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P41974 (SODE_DIRIM) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Extracellular superoxide dismutase [Cu-Zn]

Short name=EC-SOD
EC=1.15.1.1
OrganismDirofilaria immitis (Canine heartworm)
Taxonomic identifier6287 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeDirofilaria

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems. May act in the parasite defense by neutralizing superoxide generated by activated leukocytes, thus acting as both an antioxidant and an anti-inflammatory factor.

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.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 Potential
Chain39 – 195157Extracellular superoxide dismutase [Cu-Zn]
PRO_0000032862

Sites

Metal binding831Copper; catalytic By similarity
Metal binding851Copper; catalytic By similarity
Metal binding1001Copper; catalytic By similarity
Metal binding1001Zinc; structural By similarity
Metal binding1081Zinc; structural By similarity
Metal binding1171Zinc; structural By similarity
Metal binding1201Zinc; structural By similarity
Metal binding1571Copper; catalytic By similarity

Amino acid modifications

Disulfide bond94 ↔ 186 By similarity

Sequences

Sequence LengthMass (Da)Tools
P41974 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A49FC6605837C44B

FASTA19520,794
        10         20         30         40         50         60 
MMGSFIFLLS IIISINYINS LHTVHRSNIH RNMHNGGMPK KAVAVLKSDT VNGIIYFQQN 

        70         80         90        100        110        120 
NRASATTIYG TINGLTPGLH GFHIHQYGIK ANGCTSAAAH YNPFEKTHGR PTNNIKHIGD 

       130        140        150        160        170        180 
LRNIKAGADG VANVNIISNH IQLSGPLSVI GRSLVVHANP DDLGKGNGDA REESLKTGNA 

       190 
GSRIVCSIIG IAPST 

« Hide

References

[1]James E.R., McLean D.C.
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14994 mRNA. Translation: AAA50247.1.

3D structure databases

ProteinModelPortalP41974.
SMRP41974. Positions 40-192.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERPTHR10003. PTHR10003. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. False negative.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODE_DIRIM
AccessionPrimary (citable) accession number: P41974
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 6, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families