.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000044355 ; ENSMUSP00000038943 ; ENSMUSG00000041571 .
    GeneIDi 20364.
    KEGGi mmu:20364.
    UCSCi uc009fgp.1. mouse.

    Organism-specific databases

    CTDi 6415.
    MGIi MGI:1100878. Sepw1.

    Phylogenomic databases

    eggNOGi NOG84296.
    GeneTreei ENSGT00530000064138.
    HOGENOMi HOG000286957.
    HOVERGENi HBG059755.
    InParanoidi P63300.
    OMAi KKRGDGY.
    OrthoDBi EOG7QRQXF.
    PhylomeDBi P63300.
    TreeFami TF326627.

    Miscellaneous databases

    EvolutionaryTracei P63300.
    NextBioi 298265.
    PROi P63300.
    SOURCEi Search...

    Gene expression databases

    Bgeei P63300.
    CleanExi MM_SEPW1.
    Genevestigatori P63300.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR011893. Selenoprotein_Rdx-typ.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF10262. Rdx. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    TIGRFAMsi TIGR02174. CXXU_selWTH. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Conserved features of selenocysteine insertion sequence (SECIS) elements in selenoprotein W cDNAs from five species."
      Gu Q.-P., Beilstein M.A., Vendeland S.C., Lugade A., Ream W., Whanger P.D.
      Gene 193:187-196(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skeletal muscle.
    2. "Selenoprotein W is a glutathione-dependent antioxidant in vivo."
      Jeong D., Kim T.S., Chung Y.W., Lee B.J., Kim I.Y.
      FEBS Lett. 517:225-228(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF SEC-13 AND CYS-37.
      Tissue: Brain.
    3. "SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family."
      Dikiy A., Novoselov S.V., Fomenko D.E., Sengupta A., Carlson B.A., Cerny R.L., Ginalski K., Grishin N.V., Hatfield D.L., Gladyshev V.N.
      Biochemistry 46:6871-6882(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH YWHAB; YWHAG; DPYSL2; PRDX1; HSP70 AND HSP90, TISSUE SPECIFICITY.
      Tissue: Brain.
    4. Bellingham J., Gregory-Evans C.Y.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
      Tissue: Fetus.
    5. "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: Kidney and Stomach.
    6. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    7. "Selenoprotein W during development and oxidative stress."
      Loflin J., Lopez N., Whanger P.D., Kioussi C.
      J. Inorg. Biochem. 100:1679-1684(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INDUCTION.
    8. "Solution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins."
      Aachmann F.L., Fomenko D.E., Soragni A., Gladyshev V.N., Dikiy A.
      J. Biol. Chem. 282:37036-37044(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF MUTANT SER-10/CYS-13, INTERACTION WITH YWHAB AND YWHAG.

    Entry informationi

    Entry nameiSELW_MOUSE
    AccessioniPrimary (citable) accession number: P63300
    Secondary accession number(s): O35965, P49904, Q9JIC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 82 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3