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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Bos taurus (Bovine)
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.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

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, 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

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite cytoplasm Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular space Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

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.

Expressioni

Gene expression databases

BgeeiENSBTAG00000018854.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

IntActiP00442. 1 interactor.
STRINGi9913.ENSBTAP00000032384.

Structurei

Secondary structure

1152
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Beta strandi12 – 14Combined sources3
Beta strandi16 – 24Combined sources9
Beta strandi27 – 36Combined sources10
Beta strandi39 – 48Combined sources10
Turni53 – 56Combined sources4
Helixi57 – 59Combined sources3
Beta strandi76 – 78Combined sources3
Beta strandi82 – 88Combined sources7
Turni90 – 92Combined sources3
Beta strandi94 – 102Combined sources9
Beta strandi104 – 107Combined sources4
Beta strandi114 – 121Combined sources8
Beta strandi128 – 130Combined sources3
Helixi133 – 136Combined sources4
Beta strandi141 – 147Combined sources7
Beta strandi149 – 152Combined sources4

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...

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.
OMAiKVWGSIT.
OrthoDBiEOG091G0OG2.
TreeFamiTF105131.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
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.

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.

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. 1 interactor.
STRINGi9913.ENSBTAP00000032384.

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.
OMAiKVWGSIT.
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.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
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...

Entry informationi

Entry nameiSODC_BOVIN
AccessioniPrimary (citable) accession number: P00442
Secondary accession number(s): Q3ZCF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

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.