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Protein

Superoxide dismutase [Cu-Zn]

Gene

Sod1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Copper; catalyticBy similarity
Metal bindingi49 – 491Copper; catalyticBy similarity
Metal bindingi64 – 641Copper; catalyticBy similarity
Metal bindingi64 – 641Zinc; structuralBy similarity
Metal bindingi72 – 721Zinc; structuralBy similarity
Metal bindingi81 – 811Zinc; structuralBy similarity
Metal bindingi84 – 841Zinc; structuralBy similarity
Metal bindingi121 – 1211Copper; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-114608. Platelet degranulation.
R-RNO-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:Sod1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi3731. Sod1.

Subcellular locationi

GO - Cellular componenti

  • axon Source: GOC
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite cytoplasm Source: UniProtKB
  • dense core granule Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: RGD
  • extracellular space Source: UniProtKB
  • lysosome Source: CACAO
  • mitochondrial intermembrane space Source: RGD
  • mitochondrion Source: UniProtKB
  • myelin sheath Source: Ensembl
  • neuronal cell body Source: UniProtKB
  • neuron projection Source: RGD
  • nucleoplasm Source: Ensembl
  • nucleus Source: UniProtKB
  • peroxisome Source: UniProtKB
  • plasma membrane Source: Ensembl
  • protein complex Source: UniProtKB
  • secretory granule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity2 Publications
Chaini2 – 154153Superoxide dismutase [Cu-Zn]PRO_0000164067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei4 – 41N6-succinyllysineBy similarity
Lipidationi7 – 71S-palmitoyl cysteineBy similarity
Modified residuei10 – 101N6-succinyllysineBy similarity
Disulfide bondi58 ↔ 147By similarity
Modified residuei92 – 921N6-succinyllysineBy similarity
Modified residuei99 – 991PhosphoserineCombined sources
Modified residuei106 – 1061PhosphoserineCombined sources
Modified residuei108 – 1081PhosphoserineCombined sources
Modified residuei123 – 1231N6-acetyllysine; alternateBy similarity
Modified residuei123 – 1231N6-succinyllysine; alternateBy similarity
Modified residuei137 – 1371N6-acetyllysine; alternateBy similarity
Modified residuei137 – 1371N6-succinyllysine; alternateBy similarity

Post-translational modificationi

Palmitoylation helps nuclear targeting and decreases catalytic activity.By similarity
Succinylation, adjacent to copper catalytic site probably inhibit activity. Desuccinylated by SIRT5, enhancing activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP07632.
PRIDEiP07632.

PTM databases

iPTMnetiP07632.
PhosphoSiteiP07632.

Expressioni

Gene expression databases

GenevisibleiP07632. RN.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • enzyme binding Source: RGD
  • protein phosphatase 2B binding Source: UniProtKB

Protein-protein interaction databases

BioGridi246910. 4 interactions.
IntActiP07632. 1 interaction.
MINTiMINT-6612994.
STRINGi10116.ENSRNOP00000002885.

Structurei

3D structure databases

ProteinModelPortaliP07632.
SMRiP07632. Positions 2-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP07632.
KOiK04565.
OMAiVCVLKGT.
OrthoDBiEOG776SR4.
PhylomeDBiP07632.
TreeFamiTF105131.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
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.

P07632-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMKAVCVLK GDGPVQGVIH FEQKASGEPV VVSGQITGLT EGEHGFHVHQ
60 70 80 90 100
YGDNTQGCTT AGPHFNPHSK KHGGPADEER HVGDLGNVAA GKDGVANVSI
110 120 130 140 150
EDRVISLSGE HSIIGRTMVV HEKQDDLGKG GNEESTKTGN AGSRLACGVI

GIAQ
Length:154
Mass (Da):15,912
Last modified:January 23, 2007 - v2
Checksum:iB7D93A135E9279E9
GO

Sequence cautioni

The sequence AAA42160.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA79925.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00404 mRNA. Translation: CAA68465.1.
M25157 mRNA. Translation: AAA42160.1. Different initiation.
X05634 mRNA. Translation: CAA29121.1.
Z21917
, Z21918, Z21919, Z21920 Genomic DNA. Translation: CAA79925.1. Different initiation.
BC082800 mRNA. Translation: AAH82800.1.
PIRiJC1192.
RefSeqiNP_058746.1. NM_017050.1.
UniGeneiRn.6059.

Genome annotation databases

EnsembliENSRNOT00000002885; ENSRNOP00000002885; ENSRNOG00000002115.
GeneIDi24786.
KEGGirno:24786.
UCSCiRGD:3731. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00404 mRNA. Translation: CAA68465.1.
M25157 mRNA. Translation: AAA42160.1. Different initiation.
X05634 mRNA. Translation: CAA29121.1.
Z21917
, Z21918, Z21919, Z21920 Genomic DNA. Translation: CAA79925.1. Different initiation.
BC082800 mRNA. Translation: AAH82800.1.
PIRiJC1192.
RefSeqiNP_058746.1. NM_017050.1.
UniGeneiRn.6059.

3D structure databases

ProteinModelPortaliP07632.
SMRiP07632. Positions 2-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246910. 4 interactions.
IntActiP07632. 1 interaction.
MINTiMINT-6612994.
STRINGi10116.ENSRNOP00000002885.

PTM databases

iPTMnetiP07632.
PhosphoSiteiP07632.

Proteomic databases

PaxDbiP07632.
PRIDEiP07632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002885; ENSRNOP00000002885; ENSRNOG00000002115.
GeneIDi24786.
KEGGirno:24786.
UCSCiRGD:3731. rat.

Organism-specific databases

CTDi6647.
RGDi3731. Sod1.

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP07632.
KOiK04565.
OMAiVCVLKGT.
OrthoDBiEOG776SR4.
PhylomeDBiP07632.
TreeFamiTF105131.

Enzyme and pathway databases

ReactomeiR-RNO-114608. Platelet degranulation.
R-RNO-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi604408.
PROiP07632.

Gene expression databases

GenevisibleiP07632. RN.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA and deduced amino acid sequence of rat copper-zinc-containing superoxide dismutase."
    Ho Y.-S., Crapo J.D.
    Nucleic Acids Res. 15:6746-6746(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Rat lung Cu,Zn superoxide dismutase. Isolation and sequence of a full-length cDNA and studies of enzyme induction."
    Hass M.A., Iqbal J., Clerch L.B., Frank L., Massaro D.
    J. Clin. Invest. 83:1241-1246(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  3. "Rat copper/zinc superoxide dismutase gene: isolation, characterization, and species comparison."
    Hsu J.L., Visner G.A., Burr I.A., Nick H.S.
    Biochem. Biophys. Res. Commun. 186:936-943(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Isolation and analysis of the rat genomic sequence encoding Cu/Zn superoxide dismutase."
    Kim Y.H., Yoo H.Y., Jung G., Kim J.Y., Rho H.M.
    Gene 133:267-271(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  5. "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: Ovary.
  6. "The amino-acid sequence of rat Cu-Zn superoxide dismutase."
    Steffens G.J., Michelson A.M., Puget K., Flohe L.
    Biol. Chem. Hoppe-Seyler 367:1017-1024(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-154.
  7. "Cloning and sequencing of a rat CuZn superoxide dismutase cDNA. Correlation between CuZn superoxide dismutase mRNA level and enzyme activity in rat and mouse tissues."
    Delabar J.-M., Nicole A., D'Auriol L., Jacob Y., Meunier-Rotival M., Galibert F., Sinet P.-M., Jerome H.
    Eur. J. Biochem. 166:181-187(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-154.
    Tissue: Liver.
  8. "Superoxide dismutase protects calcineurin from inactivation."
    Wang X., Culotta V.C., Klee C.B.
    Nature 383:434-437(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21 AND 93-103.
  9. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 11-24; 81-116 AND 145-154, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  10. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-106 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSODC_RAT
AccessioniPrimary (citable) accession number: P07632
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.