Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Extracellular superoxide dismutase [Cu-Zn]

Gene

SOD3

Organism
Homo sapiens (Human)
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.

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)DescriptionActionsGraphical viewLength
Metal bindingi114Copper; catalytic1
Metal bindingi116Copper; catalytic1
Metal bindingi131Copper; catalytic1
Metal bindingi131Zinc; structural1
Metal bindingi139Zinc; structural1
Metal bindingi142Zinc; structural1
Metal bindingi145Zinc; structural1
Metal bindingi181Copper; catalytic1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Heparin-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS03242-MONOMER.
ZFISH:HS03242-MONOMER.
ReactomeiR-HSA-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
Gene namesi
Name:SOD3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:11181. SOD3.

Subcellular locationi

  • Secretedextracellular space

  • Note: 99% of EC-SOD is anchored to heparan sulfate proteoglycans in the tissue interstitium, and 1% is located in the vasculature in equilibrium between the plasma and the endothelium.

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: Ensembl
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • Golgi lumen Source: Reactome
  • nucleus Source: Ensembl
  • trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi6649.
OpenTargetsiENSG00000109610.
PharmGKBiPA36018.

Chemistry databases

ChEMBLiCHEMBL2069159.

Polymorphism and mutation databases

BioMutaiSOD3.
DMDMi108885292.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000003285519 – 240Extracellular superoxide dismutase [Cu-Zn]Add BLAST222

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi63 ↔ 2081 Publication
Glycosylationi107N-linked (GlcNAc...)2 Publications1
Disulfide bondi125 ↔ 2071 Publication
Glycosylationi229N-linked (Glc) (glycation); in vitro1
Glycosylationi230N-linked (Glc) (glycation); in vitro1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei41Not glycated1
Sitei92Not glycated1
Sitei238Not glycated1

Keywords - PTMi

Disulfide bond, Glycation, Glycoprotein

Proteomic databases

EPDiP08294.
MaxQBiP08294.
PaxDbiP08294.
PeptideAtlasiP08294.
PRIDEiP08294.

PTM databases

iPTMnetiP08294.
PhosphoSitePlusiP08294.

Miscellaneous databases

PMAP-CutDBP08294.

Expressioni

Tissue specificityi

Expressed in blood vessels, heart, lung, kidney and placenta. Major SOD isoenzyme in extracellular fluids such as plasma, lymph and synovial fluid.

Gene expression databases

BgeeiENSG00000109610.
CleanExiHS_SOD3.
ExpressionAtlasiP08294. baseline and differential.
GenevisibleiP08294. HS.

Organism-specific databases

HPAiHPA042110.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SGTAO437653EBI-10195782,EBI-347996

Protein-protein interaction databases

BioGridi112532. 1 interactor.
IntActiP08294. 4 interactors.
STRINGi9606.ENSP00000371554.

Chemistry databases

BindingDBiP08294.

Structurei

Secondary structure

1240
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi59 – 67Combined sources9
Beta strandi79 – 88Combined sources10
Beta strandi93 – 100Combined sources8
Beta strandi104 – 117Combined sources14
Helixi124 – 128Combined sources5
Beta strandi145 – 152Combined sources8
Beta strandi155 – 164Combined sources10
Beta strandi166 – 169Combined sources4
Beta strandi176 – 183Combined sources8
Beta strandi190 – 192Combined sources3
Helixi195 – 198Combined sources4
Beta strandi204 – 209Combined sources6
Helixi216 – 222Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JLPX-ray1.70A/B/C/D19-240[»]
ProteinModelPortaliP08294.
SMRiP08294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08294.

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.
InParanoidiP08294.
KOiK16627.
OMAiHPRHPGD.
OrthoDBiEOG091G13ID.
PhylomeDBiP08294.
TreeFamiTF105133.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
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.

P08294-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLALLCSCLL LAAGASDAWT GEDSAEPNSD SAEWIRDMYA KVTEIWQEVM
60 70 80 90 100
QRRDDDGALH AACQVQPSAT LDAAQPRVTG VVLFRQLAPR AKLDAFFALE
110 120 130 140 150
GFPTEPNSSS RAIHVHQFGD LSQGCESTGP HYNPLAVPHP QHPGDFGNFA
160 170 180 190 200
VRDGSLWRYR AGLAASLAGP HSIVGRAVVV HAGEDDLGRG GNQASVENGN
210 220 230 240
AGRRLACCVV GVCGPGLWER QAREHSERKK RRRESECKAA
Length:240
Mass (Da):25,851
Last modified:May 30, 2006 - v2
Checksum:i585B8DEBFC506CF4
GO

Polymorphismi

The variant Gly-231 which is found in about 2.2% of individual displays a 10-fold increased plasma EC-SOD content due to reduced heparin-binding affinity and thus the impairment of its binding ability to endothelial cell surface.3 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02077658A → T.5 PublicationsCorresponds to variant rs2536512dbSNPEnsembl.1
Natural variantiVAR_02077791A → T.1 PublicationCorresponds to variant rs17879876dbSNPEnsembl.1
Natural variantiVAR_014705231R → G.5 PublicationsCorresponds to variant rs1799895dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02947 mRNA. Translation: AAA66000.1.
U10116 Genomic DNA. Translation: AAA62278.1.
CR541853 mRNA. Translation: CAG46651.1.
AY787834 Genomic DNA. Translation: AAV40827.1.
BC014418 mRNA. Translation: AAH14418.1.
CCDSiCCDS3430.1.
PIRiA28301. DSHUEC.
RefSeqiNP_003093.2. NM_003102.2.
UniGeneiHs.2420.

Genome annotation databases

EnsembliENST00000382120; ENSP00000371554; ENSG00000109610.
GeneIDi6649.
KEGGihsa:6649.
UCSCiuc003gqz.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Superoxide dismutase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02947 mRNA. Translation: AAA66000.1.
U10116 Genomic DNA. Translation: AAA62278.1.
CR541853 mRNA. Translation: CAG46651.1.
AY787834 Genomic DNA. Translation: AAV40827.1.
BC014418 mRNA. Translation: AAH14418.1.
CCDSiCCDS3430.1.
PIRiA28301. DSHUEC.
RefSeqiNP_003093.2. NM_003102.2.
UniGeneiHs.2420.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JLPX-ray1.70A/B/C/D19-240[»]
ProteinModelPortaliP08294.
SMRiP08294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112532. 1 interactor.
IntActiP08294. 4 interactors.
STRINGi9606.ENSP00000371554.

Chemistry databases

BindingDBiP08294.
ChEMBLiCHEMBL2069159.

PTM databases

iPTMnetiP08294.
PhosphoSitePlusiP08294.

Polymorphism and mutation databases

BioMutaiSOD3.
DMDMi108885292.

Proteomic databases

EPDiP08294.
MaxQBiP08294.
PaxDbiP08294.
PeptideAtlasiP08294.
PRIDEiP08294.

Protocols and materials databases

DNASUi6649.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382120; ENSP00000371554; ENSG00000109610.
GeneIDi6649.
KEGGihsa:6649.
UCSCiuc003gqz.4. human.

Organism-specific databases

CTDi6649.
DisGeNETi6649.
GeneCardsiSOD3.
HGNCiHGNC:11181. SOD3.
HPAiHPA042110.
MIMi185490. gene.
neXtProtiNX_P08294.
OpenTargetsiENSG00000109610.
PharmGKBiPA36018.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP08294.
KOiK16627.
OMAiHPRHPGD.
OrthoDBiEOG091G13ID.
PhylomeDBiP08294.
TreeFamiTF105133.

Enzyme and pathway databases

BioCyciMetaCyc:HS03242-MONOMER.
ZFISH:HS03242-MONOMER.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

EvolutionaryTraceiP08294.
GeneWikiiSOD3.
GenomeRNAii6649.
PMAP-CutDBP08294.
PROiP08294.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000109610.
CleanExiHS_SOD3.
ExpressionAtlasiP08294. baseline and differential.
GenevisibleiP08294. HS.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
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...

Entry informationi

Entry nameiSODE_HUMAN
AccessioniPrimary (citable) accession number: P08294
Secondary accession number(s): Q5U781, Q6FHA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 30, 2006
Last modified: November 30, 2016
This is version 183 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.