Reviewed, UniProtKB/Swiss-Prot Q8HXP9 (SODC_CEBAP)

Names and origin

Protein names

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

Gene names

Name:

SOD1

Organism

Cebus apella (Brown-capped capuchin)

Taxonomic identifier

9515 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Platyrrhini › Cebidae › Cebinae › Cebus

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
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 By similarity
	Chain	2 – 154	153	Superoxide dismutase [Cu-Zn]		PRO_0000164054
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)
	Q8HXP9-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: AFA8A0534CBC34E9	FASTA	154	15,893
	10 20 30 40 50 60 MAMKAVCVLK GDGPVQGTIN FEQKESNGPV KVWGSITGLA EGLHGFHVHQ FGDNTQGCTS 70 80 90 100 110 120 AGPHFNPLSR KHGGPEDEER HVGDLGNVTA GKDGVAKVSI EDSVISLSGD HSIIGRTLVV 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: 12383507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB087272 mRNA. Translation: BAC20351.1.
3D structure databases
HSSP	HSSP built from PDB template 1HL5 based on UniProtKB P00441.
SMR	Q8HXP9. Positions 2-154.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q8HXP9.
Enzyme and pathway databases
BRENDA	1.15.1.1. 293018.
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_CEBAP

Accession

Primary (citable) accession number: Q8HXP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 44 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)