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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Bos taurus (Bovine)
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.1 Publication

Miscellaneous

Chemical modification of Arg-142 reduces activity by 80-90%.1 Publication

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.1 Publication

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 bindingi45Copper; catalytic2 Publications1
Metal bindingi47Copper; catalytic2 Publications1
Metal bindingi62Copper; catalytic2 Publications1
Metal bindingi62Zinc; structural1 Publication1
Metal bindingi70Zinc; structural1 Publication1
Metal bindingi79Zinc; structural1 Publication1
Metal bindingi82Zinc; structural1 Publication1
Metal bindingi119Copper; catalytic2 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntioxidant, Oxidoreductase
LigandCopper, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi1.15.1.1 908
ReactomeiR-BTA-114608 Platelet degranulation
R-BTA-3299685 Detoxification of Reactive Oxygen Species

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.11 Publication)
Gene namesi
Name:SOD1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001640492 – 152Superoxide dismutase [Cu-Zn]Add BLAST151

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei4N6-succinyllysineBy similarity1
Lipidationi7S-palmitoyl cysteineBy similarity1
Modified residuei10N6-succinyllysineBy similarity1
Disulfide bondi56 ↔ 1451 Publication
Modified residuei90N6-succinyllysineBy similarity1
Modified residuei104PhosphoserineBy similarity1
Modified residuei106PhosphoserineBy similarity1
Modified residuei121N6-acetyllysine; alternateBy similarity1
Modified residuei121N6-succinyllysine; alternateBy similarity1
Modified residuei135N6-acetyllysine; alternateBy similarity1
Modified residuei135N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

Palmitoylation helps nuclear targeting and decreases catalytic activity.By similarity
Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP00442
PeptideAtlasiP00442
PRIDEiP00442

PTM databases

iPTMnetiP00442

Expressioni

Gene expression databases

BgeeiENSBTAG00000018854 Expressed in 10 organ(s), highest expression level in liver

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RAC1P629982EBI-6654424,EBI-6654511

GO - Molecular functioni

Protein-protein interaction databases

IntActiP00442, 2 interactors
STRINGi9913.ENSBTAP00000032384

Chemistry databases

BindingDBiP00442

Structurei

Secondary structure

1152
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP00442
SMRiP00442
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00442

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441 Eukaryota
COG2032 LUCA
GeneTreeiENSGT00530000063226
HOGENOMiHOG000263447
HOVERGENiHBG000062
InParanoidiP00442
KOiK04565
OMAiMAMKAVC
OrthoDBiEOG091G0OG2
TreeFamiTF105131

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.

P00442-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATKAVCVLK GDGPVQGTIH FEAKGDTVVV TGSITGLTEG DHGFHVHQFG
60 70 80 90 100
DNTQGCTSAG PHFNPLSKKH GGPKDEERHV GDLGNVTADK NGVAIVDIVD
110 120 130 140 150
PLISLSGEYS IIGRTMVVHE KPDDLGRGGN EESTKTGNAG SRLACGVIGI

AK
Length:152
Mass (Da):15,683
Last modified:January 23, 2007 - v2
Checksum:iA467EE17E4C31CCD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54799 mRNA No translation available.
M81129 mRNA Translation: AAA73164.1
BC102432 mRNA Translation: AAI02433.1
PIRiI45883 DSBOCZ
RefSeqiNP_777040.1, NM_174615.2
UniGeneiBt.49637

Genome annotation databases

EnsembliENSBTAT00000032452; ENSBTAP00000032384; ENSBTAG00000018854
GeneIDi281495
KEGGibta:281495

Similar proteinsi

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54799 mRNA No translation available.
M81129 mRNA Translation: AAA73164.1
BC102432 mRNA Translation: AAI02433.1
PIRiI45883 DSBOCZ
RefSeqiNP_777040.1, NM_174615.2
UniGeneiBt.49637

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CB4X-ray2.30A/B2-152[»]
1CBJX-ray1.65A/B2-152[»]
1COBX-ray2.00A/B2-152[»]
1E9OX-ray1.85A/B2-152[»]
1E9PX-ray1.70A/B2-151[»]
1E9QX-ray1.75A/B2-152[»]
1Q0EX-ray1.15A/B2-152[»]
1SDAX-ray2.50B/G/O/Y2-152[»]
1SXAX-ray1.90A/B2-152[»]
1SXBX-ray2.00A/B2-152[»]
1SXCX-ray1.90A/B2-152[»]
1SXNX-ray1.90A/B2-152[»]
1SXSX-ray2.00A/B2-152[»]
1SXZX-ray2.05A/B2-152[»]
2AEOX-ray1.80A/B2-152[»]
2SODX-ray2.00B/G/O/Y2-152[»]
2Z7UX-ray2.10A/B2-152[»]
2Z7WX-ray1.80A/B2-152[»]
2Z7YX-ray1.55A/B2-152[»]
2Z7ZX-ray1.85A/B2-152[»]
2ZOWX-ray1.45A/B2-152[»]
3HW7X-ray2.00A/B2-152[»]
3SODX-ray2.10B/G/O/Y2-152[»]
ProteinModelPortaliP00442
SMRiP00442
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00442, 2 interactors
STRINGi9913.ENSBTAP00000032384

Chemistry databases

BindingDBiP00442

PTM databases

iPTMnetiP00442

Proteomic databases

PaxDbiP00442
PeptideAtlasiP00442
PRIDEiP00442

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000032452; ENSBTAP00000032384; ENSBTAG00000018854
GeneIDi281495
KEGGibta:281495

Organism-specific databases

CTDi6647

Phylogenomic databases

eggNOGiKOG0441 Eukaryota
COG2032 LUCA
GeneTreeiENSGT00530000063226
HOGENOMiHOG000263447
HOVERGENiHBG000062
InParanoidiP00442
KOiK04565
OMAiMAMKAVC
OrthoDBiEOG091G0OG2
TreeFamiTF105131

Enzyme and pathway databases

BRENDAi1.15.1.1 908
ReactomeiR-BTA-114608 Platelet degranulation
R-BTA-3299685 Detoxification of Reactive Oxygen Species

Miscellaneous databases

EvolutionaryTraceiP00442

Gene expression databases

BgeeiENSBTAG00000018854 Expressed in 10 organ(s), highest expression level in liver

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
ProtoNetiSearch...

Entry informationi

Entry nameiSODC_BOVIN
AccessioniPrimary (citable) accession number: P00442
Secondary accession number(s): Q3ZCF4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 175 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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