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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Gallus gallus (Chicken)
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 bindingi120 – 1201Copper; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:SOD1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 154153Superoxide dismutase [Cu-Zn]PRO_0000164069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Lipidationi8 – 81S-palmitoyl cysteineBy similarity
Disulfide bondi58 ↔ 146By similarity
Modified residuei154 – 1541S-glutathionyl cysteine1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Glutathionylation, Lipoprotein, Palmitate

Proteomic databases

PaxDbiP80566.
PRIDEiP80566.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
KCNMA1Q8AYS83EBI-1637015,EBI-1635766

Protein-protein interaction databases

BioGridi676211. 1 interaction.
IntActiP80566. 1 interaction.
STRINGi9031.ENSGALP00000035996.

Structurei

3D structure databases

ProteinModelPortaliP80566.
SMRiP80566. Positions 5-153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP80566.
KOiK04565.
PhylomeDBiP80566.

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.

P80566-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLKAVCVM KGDAPVEGVI HFQQQGSGPV KVTGKITGLS DGDHGFHVHE
60 70 80 90 100
FGDNTNGCTS AGAHFNPEGK QHGGPKDADR HVGDLGNVTA KGGVAEVEIE
110 120 130 140 150
DSVISLTGPH CIIGRTMVVH AKSDDLGRGG DNESKLTGNA GPRLACGVIG

IAKC
Length:154
Mass (Da):15,704
Last modified:January 23, 2007 - v3
Checksum:iF06FEF9FCBB7FB9E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141A → G AA sequence (PubMed:8647082).Curated

Mass spectrometryi

Molecular mass is 15600±2 Da from positions 2 - 154. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28407 mRNA. Translation: AAB88059.1.
PIRiS65436.
RefSeqiNP_990395.1. NM_205064.1.
UniGeneiGga.3346.

Genome annotation databases

GeneIDi395938.
KEGGigga:395938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28407 mRNA. Translation: AAB88059.1.
PIRiS65436.
RefSeqiNP_990395.1. NM_205064.1.
UniGeneiGga.3346.

3D structure databases

ProteinModelPortaliP80566.
SMRiP80566. Positions 5-153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676211. 1 interaction.
IntActiP80566. 1 interaction.
STRINGi9031.ENSGALP00000035996.

Proteomic databases

PaxDbiP80566.
PRIDEiP80566.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi395938.
KEGGigga:395938.

Organism-specific databases

CTDi6647.

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP80566.
KOiK04565.
PhylomeDBiP80566.

Miscellaneous databases

PROiP80566.

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

  1. "Characterisation of the chicken Cu,Zn superoxide dismutase gene."
    Stanton J.L., Wilton S.D., Laing N.G.
    DNA Seq. 6:357-360(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Spinal cord.
  2. "Amino acid sequence of chicken Cu,Zn-containing superoxide dismutase and identification of glutathionyl adducts at exposed cysteine residues."
    Schinina M.E., Carlini P., Polticelli F., Zappacosta F., Bossa F., Calabrese L.
    Eur. J. Biochem. 237:433-439(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-154, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, GLUTATHIONYLATION AT CYS-154, MASS SPECTROMETRY.
    Tissue: Erythrocyte.

Entry informationi

Entry nameiSODC_CHICK
AccessioniPrimary (citable) accession number: P80566
Secondary accession number(s): Q92059
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 119 of the entry and version 3 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.