Superoxide dismutase [Cu-Zn] precursor

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Preferred order of sections

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

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P34697 (SODC_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Protein names

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

Gene names

Name:	sod-1
ORF Names:	C15F1.7

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Sequence length	180 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Required for normal brood size. Ref.5
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.
Enzyme regulation	The insertion of copper which activates the protein requires glutathione. This is independent of copper chaperone for SOD1 (CCS), which activates orthologs. Ref.4
Subunit structure	Homodimer. Ref.4
Subcellular location	Cytoplasm By similarity.
Disruption phenotype	Worms exhibit increased oxidative stress and reduced brood size. Ref.5
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	age-dependent response to oxidative stress Inferred from direct assay PubMed 8389142 Ref.1. Source: WormBase regulation of brood size Inferred from mutant phenotype Ref.5. Source: UniProtKB regulation of vulval development Inferred from genetic interaction PubMed 14657502. Source: WormBase removal of superoxide radicals Inferred from mutant phenotype PubMed 19282511. Source: WormBase
Cellular_component	cytosol Inferred from direct assay PubMed 19056880. Source: WormBase mitochondrion Inferred from direct assay PubMed 19056880. Source: WormBase nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	copper ion binding Inferred from direct assay Ref.4. Source: WormBase protein homodimerization activity Inferred from direct assay Ref.4. Source: UniProtKB superoxide dismutase activity Inferred from direct assay Ref.4. Source: UniProtKB zinc ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Signal peptide

1 – 19

Potential

Chain

20 – 180

161

Superoxide dismutase [Cu-Zn]

PRO_0000164102

Metal binding

Copper; catalytic By similarity

Metal binding

Copper; catalytic By similarity

Metal binding

Copper; catalytic By similarity

Metal binding

Zinc; structural By similarity

Metal binding

Zinc; structural By similarity

Metal binding

102

Zinc; structural By similarity

Metal binding

105

Zinc; structural By similarity

Metal binding

142

Copper; catalytic By similarity

Disulfide bond

79 ↔ 171

By similarity

Alternative sequence

1 – 22

Missing in isoform b.

VSP_033146

Mutagenesis

167

A → P: Abolishes enzyme activation but has no affect on disulfide bond formation or dimer formation; when associated with A-169. Ref.4

Mutagenesis

169

A → P: Abolishes enzyme activation but has no affect on disulfide bond formation or dimer formation; when associated with A-167. Ref.4

180

Helix Strand Turn

Details...

Sequence		Length	Mass (Da)
Isoform a [UniParc]. Last modified April 29, 2008. Version 2. Checksum: 5F013D99A650AA97 Show »	FASTA	180	18,700
10 20 30 40 50 60 MFMNLLTQVS NAIFPQVEAA QKMSNRAVAV LRGETVTGTI WITQKSENDQ AVIEGEIKGL 70 80 90 100 110 120 TPGLHGFHVH QYGDSTNGCI SAGPHFNPFG KTHGGPKSEI RHVGDLGNVE AGADGVAKIK 130 140 150 160 170 180 LTDTLVTLYG PNTVVGRSMV VHAGQDDLGE GVGDKAEESK KTGNAGARAA CGVIALAAPQ « Hide
Isoform b [UniParc]. Checksum: 0B4A19EAFF87CF33 Show »	FASTA	158	16,237
10 20 30 40 50 60 MSNRAVAVLR GETVTGTIWI TQKSENDQAV IEGEIKGLTP GLHGFHVHQY GDSTNGCISA 70 80 90 100 110 120 GPHFNPFGKT HGGPKSEIRH VGDLGNVEAG ADGVAKIKLT DTLVTLYGPN TVVGRSMVVH 130 140 150 AGQDDLGEGV GDKAEESKKT GNAGARAACG VIALAAPQ « Hide

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Aging and resistance to oxidative damage in Caenorhabditis elegans." Larsen P.L. Proc. Natl. Acad. Sci. U.S.A. 90:8905-8909(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[2]	"The copper/zinc superoxide dismutase gene of Caenorhabditis elegans." Giglio M.P., Hunter T., Bannister J.V., Bannister W.H., Hunter G.J. Biochem. Mol. Biol. Int. 33:41-44(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B). Strain: Bristol N2.
[3]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Bristol N2.
[4]	"Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS." Jensen L.T., Culotta V.C. J. Biol. Chem. 280:41373-41379(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF ALA-167 AND ALA-169.
[5]	"A measurable increase in oxidative damage due to reduction in superoxide detoxification fails to shorten the life span of long-lived mitochondrial mutants of Caenorhabditis elegans." Yang W., Li J., Hekimi S. Genetics 177:2063-2074(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

EMBL
GenBank
DDBJ

L20135 mRNA. Translation: AAA28147.1.
X77020 Genomic DNA. Translation: CAA54318.1.
FO080553 Genomic DNA. Translation: CCD64617.1.
FO080553 Genomic DNA. Translation: CCD64618.1.

PIR

A48256. S41319.

RefSeq

NP_001021956.1. NM_001026785.2.
NP_001021957.1. NM_001026786.3.

UniGene

Cel.19756.

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KBE	X-ray	1.10	A	24-180	[»]
3KBF	X-ray	1.30	A	24-180	[»]

ProteinModelPortal

P34697.

SMR

P34697. Positions 24-179.

ModBase

Search...

IntAct

P34697. 1 interaction.

PaxDb

P34697.

PRIDE

P34697.

StructuralBiologyKnowledgebase

Search...

EnsemblMetazoa

C15F1.7a; C15F1.7a; C15F1.7.

GeneID

174141.

KEGG

cel:CELE_C15F1.7.

UCSC

C15F1.7a. c. elegans.

CTD

174141.

WormBase

C15F1.7a; CE23550; WBGene00004930; sod-1.
C15F1.7b; CE20508; WBGene00004930; sod-1.

eggNOG

COG2032.

GeneTree

ENSGT00530000063226.

HOGENOM

HOG000263447.

InParanoid

P34697.

K04565.

OMA

HANADDY.

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...

EvolutionaryTrace

P34697.

NextBio

882707.

Entry name

SODC_CAEEL

Accession

Primary (citable) accession number: P34697
Secondary accession number(s): Q5W7E8, Q9N5Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	April 29, 2008
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform a (identifier: P34697-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform b (identifier: P34697-2)

The sequence of this isoform differs from the canonical sequence as follows:
1-22: Missing.