Reviewed, UniProtKB/Swiss-Prot A8XCP3 (SODC_CAEBR)

Names and origin

Protein names

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

Gene names

Name:	sod-1
ORF Names:	CBG11197

Organism

Caenorhabditis briggsae [Complete proteome]

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Required for normal brood size By similarity. UniProtKB P00441 UniProtKB P34697
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2. UniProtKB P00441
Cofactor	Binds 1 copper ion per subunit By similarity. UniProtKB P00441 Binds 1 zinc ion per subunit By similarity. UniProtKB P00441
Subunit structure	Homodimer By similarity. UniProtKB P00441
Subcellular location	Cytoplasm By similarity. UniProtKB P00441
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of brood size Inferred from sequence or structural similarity. Source: UniProtKB superoxide metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	antioxidant activity Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB superoxide dismutase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 180	161	Superoxide dismutase [Cu-Zn]		PRO_0000331231
Sites
	Metal binding	68	1	Copper; catalytic By similarity UniProtKB P00441
	Metal binding	70	1	Copper; catalytic By similarity UniProtKB P00441
	Metal binding	85	1	Copper; catalytic By similarity UniProtKB P00441
	Metal binding	85	1	Zinc; structural By similarity
	Metal binding	93	1	Zinc; structural By similarity UniProtKB P00441
	Metal binding	102	1	Zinc; structural By similarity UniProtKB P00441
	Metal binding	105	1	Zinc; structural By similarity UniProtKB P00441
	Metal binding	142	1	Copper; catalytic By similarity UniProtKB P00441
Amino acid modifications
	Disulfide bond	79 ↔ 171		By similarity UniProtKB P00441

Sequences

	Sequence		Length	Mass (Da)
	A8XCP3-1 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: 24362A5FEDF4D8E0	FASTA	180	18,524
	10 20 30 40 50 60 MFMNLLSQVS NAIFPQVEAA QKMSNRAVAV LRGDVVSGTI WITQNSESDP AVIEGEIKGL 70 80 90 100 110 120 TPGLHGFHVH QYGDSTNGCL SAGPHFNPFG KTHGGPNSET RHVGDLGNVE AGADGVAKVH 130 140 150 160 170 180 ITDKLITLYG ANTVIGRSMV VHAGQDDLGQ GVGDKAEESA KTGNAGARAA CGVIALAAPQ

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CAAC02000499 Genomic DNA. Translation: CAP30392.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GenomeReviews	Gene locus sod-1 in contig CU538965_GR.
UCSC	C15F1.7a. c. elegans.
Organism-specific databases
WormBase	WBGene00032360. Cbr-sod-1.
Phylogenomic databases
OMA	HAGQDDL.
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_CAEBR

Accession

Primary (citable) accession number: A8XCP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	January 15, 2008
Last modified:	November 3, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project