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P24704

- SODC1_ARATH

UniProt

P24704 - SODC1_ARATH

Protein

Superoxide dismutase [Cu-Zn] 1

Gene

CSD1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

    Catalytic activityi

    2 superoxide + 2 H+ = O2 + H2O2.

    Cofactori

    Binds 1 copper ion per subunit.By similarity
    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi45 – 451Copper; catalyticBy similarity
    Metal bindingi47 – 471Copper; catalyticBy similarity
    Metal bindingi62 – 621Copper; catalyticBy similarity
    Metal bindingi62 – 621Zinc; structuralBy similarity
    Metal bindingi70 – 701Zinc; structuralBy similarity
    Metal bindingi79 – 791Zinc; structuralBy similarity
    Metal bindingi82 – 821Zinc; structuralBy similarity
    Metal bindingi119 – 1191Copper; catalyticBy similarity

    GO - Molecular functioni

    1. copper ion binding Source: RefGenome
    2. protein binding Source: UniProtKB
    3. superoxide dismutase activity Source: TAIR
    4. zinc ion binding Source: RefGenome

    GO - Biological processi

    1. cellular response to copper ion Source: TAIR
    2. cellular response to light intensity Source: UniProtKB
    3. cellular response to oxidative stress Source: UniProtKB
    4. cellular response to ozone Source: UniProtKB
    5. cellular response to salt stress Source: UniProtKB
    6. cellular response to sucrose stimulus Source: UniProtKB
    7. cellular response to UV-B Source: UniProtKB
    8. defense response to bacterium Source: TAIR
    9. gene silencing by miRNA Source: UniProtKB
    10. removal of superoxide radicals Source: RefGenome
    11. response to copper ion Source: TAIR
    12. response to iron ion Source: TAIR
    13. response to oxidative stress Source: TAIR
    14. response to ozone Source: TAIR
    15. response to salt stress Source: TAIR

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciARA:AT1G08830-MONOMER.
    ARA:GQT-656-MONOMER.
    MetaCyc:AT1G08830-MONOMER.
    ReactomeiREACT_180046. Detoxification of Reactive Oxygen Species.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superoxide dismutase [Cu-Zn] 1 (EC:1.15.1.1)
    Alternative name(s):
    Copper/zinc superoxide dismutase 1
    Gene namesi
    Name:CSD1
    Synonyms:SODCC
    Ordered Locus Names:At1g08830
    ORF Names:F22O13.32
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G08830.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular region Source: RefGenome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 152151Superoxide dismutase [Cu-Zn] 1PRO_0000164131Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi56 ↔ 145By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP24704.
    PRIDEiP24704.

    Expressioni

    Tissue specificityi

    Expressed in leaves and pollen (at protein level). The spatial localization is regulated by miR398-mediated silencing. Mostly present in flowers, old rosette leaves and inflorescence, and, to a lower extent, in cauline leaves, stems and roots.3 Publications

    Inductioni

    Upon photosynthetically active radiation (PAR) (e.g. light fluence) increase and UV-B treatment. Accumulates in response to ozone fumigation. Induced in response to oxidative stress, via a reduction of miR398-mediated silencing. Repressed by sucrose in a miR398-mediated silencing-dependent manner. Induced by salt stress.4 Publications

    Gene expression databases

    ArrayExpressiP24704.
    GenevestigatoriP24704.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with DJ1A and CCS.2 Publications

    Protein-protein interaction databases

    BioGridi22646. 4 interactions.
    IntActiP24704. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP24704.
    SMRiP24704. Positions 1-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Cu-Zn superoxide dismutase family.Curated

    Phylogenomic databases

    eggNOGiCOG2032.
    HOGENOMiHOG000263447.
    InParanoidiP24704.
    KOiK04565.
    OMAiEIEVKLH.
    PhylomeDBiP24704.

    Family and domain databases

    Gene3Di2.60.40.200. 1 hit.
    InterProiIPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view]
    PfamiPF00080. Sod_Cu. 1 hit.
    [Graphical view]
    PRINTSiPR00068. CUZNDISMTASE.
    SUPFAMiSSF49329. SSF49329. 1 hit.
    PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P24704-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKGVAVLNS SEGVTGTIFF TQEGDGVTTV SGTVSGLKPG LHGFHVHALG    50
    DTTNGCMSTG PHFNPDGKTH GAPEDANRHA GDLGNITVGD DGTATFTITD 100
    CQIPLTGPNS IVGRAVVVHA DPDDLGKGGH ELSLATGNAG GRVACGIIGL 150
    QG 152
    Length:152
    Mass (Da):15,098
    Last modified:January 23, 2007 - v2
    Checksum:i59E01FF9794F34BD
    GO

    Sequence cautioni

    The sequence AAF99769.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti148 – 1481I → F in ABN50366. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60935 mRNA. Translation: CAA43270.1.
    EF408820 mRNA. Translation: ABN50366.1.
    AC003981 Genomic DNA. Translation: AAF99769.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE28354.1.
    CP002684 Genomic DNA. Translation: AEE28355.1.
    AY091168 mRNA. Translation: AAM14107.1.
    AY050932 mRNA. Translation: AAK93609.1.
    AY087273 mRNA. Translation: AAM64826.1.
    PIRiS19117. DSMUZ.
    RefSeqiNP_001077494.1. NM_001084025.1.
    NP_172360.1. NM_100757.3.
    UniGeneiAt.25177.

    Genome annotation databases

    EnsemblPlantsiAT1G08830.1; AT1G08830.1; AT1G08830.
    AT1G08830.2; AT1G08830.2; AT1G08830.
    GeneIDi837405.
    KEGGiath:AT1G08830.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60935 mRNA. Translation: CAA43270.1 .
    EF408820 mRNA. Translation: ABN50366.1 .
    AC003981 Genomic DNA. Translation: AAF99769.1 . Sequence problems.
    CP002684 Genomic DNA. Translation: AEE28354.1 .
    CP002684 Genomic DNA. Translation: AEE28355.1 .
    AY091168 mRNA. Translation: AAM14107.1 .
    AY050932 mRNA. Translation: AAK93609.1 .
    AY087273 mRNA. Translation: AAM64826.1 .
    PIRi S19117. DSMUZ.
    RefSeqi NP_001077494.1. NM_001084025.1.
    NP_172360.1. NM_100757.3.
    UniGenei At.25177.

    3D structure databases

    ProteinModelPortali P24704.
    SMRi P24704. Positions 1-152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 22646. 4 interactions.
    IntActi P24704. 1 interaction.

    Proteomic databases

    PaxDbi P24704.
    PRIDEi P24704.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G08830.1 ; AT1G08830.1 ; AT1G08830 .
    AT1G08830.2 ; AT1G08830.2 ; AT1G08830 .
    GeneIDi 837405.
    KEGGi ath:AT1G08830.

    Organism-specific databases

    TAIRi AT1G08830.

    Phylogenomic databases

    eggNOGi COG2032.
    HOGENOMi HOG000263447.
    InParanoidi P24704.
    KOi K04565.
    OMAi EIEVKLH.
    PhylomeDBi P24704.

    Enzyme and pathway databases

    BioCyci ARA:AT1G08830-MONOMER.
    ARA:GQT-656-MONOMER.
    MetaCyc:AT1G08830-MONOMER.
    Reactomei REACT_180046. Detoxification of Reactive Oxygen Species.

    Gene expression databases

    ArrayExpressi P24704.
    Genevestigatori P24704.

    Family and domain databases

    Gene3Di 2.60.40.200. 1 hit.
    InterProi IPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view ]
    Pfami PF00080. Sod_Cu. 1 hit.
    [Graphical view ]
    PRINTSi PR00068. CUZNDISMTASE.
    SUPFAMi SSF49329. SSF49329. 1 hit.
    PROSITEi PS00087. SOD_CU_ZN_1. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA and derived amino acid sequence of a cytosolic Cu,Zn superoxide dismutase from Arabidopsis thaliana (L.) Heyhn."
      Hindges R., Slusarenko A.J.
      Plant Mol. Biol. 18:123-125(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
      Tissue: Leaf and Stem.
    2. "Copper, zinc superoxide dismutase [Arabidopsis thaliana]."
      Rani A., Kumar S.
      Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Superoxide dismutase in Arabidopsis: an eclectic enzyme family with disparate regulation and protein localization."
      Kliebenstein D.J., Monde R.A., Last R.L.
      Plant Physiol. 118:637-650(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION BY LIGHT; UV-B AND OZONE, GENE FAMILY.
    8. "A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis."
      Chu C.C., Lee W.C., Guo W.Y., Pan S.M., Chen L.J., Li H.M., Jinn T.L.
      Plant Physiol. 139:425-436(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCS.
    9. "Proteome mapping of mature pollen of Arabidopsis thaliana."
      Holmes-Davis R., Tanaka C.K., Vensel W.H., Hurkman W.J., McCormick S.
      Proteomics 5:4864-4884(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY [LARGE SCALE ANALYSIS].
    10. "Posttranscriptional induction of two Cu/Zn superoxide dismutase genes in Arabidopsis is mediated by downregulation of miR398 and important for oxidative stress tolerance."
      Sunkar R., Kapoor A., Zhu J.-K.
      Plant Cell 18:2051-2065(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION BY OXIDATIVE STRESS.
    11. "Long-term effects of mild salt stress on growth, ion accumulation and superoxide dismutase expression of Arabidopsis rosette leaves."
      Attia H., Arnaud N., Karray N., Lachaal M.
      Physiol. Plantarum 132:293-305(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY SALT.
      Strain: cv. Columbia.
    12. "Sucrose induction of Arabidopsis miR398 represses two Cu/Zn superoxide dismutases."
      Dugas D.V., Bartel B.
      Plant Mol. Biol. 67:403-417(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY SUCROSE.
      Strain: cv. Columbia.
    13. "The Arabidopsis DJ-1a protein confers stress protection through cytosolic SOD activation."
      Xu X.M., Lin H., Maple J., Bjoerkblom B., Alves G., Larsen J.P., Moeller S.G.
      J. Cell Sci. 123:1644-1651(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DJ1A.

    Entry informationi

    Entry nameiSODC1_ARATH
    AccessioniPrimary (citable) accession number: P24704
    Secondary accession number(s): A3FMJ0, Q9FRQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3