Reviewed, UniProtKB/Swiss-Prot P33431 (SODC_CAVPO)

Names and origin

Protein names

Recommended name:
    Superoxide dismutase [Cu-Zn]
    EC=1.15.1.1

Gene names

Name:

SOD1

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2.
Cofactor	Binds 1 copper ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptosis Inferred from sequence or structural similarity. Source: UniProtKB activation of MAPK activity Inferred from sequence or structural similarity. Source: UniProtKB auditory receptor cell stereocilium organization Inferred from sequence or structural similarity. Source: UniProtKB cell aging Inferred from sequence or structural similarity. Source: UniProtKB cellular iron ion homeostasis Inferred from sequence or structural similarity. Source: UniProtKB double-strand break repair Inferred from sequence or structural similarity. Source: UniProtKB embryo implantation Inferred from sequence or structural similarity. Source: UniProtKB glutathione metabolic process Inferred from sequence or structural similarity. Source: UniProtKB heart contraction Inferred from sequence or structural similarity. Source: UniProtKB hydrogen peroxide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB locomotory behavior Inferred from sequence or structural similarity. Source: UniProtKB muscle homeostasis Inferred from sequence or structural similarity. Source: UniProtKB myelin maintenance in the peripheral nervous system Inferred from sequence or structural similarity. Source: UniProtKB myeloid cell homeostasis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cholesterol biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of neuron apoptosis Inferred from sequence or structural similarity. Source: UniProtKB neurofilament cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB ovarian follicle development Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cytokine production Inferred from sequence or structural similarity. Source: UniProtKB regulation of blood pressure Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitochondrial membrane potential Inferred from sequence or structural similarity. Source: UniProtKB regulation of multicellular organism growth Inferred from sequence or structural similarity. Source: UniProtKB relaxation of vascular smooth muscle Inferred from sequence or structural similarity. Source: UniProtKB removal of superoxide radicals Inferred from sequence or structural similarity. Source: UniProtKB response to axon injury Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from sequence or structural similarity. Source: UniProtKB response to ethanol Inferred from sequence or structural similarity. Source: UniProtKB response to heat Inferred from sequence or structural similarity. Source: UniProtKB response to hydrogen peroxide Inferred from sequence or structural similarity. Source: UniProtKB response to superoxide Inferred from sequence or structural similarity. Source: UniProtKB retina homeostasis Inferred from sequence or structural similarity. Source: UniProtKB sensory perception of sound Inferred from sequence or structural similarity. Source: UniProtKB spermatogenesis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cell soma Inferred from sequence or structural similarity. Source: UniProtKB cytoplasmic vesicle Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB dendrite cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB extracellular matrix Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	antioxidant activity Inferred from electronic annotation. Source: UniProtKB-KW chaperone binding Inferred from sequence or structural similarity. Source: UniProtKB copper ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein phosphatase 2B binding Inferred from sequence or structural similarity. Source: UniProtKB superoxide dismutase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 153	152	Superoxide dismutase [Cu-Zn]		PRO_0000164053
Sites
	Metal binding	46	1	Copper; catalytic By similarity
	Metal binding	48	1	Copper; catalytic By similarity
	Metal binding	63	1	Copper; catalytic By similarity
	Metal binding	63	1	Zinc; structural By similarity
	Metal binding	71	1	Zinc; structural By similarity
	Metal binding	80	1	Zinc; structural By similarity
	Metal binding	83	1	Zinc; structural By similarity
	Metal binding	120	1	Copper; catalytic By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine
	Modified residue	70	1	N6-acetyllysine By similarity
	Modified residue	98	1	Phosphoserine By similarity
	Modified residue	122	1	N6-acetyllysine By similarity
	Disulfide bond	57 ↔ 146		By similarity
Experimental info
	Sequence conflict	103 – 104	2	LI → IL AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P33431-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B82C13327FACF227	FASTA	153	15,670
	10 20 30 40 50 60 MATKAVCVLK GDGPVQGIIH FEQKANGPVV VKGRITGLVE GKHGFHVHEF GDNTQGCTSA 70 80 90 100 110 120 GPHFNPLSKK HGGPQDEERH VGDLGNVTAG ADGVANVSIE DSLISLSGAN SIIGRTMVVH 130 140 150 EKPDDLGKGG NEESTKTGNA GSRLACGVIG IAQ

References

[1]	"Differential patterns of antioxidant enzyme mRNA expression in guinea pig lung and liver during development." Yuan H.T., Bingle C.D., Kelly F.J. Biochim. Biophys. Acta 1305:163-171(1996) [PubMed: 8597602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Hartley. Tissue: Lung.
[2]	"Taxonomical classification of the guinea pig based on its Cu/Zn superoxide dismutase sequence." Wolf B., Reinecke K., Aumann K.-D., Brigelius-Flohe R., Flohe L. Biol. Chem. Hoppe-Seyler 374:641-649(1993) [PubMed: 8240718] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-153. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U39844 mRNA. Translation: AAC52720.1.
PIR	S36108.
3D structure databases
HSSP	HSSP built from PDB template 1HL5 based on UniProtKB P00441.
SMR	P33431. Positions 4-153.
ModBase	Search...
Protein-protein interaction databases
STRING	P33431.
Genome annotation databases
Ensembl	ENSCPOT00000014365; ENSCPOP00000012815; ENSCPOG00000014223; Cavia porcellus. [Genome view]
Phylogenomic databases
HOVERGEN	P33431.
Enzyme and pathway databases
BRENDA	1.15.1.1. 44.
Family and domain databases
InterPro	IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn. [Graphical view]
Gene3D	G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PANTHER	PTHR10003. SOD_Cu_Zn. 1 hit.
Pfam	PF00080. Sod_Cu. 1 hit. [Graphical view]
PRINTS	PR00068. CUZNDISMTASE.
ProDom	PD000469. SOD_CU_ZN. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SODC_CAVPO

Accession

Primary (citable) accession number: P33431

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)