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P41975 (SODE_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 90. 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
Gene names
Name:SOD3
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

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

Homotetramer By similarity.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 244226Extracellular superoxide dismutase [Cu-Zn]
PRO_0000032858

Sites

Metal binding1181Copper; catalytic By similarity
Metal binding1201Copper; catalytic By similarity
Metal binding1351Copper; catalytic By similarity
Metal binding1351Zinc; structural By similarity
Metal binding1431Zinc; structural By similarity
Metal binding1461Zinc; structural By similarity
Metal binding1491Zinc; structural By similarity
Metal binding1851Copper; catalytic By similarity

Amino acid modifications

Glycosylation1111N-linked (GlcNAc...) Potential
Disulfide bond67 ↔ 212 By similarity
Disulfide bond129 ↔ 211 By similarity

Experimental info

Sequence conflict531R → W in CAA55018. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P41975 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 7C9B1C59F942F2C5

FASTA24425,688
        10         20         30         40         50         60 
MLALVCSCLL LAALPADTWS GPAAVELGSD TVEQIRDTHA KVTEIWQALT QQRAAQGEPA 

        70         80         90        100        110        120 
GALHAVCRVQ PSATLDAAQP RVSGLVVFRQ LGPGAQLEAF FDLEGFPVEA NLSSRAIHVH 

       130        140        150        160        170        180 
QFGDLSQGCD STGAHYNPLA VQHPQHPGDF GNFAVRDGRL WKYRSGLAAS LAGPHSIVGR 

       190        200        210        220        230        240 
AVVVHAGEDD LGRGGNAASV ENGNAGPRLA CCVVGASGPA PWARQAQEHA ERKKRRRESE 


CKAA 

« Hide

References

[1]Laukkanen M.O., Aittomaki S.J., Hiltunen T.P., Yla-Herttuala S.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: New Zealand white.
[2]Laukkanen M.O., Hiltunen M.O., Aittomaki S., Janne J., Yla-Herttuala S.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: New Zealand white.
Tissue: Heart.
[3]"Cloning and characterization of rabbit extracellular superoxide dismutase."
Laukkanen M.O., Aittomaeki S., Mannermaa S., Hiltunen M.O., Yla-Herttuala S.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[4]Hiltunen T.P., Nikkari T., Yla-Herttuala S.
Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 43-155.
Strain: New Zealand white.
Tissue: Aorta.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z67878 mRNA. Translation: CAA91785.1.
Y13339 Genomic DNA. Translation: CAA73783.1.
AJ007044 Genomic DNA. Translation: CAA07431.1.
X78139 mRNA. Translation: CAA55018.1.
RefSeqNP_001076101.1. NM_001082632.1.
UniGeneOcu.3290.

3D structure databases

ProteinModelPortalP41975.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000006450.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000007456; ENSOCUP00000006450; ENSOCUG00000007460.
GeneID100009320.

Organism-specific databases

CTD6649.

Phylogenomic databases

eggNOGCOG2032.
GeneTreeENSGT00530000063226.
HOGENOMHOG000263447.
HOVERGENHBG000062.
OMACCVIGIC.
OrthoDBEOG4MCX1S.

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...

Entry information

Entry nameSODE_RABIT
AccessionPrimary (citable) accession number: P41975
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 90 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