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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

Miscellaneous

Present with 519000 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationNote: Binds 1 copper ion per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi43Zinc 2; shared with CCS1; in apo form2 Publications1
Metal bindingi47Copper; catalytic2 Publications1
Metal bindingi49Copper; catalytic2 Publications1
Metal bindingi64Copper; catalytic2 Publications1
Metal bindingi64Zinc 1; structural2 Publications1
Metal bindingi72Zinc 1; structural2 Publications1
Metal bindingi81Zinc 1; structural2 Publications1
Metal bindingi84Zinc 1; structural2 Publications1
Metal bindingi121Copper; catalytic2 Publications1
Binding sitei144SubstrateCurated1

GO - Molecular functioni

  • copper ion binding Source: GO_Central
  • superoxide dismutase activity Source: SGD
  • zinc ion binding Source: GO_Central

GO - Biological processi

  • age-dependent response to reactive oxygen species involved in chronological cell aging Source: SGD
  • cellular copper ion homeostasis Source: SGD
  • cellular zinc ion homeostasis Source: SGD
  • fungal-type cell wall organization Source: SGD
  • negative regulation of cellular respiration Source: SGD
  • positive regulation of DNA binding transcription factor activity Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: SGD
  • protein stabilization Source: SGD
  • superoxide metabolic process Source: SGD

Keywordsi

Molecular functionAntioxidant, Oxidoreductase
LigandCopper, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-1629
ReactomeiR-SCE-114608 Platelet degranulation
R-SCE-3299685 Detoxification of Reactive Oxygen Species

Protein family/group databases

MoonProtiP00445

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:SOD1
Ordered Locus Names:YJR104C
ORF Names:J1968
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR104C
SGDiS000003865 SOD1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi123G → K: Does not enable copper chaperone-independent activation. 1 Publication1
Mutagenesisi131 – 132DT → GN: Does not enable copper chaperone-independent activation. 1 Publication2
Mutagenesisi143P → A or S: Enables copper chaperone-independent activation; when associated with A-145 or with L-145. 2 Publications1
Mutagenesisi145P → A or L: Enables copper chaperone-independent activation; when associated with A-143 or with S-143. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00001641292 – 154Superoxide dismutase [Cu-Zn]Add BLAST153

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei26PhosphoserineCombined sources1
Modified residuei39PhosphoserineCombined sources1
Disulfide bondi58 ↔ 147
Disulfide bondi58Interchain (with C-229 in CCS1); in linked form
Cross-linki70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei99PhosphoserineCombined sources1
Modified residuei117PhosphoserineCombined sources1
Modified residuei132PhosphothreonineCombined sources1
Modified residuei138PhosphothreonineCombined sources1

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP00445
PaxDbiP00445
PRIDEiP00445
TopDownProteomicsiP00445

2D gel databases

SWISS-2DPAGEiP00445

PTM databases

iPTMnetiP00445

Interactioni

Subunit structurei

Homodimer in holo form. In apo form, heterodimer with CCS1. Zinc-binding at 'His-16' of CCS1 and Glu-43 of apo-SOD1 is required for this heterodimerization.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi33860, 243 interactors
ComplexPortaliCPX-2267 SOD1-CCS1 Superoxide Dismutase heterodimer
CPX-2896 [Cu-Zn] Superoxide dismutase complex
DIPiDIP-5859N
IntActiP00445, 17 interactors
MINTiP00445
STRINGi4932.YJR104C

Structurei

Secondary structure

1154
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Beta strandi11 – 13Combined sources3
Beta strandi15 – 21Combined sources7
Beta strandi23 – 27Combined sources5
Beta strandi29 – 37Combined sources9
Beta strandi43 – 50Combined sources8
Turni55 – 58Combined sources4
Helixi59 – 61Combined sources3
Beta strandi77 – 80Combined sources4
Beta strandi84 – 89Combined sources6
Beta strandi96 – 104Combined sources9
Beta strandi107 – 109Combined sources3
Beta strandi116 – 120Combined sources5
Beta strandi130 – 132Combined sources3
Helixi135 – 138Combined sources4
Beta strandi146 – 149Combined sources4
Beta strandi151 – 153Combined sources3

3D structure databases

ProteinModelPortaliP00445
SMRiP00445
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00445

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063226
HOGENOMiHOG000263447
InParanoidiP00445
KOiK04565
OMAiIHTFGDN
OrthoDBiEOG092C578I

Family and domain databases

CDDicd00305 Cu-Zn_Superoxide_Dismutase, 1 hit
Gene3Di2.60.40.200, 1 hit
InterProiView protein in InterPro
IPR036423 SOD-like_Cu/Zn_dom_sf
IPR024134 SOD_Cu/Zn_/chaperone
IPR018152 SOD_Cu/Zn_BS
IPR001424 SOD_Cu_Zn_dom
PANTHERiPTHR10003 PTHR10003, 1 hit
PfamiView protein in Pfam
PF00080 Sod_Cu, 1 hit
PRINTSiPR00068 CUZNDISMTASE
SUPFAMiSSF49329 SSF49329, 1 hit
PROSITEiView protein in PROSITE
PS00087 SOD_CU_ZN_1, 1 hit
PS00332 SOD_CU_ZN_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P00445-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQAVAVLKG DAGVSGVVKF EQASESEPTT VSYEIAGNSP NAERGFHIHE
60 70 80 90 100
FGDATNGCVS AGPHFNPFKK THGAPTDEVR HVGDMGNVKT DENGVAKGSF
110 120 130 140 150
KDSLIKLIGP TSVVGRSVVI HAGQDDLGKG DTEESLKTGN AGPRPACGVI

GLTN
Length:154
Mass (Da):15,855
Last modified:January 23, 2007 - v2
Checksum:iE263A74679AF11F7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56N → D AA sequence (PubMed:6993479).Curated1
Sequence conflicti93N → D AA sequence (PubMed:6993479).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03279 Genomic DNA Translation: AAA34543.1
AY690619 Genomic DNA Translation: AAT99430.1
Z49604 Genomic DNA Translation: CAA89634.1
AY558073 Genomic DNA Translation: AAS56399.1
BK006943 Genomic DNA Translation: DAA08889.1
PIRiA36171 DSBYC
RefSeqiNP_012638.1, NM_001181762.1

Genome annotation databases

EnsemblFungiiYJR104C; YJR104C; YJR104C
GeneIDi853568
KEGGisce:YJR104C

Similar proteinsi

Entry informationi

Entry nameiSODC_YEAST
AccessioniPrimary (citable) accession number: P00445
Secondary accession number(s): D6VWS3, Q68HB2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 210 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

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