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P16026 (SODE_SCHMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=EC-SOD
EC=1.15.1.1
OrganismSchistosoma mansoni (Blood fluke)
Taxonomic identifier6183 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length184 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.

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.

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
Glycoprotein
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 – 1818
Chain19 – 184166Extracellular superoxide dismutase [Cu-Zn]
PRO_0000032865

Sites

Metal binding761Copper; catalytic By similarity
Metal binding781Copper; catalytic By similarity
Metal binding931Copper; catalytic By similarity
Metal binding931Zinc; structural By similarity
Metal binding1011Zinc; structural By similarity
Metal binding1101Zinc; structural By similarity
Metal binding1131Zinc; structural By similarity
Metal binding1501Copper; catalytic By similarity

Amino acid modifications

Glycosylation611N-linked (GlcNAc...) Potential
Disulfide bond87 ↔ 176 By similarity

Sequences

Sequence LengthMass (Da)Tools
P16026 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: C14FD37026FA88B3

FASTA18420,346
        10         20         30         40         50         60 
MTVYSYLVIL FILLDNYCSA YGYGYSYYHR RHFDPAIASF TKEPYIGAVW FTQHGDYMYV 

        70         80         90        100        110        120 
NGSVAGLPPG KLLGTHVHRY GGLGNMCLEA GPHFNPFNQR HGPRHGYPRH AGDLGNIRVG 

       130        140        150        160        170        180 
RGGVAKFDFY VTIKGLGPFD GFIGRALVIH ANRDDLGRNR DEGSRTTGNS GPRLACATIG 


FRAP 

« Hide

References

[1]"Schistosoma mansoni: identification and analysis of an mRNA and a gene encoding superoxide dismutase (Cu/Zn)."
Simurda M.C., van Kuelen H., Rekosh D.M., Loverde P.T.
Exp. Parasitol. 67:73-84(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27529 mRNA. Translation: AAA29937.1.
M28545, M28543, M28544 Genomic DNA. Translation: AAA29934.1.
PIRA37019.
RefSeqXP_002580485.1. XM_002580439.1.
UniGeneSma.277.

3D structure databases

ProteinModelPortalP16026.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8341691.
KEGGsmm:Smp_095980.

Organism-specific databases

CTD8341691.

Phylogenomic databases

HOGENOMHOG000263447.
PhylomeDBP16026.

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. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODE_SCHMA
AccessionPrimary (citable) accession number: P16026
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 3, 2013
This is version 87 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