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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Sus scrofa (Pig)
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.

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)DescriptionActionsGraphical viewLength
Metal bindingi46Copper; catalyticBy similarity1
Metal bindingi48Copper; catalyticBy similarity1
Metal bindingi63Copper; catalyticBy similarity1
Metal bindingi63Zinc; structuralBy similarity1
Metal bindingi71Zinc; structuralBy similarity1
Metal bindingi80Zinc; structuralBy similarity1
Metal bindingi83Zinc; structuralBy similarity1
Metal bindingi120Copper; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntioxidant, Oxidoreductase
LigandCopper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SSC-114608 Platelet degranulation
R-SSC-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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

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_00001640642 – 153Superoxide dismutase [Cu-Zn]Add BLAST152

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 bondi57 ↔ 146
Modified residuei91N6-succinyllysineBy similarity1
Modified residuei102PhosphoserineBy similarity1
Modified residuei107PhosphoserineBy similarity1
Modified residuei122N6-acetyllysine; alternateBy similarity1
Modified residuei122N6-succinyllysine; alternateBy similarity1
Modified residuei136N6-acetyllysine; alternateBy similarity1
Modified residuei136N6-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

PaxDbiP04178
PeptideAtlasiP04178
PRIDEiP04178

PTM databases

iPTMnetiP04178

Expressioni

Gene expression databases

BgeeiENSSSCG00000021355
GenevisibleiP04178 SS

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000026815

Structurei

3D structure databases

ProteinModelPortaliP04178
SMRiP04178
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441 Eukaryota
COG2032 LUCA
HOVERGENiHBG000062
InParanoidiP04178
KOiK04565
OMAiIHTFGDN
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.

P04178-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKAVCVLK GDGPVQGTIY FELKGEKTVL VTGTIKGLAE GDHGFHVHQF
60 70 80 90 100
GDNTQGCTSA GPHFNPESKK HGGPKDQERH VGDLGNVTAG KDGVATVYIE
110 120 130 140 150
DSVIALSGDH SIIGRTMVVH EKPDDLGRGG NEESTKTGNA GSRLACGVIG

ITQ
Length:153
Mass (Da):15,892
Last modified:January 23, 2007 - v2
Checksum:i06B625E7D96DA318
GO

Sequence databases

PIRiA00514 DSPGCZ
RefSeqiNP_001177351.1, NM_001190422.1
UniGeneiSsc.12390

Genome annotation databases

GeneIDi397036
KEGGissc:397036

Similar proteinsi

Entry informationi

Entry nameiSODC_PIG
AccessioniPrimary (citable) accession number: P04178
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 139 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

Complete proteome, Direct protein sequencing, Reference proteome

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