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Q08420 (SODE_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Alternative name(s):
Superoxide dismutase B
Gene names
Name:Sod3
Synonyms:Sod-3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen By similarity.

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

Secreted › extracellular space.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 244229Extracellular superoxide dismutase [Cu-Zn]
PRO_0000032859

Sites

Metal binding1211Copper; catalytic By similarity
Metal binding1231Copper; catalytic By similarity
Metal binding1381Copper; catalytic By similarity
Metal binding1381Zinc; structural By similarity
Metal binding1461Zinc; structural By similarity
Metal binding1491Zinc; structural By similarity
Metal binding1521Zinc; structural By similarity
Metal binding1881Copper; catalytic By similarity

Amino acid modifications

Glycosylation1141N-linked (GlcNAc...) Potential
Disulfide bond70 ↔ 215 By similarity
Disulfide bond132 ↔ 214 By similarity

Experimental info

Mutagenesis481D → V: Homotetramerization.
Sequence conflict235 – 2373RRR → WRW in CAA48177. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q08420 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: B66726301CE5B614

FASTA24426,620
        10         20         30         40         50         60 
MVAFLFCNLL LVACGSVTWT MSDTGESGVD LADRLDLVEK IGDTHSKDLE IWMELGKQRE 

        70         80         90        100        110        120 
ADAREMHAVC RVQPSAMLPP DQPQITGLVL FRQLGPSSRL EASFNLEGFP AEQNTSNHAI 

       130        140        150        160        170        180 
HVHEFGDLSQ GCESTGPHYN PLGVPHPQHP GDFGNFVVRD GRLWKHRMGL ATSLAGPHSI 

       190        200        210        220        230        240 
LGRAVVVHAG EDDLGKGGNQ ASVQNGNAGR RLACCVVGTS NSEAWESQTK ERKKRRRESE 


CKTT

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a rat cDNA clone encoding a secreted superoxide dismutase reveals the epididymis to be a major site of its expression."
Perry A.C.F., Jones R., Hall L.
Biochem. J. 293:21-25(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Epididymis.
[2]"Purification and sequence of rat extracellular superoxide dismutase B secreted by C6 glioma."
Willems J., Zwijsen A., Slegers H., Nicolai S., Bettadapura J., Raymackers J., Scarcez T.
J. Biol. Chem. 268:24614-24621(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]"The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid."
Carlsson L.M., Marklund S.M., Edlund T.
Proc. Natl. Acad. Sci. U.S.A. 93:5219-5222(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS.
Strain: Sprague-Dawley.
Tissue: Uterus.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X68041 mRNA. Translation: CAA48177.1.
Z24721 mRNA. Translation: CAA80849.1.
X94371 mRNA. Translation: CAA64149.1.
BC061861 mRNA. Translation: AAH61861.1.
IPIIPI00200507.
PIRA49097.
RefSeqNP_037012.1. NM_012880.1.
UniGeneRn.10358.

3D structure databases

ProteinModelPortalQ08420.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000005155.

Proteomic databases

PaxDbQ08420.
PRIDEQ08420.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000005155; ENSRNOP00000005155; ENSRNOG00000003869.
GeneID25352.
KEGGrno:25352.

Organism-specific databases

CTD6649.
RGD3733. Sod3.

Phylogenomic databases

eggNOGCOG2032.
GeneTreeENSGT00530000063226.
HOGENOMHOG000263447.
HOVERGENHBG000062.
InParanoidQ08420.
KOK16627.
OMACCVIGIC.
OrthoDBEOG4MCX1S.

Gene expression databases

GenevestigatorQ08420.
GermOnlineENSRNOG00000003869. Rattus norvegicus.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR024141. SOD_Cu/Zn_extracel.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERPTHR10003. PTHR10003. 1 hit.
PTHR10003:SF10. PTHR10003:SF10. 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...

Other

NextBio606301.

Entry information

Entry nameSODE_RAT
AccessionPrimary (citable) accession number: Q08420
Secondary accession number(s): Q64667
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 15, 1999
Last modified: April 3, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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