PTGS1 prostaglandin-endoperoxide synthase 1 [Ovis aries (sheep)] - Gene

Summary

Gene symbol: PTGS1
Gene description: prostaglandin-endoperoxide synthase 1
See related: EnsemblRapid:ENSOARG00020013914
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Ovis aries
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Caprinae; Ovis
Also known as: COX1; COX-1; PGHS-1
Summary: This is one of two genes encoding similar enzymes that catalyze the conversion of arachinodate to prostaglandin. The encoded protein regulates angiogenesis in endothelial cells, and is inhibited by nonsteroidal anti-inflammatory drugs such as aspirin. Based on its ability to function as both a cyclooxygenase and as a peroxidase, the encoded protein has been identified as a moonlighting protein. [provided by RefSeq, Jan 2014]
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 3

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	ARS-UI_Ramb_v3.0 (GCF_016772045.2)	3	NC_056056.1 (13515914..13540542, complement)

Chromosome 3 - NC_056056.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_056056.1 Chromosome 3 Reference ARS-UI_Ramb_v3.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

mechanisms for the PGHS/AA/GSH-dependent formation of MDA, 15(S)-8-iso-prostaglandin F(2alpha) and other F(2)-isoprostanes
Title: Glutathione promotes prostaglandin H synthase (cyclooxygenase)-dependent formation of malondialdehyde and 15(S)-8-iso-prostaglandin F2α.
The study compares crystal strucrures of COX1 in the presence and absence of different nonsteroidal antiinflammatory drugs and COX-2 inhibitors.
Title: Comparison of cyclooxygenase-1 crystal structures: cross-talk between monomers comprising cyclooxygenase-1 homodimers.
regulation of expression of these enzymes is region-specific, suggesting that the activity of PGHS-1 & PGHS-2 is likely to be critical for brain development in the late-gestation ovine fetus.
Title: Development of prostaglandin endoperoxide synthase expression in the ovine fetal central nervous system and pituitary.
N-(3-hydroxyphenyl)arachidonoylamide is a substrate but not a inhibitor of PGHS-1.
Title: Characterization of an AM404 analogue, N-(3-hydroxyphenyl)arachidonoylamide, as a substrate and inactivator of prostaglandin endoperoxide synthase.
oxygenase reaction occurs by a sequential mechanism which most likely involves reversible abstraction of a hydrogen atom from the fatty acid prior to the trapping of the delocalized substrate radical by O2.
Title: Molecular oxygen dependent steps in fatty acid oxidation by cyclooxygenase-1.

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General gene information

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Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables heme binding	IEA Inferred from Electronic Annotation more info	PubMed
enables oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen	IEA Inferred from Electronic Annotation more info	PubMed
enables peroxidase activity	IEA Inferred from Electronic Annotation more info	PubMed
enables prostaglandin-endoperoxide synthase activity	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in cyclooxygenase pathway	IEA Inferred from Electronic Annotation more info	PubMed
involved_in response to oxidative stress	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info	PubMed
located_in neuron projection	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: prostaglandin G/H synthase 1

Names: PGH synthase 1; PHS 1; cyclooxygenase-1; prostaglandin H2 synthase 1; prostaglandin endoperoxide synthase

NP_001009476.1

EC 1.14.99.1

XP_042101169.1

EC 1.14.99.1

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_001009476.1 → NP_001009476.1 prostaglandin G/H synthase 1 precursor

See identical proteins and their annotated locations for NP_001009476.1

Status: PROVISIONAL

Source sequence(s)

Y00750

UniProtKB/Swiss-Prot

P05979

UniProtKB/TrEMBL

A0A836A6F1

Related

ENSOARP00020017545.2, ENSOART00020021205.2

Conserved Domains (2) summary

cd09816
Location:90 → 576

prostaglandin_endoperoxide_synthase; Animal prostaglandin endoperoxide synthase and related bacterial proteins

cd00054
Location:33 → 70

EGF_CA; Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the ...

RefSeqs of Annotated Genomes: GCF_016772045.2-RS_2023_10

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ARS-UI_Ramb_v3.0 Primary Assembly

Genomic

NC_056056.1 Reference ARS-UI_Ramb_v3.0 Primary Assembly

Range

13515914..13540542 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_042245235.2 → XP_042101169.1 prostaglandin G/H synthase 1 isoform X1

UniProtKB/TrEMBL

A0A836A6F1

Related

ENSOARP00020054412.1, ENSOART00020079642.1

Conserved Domains (2) summary

cd09816
Location:90 → 528

prostaglandin_endoperoxide_synthase; Animal prostaglandin endoperoxide synthase and related bacterial proteins

cd00054
Location:33 → 70

EGF_CA; Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the ...