P60052 (SODC_PANTR) 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

Pan troglodytes (Chimpanzee) [Reference proteome]

Taxonomic identifier

9598 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Pan

Protein attributes

Sequence length	154 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
Subcellular location	Cytoplasm By similarity.
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 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 By similarity
	Chain	2 – 154	153	Superoxide dismutase [Cu-Zn]		PRO_0000164063
Sites
	Metal binding	47	1	Copper; catalytic By similarity
	Metal binding	49	1	Copper; catalytic By similarity
	Metal binding	64	1	Copper; catalytic By similarity
	Metal binding	64	1	Zinc; structural By similarity
	Metal binding	72	1	Zinc; structural By similarity
	Metal binding	81	1	Zinc; structural By similarity
	Metal binding	84	1	Zinc; structural By similarity
	Metal binding	121	1	Copper; catalytic By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	71	1	N6-acetyllysine By similarity
	Modified residue	99	1	Phosphoserine By similarity
	Modified residue	123	1	N6-acetyllysine By similarity
	Disulfide bond	58 ↔ 147		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P60052 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 25CA38DA8D564483	FASTA	154	15,936
	10 20 30 40 50 60 MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS 70 80 90 100 110 120 AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV 130 140 150 HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ

References

[1]	"Structure, molecular evolution, and gene expression of primate superoxide dismutases." Fukuhara R., Tezuka T., Kageyama T. Gene 296:99-109(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB087266 mRNA. Translation: BAC20345.1.
RefSeq	NP_001009025.1. NM_001009025.1.
UniGene	Ptr.428.
3D structure databases
ProteinModelPortal	P60052.
ModBase	Search...
Protein-protein interaction databases
STRING	9598.ENSPTRP00000056696.
Proteomic databases
PRIDE	P60052.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSPTRT00000025826; ENSPTRP00000023837; ENSPTRG00000013847.
GeneID	449637.
KEGG	ptr:449637.
Organism-specific databases
CTD	6647.
Phylogenomic databases
eggNOG	COG2032.
GeneTree	ENSGT00530000063226.
HOGENOM	HOG000263447.
HOVERGEN	HBG000062.
KO	K04565.
OMA	APRFESS.
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...
Other
BindingDB	P60052.
NextBio	20832742.

Entry information

Entry name

SODC_PANTR

Accession

Primary (citable) accession number: P60052

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program