SOD1 superoxide dismutase 1 [Bos taurus (domestic cattle)] - Gene

Summary

Gene symbol: SOD1
Gene description: superoxide dismutase 1
See related: BGD:BT12476
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Bos taurus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Also known as: SOD1L1
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 1

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2023_09	current	ARS-UCD2.0 (GCF_002263795.3)	1	NC_037328.1 (3824612..3833280, complement)

Chromosome 1 - NC_037328.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_037328.1 Chromosome 1 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

a pi-H pathway assembled across the beta-sheets from both subunits in the SOD-dimer protein connecting the two Cu-centers and thus the two half-reactions, is described.
Title: Pathways of electron transfer and proton translocation in the action of superoxide dismutase dimer.
the present study aims to evaluate the peritoneal fluid impact from infertile women with minimal and mild endometriosis and from fertile control women without endometriosis on SOD1, CAT, GSR gene's expression in experimental bovine oocytes matured in vitro.
Title: Peritoneal fluid of women with endometriosis reduces SOD1 in bovine oocytes in vitro maturation.
Results indicate that variants of the PRLH and SOD1 genes are associated with heat tolerance in Chinese cattle.
Title: PRLH and SOD1 gene variations associated with heat tolerance in Chinese cattle.
The three-dimensional structure of bSOD1 reveals the imidazole ring of His19 localized within 5A from the alpha-carbon of Gly31 providing a structural basis that copper ion, most likely coordinated by His19, catalyzes the specific cleavage reaction
Title: Distinct oxidative cleavage and modification of bovine [Cu- Zn]-SOD by an ascorbic acid/Cu(II) system: Identification of novel copper binding site on SOD molecule.
SOD catalyzes reversal of autoxidation manifesting as its inhibition. SOD saves catechols from autoxidation and extends their bioavailability
Title: New insights of superoxide dismutase inhibition of pyrogallol autoxidation.
antioxidative enzymatic mechanisms in bovine placental tissues are represented by superoxide dismutase 1 and glutathione peroxidase, which show the changes in their expression during improper placental release
Title: The presence of SOD 1 and GSH-Px in bovine retained and properly released foetal membranes.
Results sugget thet Copper/Zinc superoxide dismutase (SOD1) may play a role in controlling intraluteal prostaglandin F2alph and reactive oxygen species action during functional and structural luteolysis.
Title: Roles of prostaglandin F2alpha and hydrogen peroxide in the regulation of Copper/Zinc superoxide dismutase in bovine corpus luteum and luteal endothelial cells.
ALOX5AP, CPNE3, IL1R2, IL6, TLR2, TLR4, and THY1 were upregulated in blood polymorphonuclear cells in negative energy balance versus positive energy balance cows.
Title: Greater expression of TLR2, TLR4, and IL6 due to negative energy balance is associated with lower expression of HLA-DRA and HLA-A in bovine blood neutrophils after intramammary mastitis challenge with Streptococcus uberis.
Acute elevation of SOD may represent a response of luteal endothelial cells to protect themselves against oxidative stress induced by PGF during functional luteolysis.
Title: Role of nitric oxide in the regulation of superoxide dismutase and prostaglandin F(2alpha) production in bovine luteal endothelial cells.
At room temperature (25.0 degrees C) and higher, the addition of high concentrations of polymer is found to significantly enhance the affinity of SOD for catalase.
Title: Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria.

Submit: New GeneRIF Correction See all GeneRIFs (27)

General gene information

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Markers

Sod1 (e-PCR), detects polymorphism
- UniSTS:144477

SOD1L-P (e-PCR)
- UniSTS:253822

SOD1 (e-PCR), detects polymorphism
- UniSTS:264864

RH144700 (e-PCR)
- UniSTS:239035

RH144717 (e-PCR)
- UniSTS:239051

SOD1 (e-PCR), detects polymorphism
- UniSTS:239051

Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables copper ion binding	IEA Inferred from Electronic Annotation more info	PubMed
enables superoxide dismutase activity	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in removal of superoxide radicals	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
located_in cytosol	IEA Inferred from Electronic Annotation more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info	PubMed
located_in peroxisome	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: superoxide dismutase [Cu-Zn]

Names: Cu-Zn superoxide dismutase; superoxide dismutase 1, soluble

NP_777040.1

EC 1.15.1.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_174615.2 → NP_777040.1 superoxide dismutase [Cu-Zn]

See identical proteins and their annotated locations for NP_777040.1

Status: PROVISIONAL

Source sequence(s)

M81129

UniProtKB/Swiss-Prot

P00442, Q3ZCF4

UniProtKB/TrEMBL

F1MNQ4

Conserved Domains (1) summary

cd00305
Location:3 → 145

Cu-Zn_Superoxide_Dismutase; Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the ...