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P08294

- SODE_HUMAN

UniProt

P08294 - SODE_HUMAN

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Protein

Extracellular superoxide dismutase [Cu-Zn]

Gene
SOD3
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 copper ion per subunit By similarity.
Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei41 – 411Not glycated
Sitei92 – 921Not glycated
Metal bindingi114 – 1141Copper; catalytic
Metal bindingi116 – 1161Copper; catalytic
Metal bindingi131 – 1311Copper; catalytic
Metal bindingi131 – 1311Zinc; structural
Metal bindingi139 – 1391Zinc; structural
Metal bindingi142 – 1421Zinc; structural
Metal bindingi145 – 1451Zinc; structural
Metal bindingi181 – 1811Copper; catalytic
Sitei238 – 2381Not glycated

GO - Molecular functioni

  1. copper ion binding Source: RefGenome
  2. heparin binding Source: UniProtKB-KW
  3. protein binding Source: BHF-UCL
  4. superoxide dismutase activity Source: RefGenome
  5. zinc ion binding Source: RefGenome

GO - Biological processi

  1. removal of superoxide radicals Source: RefGenome
  2. response to copper ion Source: Ensembl
  3. response to hypoxia Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Heparin-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_172715. 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
ProteomesiUP000005640: 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

  1. cytoplasm Source: RefGenome
  2. extracellular matrix Source: Ensembl
  3. extracellular region Source: Reactome
  4. extracellular space Source: BHF-UCL
  5. extracellular vesicular exosome Source: UniProt
  6. Golgi lumen Source: Reactome
  7. nucleus Source: Ensembl
  8. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36018.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 240222Extracellular superoxide dismutase [Cu-Zn]PRO_0000032855Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi63 ↔ 2081 Publication
Glycosylationi107 – 1071N-linked (GlcNAc...)2 Publications
Disulfide bondi125 ↔ 2071 Publication
Glycosylationi229 – 2291N-linked (Glc) (glycation); in vitro1 Publication
Glycosylationi230 – 2301N-linked (Glc) (glycation); in vitro1 Publication

Keywords - PTMi

Disulfide bond, Glycation, Glycoprotein

Proteomic databases

MaxQBiP08294.
PaxDbiP08294.
PeptideAtlasiP08294.
PRIDEiP08294.

PTM databases

PhosphoSiteiP08294.

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

ArrayExpressiP08294.
BgeeiP08294.
CleanExiHS_SOD3.
GenevestigatoriP08294.

Organism-specific databases

HPAiCAB008671.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000371554.

Structurei

Secondary structure

1
240
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi59 – 679
Beta strandi79 – 8810
Beta strandi93 – 1008
Beta strandi104 – 11714
Helixi124 – 1285
Beta strandi145 – 1528
Beta strandi155 – 16410
Beta strandi166 – 1694
Beta strandi176 – 1838
Beta strandi190 – 1923
Helixi195 – 1984
Beta strandi204 – 2096
Helixi216 – 2227

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JLPX-ray1.70A/B/C/D19-240[»]
ProteinModelPortaliP08294.
SMRiP08294. Positions 55-223.

Miscellaneous databases

EvolutionaryTraceiP08294.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2032.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP08294.
KOiK16627.
OMAiHPRHPGD.
PhylomeDBiP08294.
TreeFamiTF105133.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR024141. SOD_Cu/Zn_extracel.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003:SF36. PTHR10003:SF36. 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

MLALLCSCLL LAAGASDAWT GEDSAEPNSD SAEWIRDMYA KVTEIWQEVM    50
QRRDDDGALH AACQVQPSAT LDAAQPRVTG VVLFRQLAPR AKLDAFFALE 100
GFPTEPNSSS RAIHVHQFGD LSQGCESTGP HYNPLAVPHP QHPGDFGNFA 150
VRDGSLWRYR AGLAASLAGP HSIVGRAVVV HAGEDDLGRG GNQASVENGN 200
AGRRLACCVV GVCGPGLWER QAREHSERKK RRRESECKAA 240
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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581A → T.5 Publications
Corresponds to variant rs2536512 [ dbSNP | Ensembl ].
VAR_020776
Natural varianti91 – 911A → T.1 Publication
Corresponds to variant rs17879876 [ dbSNP | Ensembl ].
VAR_020777
Natural varianti231 – 2311R → G.5 Publications
Corresponds to variant rs1799895 [ dbSNP | Ensembl ].
VAR_014705

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi108885292.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Superoxide dismutase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3430.1.
PIRi A28301. DSHUEC.
RefSeqi NP_003093.2. NM_003102.2.
UniGenei Hs.2420.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JLP X-ray 1.70 A/B/C/D 19-240 [» ]
ProteinModelPortali P08294.
SMRi P08294. Positions 55-223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000371554.

Chemistry

ChEMBLi CHEMBL2069159.

PTM databases

PhosphoSitei P08294.

Polymorphism databases

DMDMi 108885292.

Proteomic databases

MaxQBi P08294.
PaxDbi P08294.
PeptideAtlasi P08294.
PRIDEi P08294.

Protocols and materials databases

DNASUi 6649.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000382120 ; ENSP00000371554 ; ENSG00000109610 .
GeneIDi 6649.
KEGGi hsa:6649.
UCSCi uc003gqz.3. human.

Organism-specific databases

CTDi 6649.
GeneCardsi GC04P024798.
HGNCi HGNC:11181. SOD3.
HPAi CAB008671.
MIMi 185490. gene.
neXtProti NX_P08294.
PharmGKBi PA36018.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2032.
HOGENOMi HOG000263447.
HOVERGENi HBG000062.
InParanoidi P08294.
KOi K16627.
OMAi HPRHPGD.
PhylomeDBi P08294.
TreeFami TF105133.

Enzyme and pathway databases

Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSi SOD3. human.
EvolutionaryTracei P08294.
GeneWikii SOD3.
GenomeRNAii 6649.
NextBioi 25915.
PMAP-CutDB P08294.
PROi P08294.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08294.
Bgeei P08294.
CleanExi HS_SOD3.
Genevestigatori P08294.

Family and domain databases

Gene3Di 2.60.40.200. 1 hit.
InterProi IPR018152. SOD_Cu/Zn_BS.
IPR024141. SOD_Cu/Zn_extracel.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view ]
PANTHERi PTHR10003:SF36. PTHR10003:SF36. 1 hit.
Pfami PF00080. Sod_Cu. 1 hit.
[Graphical view ]
PRINTSi PR00068. CUZNDISMTASE.
SUPFAMi SSF49329. SSF49329. 1 hit.
PROSITEi PS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase."
    Hjalmarsson K., Marklund S.L., Engstroem A., Edlund T.
    Proc. Natl. Acad. Sci. U.S.A. 84:6340-6344(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT THR-58.
  2. "Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene."
    Folz R.J., Crapo J.D.
    Genomics 22:162-171(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-58.
    Tissue: Blood.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-58.
  4. NIEHS SNPs program
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-58; THR-91 AND GLY-231.
  5. "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], VARIANT THR-58.
    Tissue: Colon.
  6. "The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro."
    Adachi T., Ohta H., Hayashi K., Hirano K., Marklund S.L.
    Free Radic. Biol. Med. 13:205-210(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCATION AT LYS-229 AND LYS-230.
  7. Cited for: REVIEW.
  8. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
    Tissue: Plasma.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
    Tissue: Liver.
  10. "The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding."
    Antonyuk S.V., Strange R.W., Marklund S.L., Hasnain S.S.
    J. Mol. Biol. 388:310-326(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-240, SUBUNIT, METAL-BINDING SITES, DISULFIDE BONDS.
  11. "10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain."
    Sandstrom J., Nilsson P., Karlsson K., Marklund S.L.
    J. Biol. Chem. 269:19163-19166(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLY-231.
  12. "Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum."
    Yamada H., Yamada Y., Adachi T., Goto H., Ogasawara N., Futenma A., Kitano M., Hirano K., Kato K.
    Jpn. J. Hum. Genet. 40:177-184(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLY-231.
  13. "Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface."
    Adachi T., Yamada H., Yamada Y., Morihara N., Yamazaki N., Murakami T., Futenma A., Kato K., Hirano K.
    Biochem. J. 313:235-239(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLY-231.
  14. "An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases."
    Adachi T., Morihara N., Yamazaki N., Yamada H., Futenma A., Kato K., Hirano K.
    J. Biochem. 120:184-188(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLY-231.

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: September 3, 2014
This is version 160 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

External Data

Dasty 3

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