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SOD3

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
SOD3
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

2JLP

Identifiers
AliasesSOD3, EC-SOD, superoxide dismutase 3, extracellular, superoxide dismutase 3
External IDsOMIM:185490;MGI:103181;HomoloGene:2334;GeneCards:SOD3;OMA:SOD3 - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for SOD3
Genomic location for SOD3
Band4p15.2Start24,789,912bp[1]
End24,800,842bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for SOD3
Genomic location for SOD3
Band5 C1|5 27.92 cMStart52,521,133bp[2]
End52,528,760bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Descending thoracic aorta

  • right uterine tube

  • ascending aorta

  • right coronary artery

  • popliteal artery

  • tibial arteries

  • left coronary artery

  • gastric mucosa

  • canal of the cervix

  • right lung
Top expressed in
  • choroid plexus of fourth ventricle

  • ascending aorta

  • right kidney

  • aortic valve

  • lactiferous gland

  • human kidney

  • right lung

  • brown adipose tissue

  • adrenal gland

  • ankle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6649

20657

Ensembl

ENSG00000109610

ENSMUSG00000072941

UniProt

P08294

O09164

RefSeq (mRNA)

NM_003102

NM_011435

RefSeq (protein)

NP_003093

NP_035565

Location (UCSC)Chr 4: 24.79 – 24.8 MbChr 5: 52.52 – 52.53 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Extracellular superoxide dismutase [Cu-Zn] is anenzyme that inhumans is encoded by theSOD3gene.

This gene encodes a member of thesuperoxide dismutase (SOD) protein family. SODs areantioxidantenzymes thatcatalyze thedismutation of twosuperoxide radicals intohydrogen peroxide andoxygen. The product of this gene is thought to protect thebrain,lungs, and other tissues fromoxidative stress. The protein is secreted into theextracellular space and forms aglycosylatedhomotetramer that is anchored to theextracellular matrix (ECM) and cell surfaces through an interaction withheparan sulfateproteoglycan andcollagen. A fraction of the protein is cleaved near theC-terminus before secretion to generate circulating tetramers that do not interact with the ECM.[5]

Amongblack garden ants (Lasius niger), the lifespan ofqueens is an order of magnitude greater than that of workers despite no systematic nucleotide sequence difference between them.[6] TheSOD3 gene was found to be the most differentially over-expressed gene in the brains of queen vs worker ants. This finding raises the possibility that SOD3 antioxidant activity plays a key role in the striking longevity of social insect queens.[6]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000109610Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000072941Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^"Entrez Gene: SOD3 superoxide dismutase 3, extracellular".
  6. ^abLucas ER, Keller L. Elevated expression of ageing and immunity genes in queens of the black garden ant. Exp Gerontol. 2018 Jul 15;108:92-98. doi: 10.1016/j.exger.2018.03.020. Epub 2018 Apr 3. PMID: 29625209

Further reading

[edit]
Otheroxidoreductases (EC 1.15–1.21)
1.15: Acting onsuperoxide as acceptor
1.16: Oxidizingmetal ions
1.17: Acting on CH or CH2 groups
1.18: Acting oniron–sulfur proteins as donors
1.19: Acting on reducedflavodoxin as donor
1.20: Acting onphosphorus orarsenic in donors
1.21: Acting on X-H and Y-H to form an X-Y bond
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