P33431 (SODC_CAVPO) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of MAPK activity Inferred from sequence or structural similarity. Source: UniProtKB anterograde axon cargo transport Inferred from electronic annotation. Source: Compara apoptotic DNA fragmentation 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 cell homeostasis 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 apoptotic process 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 peripheral nervous system myelin maintenance Inferred from sequence or structural similarity. Source: UniProtKB 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 retina homeostasis Inferred from sequence or structural similarity. Source: UniProtKB retrograde axon cargo transport Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from sequence or structural similarity. Source: UniProtKB spermatogenesis Inferred from sequence or structural similarity. Source: UniProtKB superoxide anion generation Inferred from electronic annotation. Source: Compara
Cellular_component	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 neuronal cell body Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara protein complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	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 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-153. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U39844 mRNA. Translation: AAC52720.1.
PIR	S36108.
RefSeq	XP_003467296.1. XM_003467248.1.
3D structure databases
ProteinModelPortal	P33431.
SMR	P33431. Positions 4-153.
ModBase	Search...
Protein-protein interaction databases
STRING	10141.ENSCPOP00000012815.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100135622.
Organism-specific databases
CTD	6647.
Phylogenomic databases
eggNOG	COG2032.
HOGENOM	HOG000263447.
HOVERGEN	HBG000062.
InParanoid	P33431.
OrthoDB	EOG45HRZM.
Family and domain databases
Gene3D	2.60.40.200. 1 hit.
InterPro	IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
PANTHER	PTHR10003. PTHR10003. 1 hit.
Pfam	PF00080. Sod_Cu. 1 hit. [Graphical view]
PRINTS	PR00068. CUZNDISMTASE.
SUPFAM	SSF49329. SOD_Cu_Zn. 1 hit.
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:	April 3, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program