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Protein

Extracellular superoxide dismutase [Cu-Zn]

Gene

Sod3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi121 – 1211Copper; catalyticBy similarity
Metal bindingi123 – 1231Copper; catalyticBy similarity
Metal bindingi138 – 1381Copper; catalyticBy similarity
Metal bindingi138 – 1381Zinc; structuralBy similarity
Metal bindingi146 – 1461Zinc; structuralBy similarity
Metal bindingi149 – 1491Zinc; structuralBy similarity
Metal bindingi152 – 1521Zinc; structuralBy similarity
Metal bindingi188 – 1881Copper; catalyticBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • superoxide dismutase activity Source: RGD

GO - Biological processi

  • response to copper ion Source: RGD
  • response to hypoxia Source: Ensembl
  • response to oxidative stress Source: RGD
  • response to superoxide Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Short name:
EC-SOD
Alternative name(s):
Superoxide dismutase B
Gene namesi
Name:Sod3
Synonyms:Sod-3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi3733. Sod3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular matrix Source: RGD
  • extracellular space Source: RGD
  • nucleus Source: RGD
  • trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481D → V: Homotetramerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence analysisAdd
BLAST
Chaini16 – 244229Extracellular superoxide dismutase [Cu-Zn]PRO_0000032859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi70 ↔ 215By similarity
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence analysis
Disulfide bondi132 ↔ 214By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ08420.
PRIDEiQ08420.

Expressioni

Gene expression databases

GenevisibleiQ08420. RN.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005155.

Structurei

3D structure databases

ProteinModelPortaliQ08420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiQ08420.
KOiK16627.
OMAiHPRHPGD.
OrthoDBiEOG77HDHG.
PhylomeDBiQ08420.
TreeFamiTF105133.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08420-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAFLFCNLL LVACGSVTWT MSDTGESGVD LADRLDLVEK IGDTHSKDLE
60 70 80 90 100
IWMELGKQRE ADAREMHAVC RVQPSAMLPP DQPQITGLVL FRQLGPSSRL
110 120 130 140 150
EASFNLEGFP AEQNTSNHAI HVHEFGDLSQ GCESTGPHYN PLGVPHPQHP
160 170 180 190 200
GDFGNFVVRD GRLWKHRMGL ATSLAGPHSI LGRAVVVHAG EDDLGKGGNQ
210 220 230 240
ASVQNGNAGR RLACCVVGTS NSEAWESQTK ERKKRRRESE CKTT
Length:244
Mass (Da):26,620
Last modified:July 15, 1999 - v2
Checksum:iB66726301CE5B614
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2373RRR → WRW in CAA48177 (PubMed:8328962).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68041 mRNA. Translation: CAA48177.1.
Z24721 mRNA. Translation: CAA80849.1.
X94371 mRNA. Translation: CAA64149.1.
BC061861 mRNA. Translation: AAH61861.1.
PIRiA49097.
RefSeqiNP_037012.1. NM_012880.1.
UniGeneiRn.10358.

Genome annotation databases

EnsembliENSRNOT00000005155; ENSRNOP00000005155; ENSRNOG00000003869.
GeneIDi25352.
KEGGirno:25352.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68041 mRNA. Translation: CAA48177.1.
Z24721 mRNA. Translation: CAA80849.1.
X94371 mRNA. Translation: CAA64149.1.
BC061861 mRNA. Translation: AAH61861.1.
PIRiA49097.
RefSeqiNP_037012.1. NM_012880.1.
UniGeneiRn.10358.

3D structure databases

ProteinModelPortaliQ08420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005155.

Proteomic databases

PaxDbiQ08420.
PRIDEiQ08420.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005155; ENSRNOP00000005155; ENSRNOG00000003869.
GeneIDi25352.
KEGGirno:25352.

Organism-specific databases

CTDi6649.
RGDi3733. Sod3.

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiQ08420.
KOiK16627.
OMAiHPRHPGD.
OrthoDBiEOG77HDHG.
PhylomeDBiQ08420.
TreeFamiTF105133.

Enzyme and pathway databases

ReactomeiR-RNO-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

PROiQ08420.

Gene expression databases

GenevisibleiQ08420. RN.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiSODE_RAT
AccessioniPrimary (citable) accession number: Q08420
Secondary accession number(s): Q64667
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 15, 1999
Last modified: June 8, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.