LOCUS NP_032995 602 aa linear ROD 24-FEB-2019
DEFINITION prostaglandin G/H synthase 1 precursor [Mus musculus].
ACCESSION NP_032995
VERSION NP_032995.1
DBSOURCE REFSEQ: accession NM_008969.4
KEYWORDS RefSeq.
SOURCE Mus musculus (house mouse)
ORGANISM Mus musculus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE 1 (residues 1 to 602)
AUTHORS Theisen E, McDougal CE, Nakanishi M, Stevenson DM, Amador-Noguez D,
Rosenberg DW, Knoll LJ and Sauer JD.
TITLE Cyclooxygenase-1 and -2 Play Contrasting Roles in
Listeria-Stimulated Immunity
JOURNAL J. Immunol. 200 (11), 3729-3738 (2018)
PUBMED 29678951
REFERENCE 2 (residues 1 to 602)
AUTHORS Hilander T, Zhou XL, Konovalova S, Zhang FP, Euro L, Chilov D,
Poutanen M, Chihade J, Wang ED and Tyynismaa H.
TITLE Editing activity for eliminating mischarged tRNAs is essential in
mammalian mitochondria
JOURNAL Nucleic Acids Res. 46 (2), 849-860 (2018)
PUBMED 29228266
REFERENCE 3 (residues 1 to 602)
AUTHORS Herington JL, O'Brien C, Robuck MF, Lei W, Brown N, Slaughter JC,
Paria BC, Mahadevan-Jansen A and Reese J.
TITLE Prostaglandin-Endoperoxide Synthase 1 Mediates the Timing of
Parturition in Mice Despite Unhindered Uterine Contractility
JOURNAL Endocrinology 159 (1), 490-505 (2018)
PUBMED 29029054
REMARK GeneRIF: Data (including data from studies in knockout mice)
suggest that delayed parturition in Cox-1 knockout mice is result
of impaired luteolysis and cervical dilation, despite the presence
of strong uterine contractions.
REFERENCE 4 (residues 1 to 602)
AUTHORS Li X, Mazaleuskaya LL, Yuan C, Ballantyne LL, Meng H, Smith WL,
FitzGerald GA and Funk CD.
TITLE Flipping the cyclooxygenase (Ptgs) genes reveals isoform-specific
compensatory functions
JOURNAL J. Lipid Res. 59 (1), 89-101 (2018)
PUBMED 29180445
REMARK Erratum:[J Lipid Res. 2018 Oct;59(10):2035. PMID: 30275118]
REFERENCE 5 (residues 1 to 602)
AUTHORS Newson J, Motwani MP, Kendall AC, Nicolaou A, Muccioli GG,
Alhouayek M, Bennett M, Van De Merwe R, James S, De Maeyer RPH and
Gilroy DW.
TITLE Inflammatory Resolution Triggers a Prolonged Phase of Immune
Suppression through COX-1/mPGES-1-Derived Prostaglandin E2
JOURNAL Cell Rep 20 (13), 3162-3175 (2017)
PUBMED 28954232
REMARK GeneRIF: IFNgamma upregulated microsomal prostaglandin E synthase-1
(mPGES-1) alongside cyclo-oxygenase (COX-1) within macrophage
populations, resulting in sustained prostaglandin (PG)E2
biosynthesis.
REFERENCE 6 (residues 1 to 602)
AUTHORS Picot D, Loll PJ and Garavito RM.
TITLE The X-ray crystal structure of the membrane protein prostaglandin
H2 synthase-1
JOURNAL Nature 367 (6460), 243-249 (1994)
PUBMED 8121489
REMARK GeneRIF: Prostaglandin G/H synthase is a moonlighting protein that
functions both as a peroxidase as well as a cyclooxygenase.
REFERENCE 7 (residues 1 to 602)
AUTHORS Kraemer SA, Meade EA and DeWitt DL.
TITLE Prostaglandin endoperoxide synthase gene structure: identification
of the transcriptional start site and 5'-flanking regulatory
sequences
JOURNAL Arch. Biochem. Biophys. 293 (2), 391-400 (1992)
PUBMED 1536575
REFERENCE 8 (residues 1 to 602)
AUTHORS Kujubu DA, Fletcher BS, Varnum BC, Lim RW and Herschman HR.
TITLE TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3
cells, encodes a novel prostaglandin synthase/cyclooxygenase
homologue
JOURNAL J. Biol. Chem. 266 (20), 12866-12872 (1991)
PUBMED 1712772
REFERENCE 9 (residues 1 to 602)
AUTHORS Marshburn PB, Shabanowitz RB and Clark MR.
TITLE Immunohistochemical localization of prostaglandin H synthase in the
embryo and uterus of the mouse from ovulation through implantation
JOURNAL Mol. Reprod. Dev. 25 (4), 309-316 (1990)
PUBMED 2109618
REFERENCE 10 (residues 1 to 602)
AUTHORS DeWitt DL, el-Harith EA, Kraemer SA, Andrews MJ, Yao EF, Armstrong
RL and Smith WL.
TITLE The aspirin and heme-binding sites of ovine and murine
prostaglandin endoperoxide synthases
JOURNAL J. Biol. Chem. 265 (9), 5192-5198 (1990)
PUBMED 2108169
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AK159907.1 and AW493573.1.
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].
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: BC005573.1, AK159907.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMN00849374, SAMN00849375
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
multifunctional gene product(s) :: PMID: 8121489
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..602
/organism="Mus musculus"
/strain="C57BL/6"
/db_xref="taxon:10090"
/chromosome="2"
/map="2 24.19 cM"
Protein 1..602
/product="prostaglandin G/H synthase 1 precursor"
/EC_number="1.14.99.1"
/note="prostaglandin G/H synthase 1; PGH synthase 1;
cyclooxygenase-1; prostaglandin H2 synthase 1"
/calculated_mol_wt=66084
sig_peptide 1..26
/experiment="experimental evidence, no additional details
recorded"
/note="propagated from UniProtKB/Swiss-Prot (P22437.1)"
/calculated_mol_wt=2977
mat_peptide 27..602
/product="Prostaglandin G/H synthase 1"
/experiment="experimental evidence, no additional details
recorded"
/note="propagated from UniProtKB/Swiss-Prot (P22437.1)"
/calculated_mol_wt=66084
Region 35..72
/region_name="EGF_CA"
/note="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...; cd00054"
/db_xref="CDD:238011"
Site 70
/site_type="glycosylation"
/experiment="experimental evidence, no additional details
recorded"
/note="N-linked (GlcNAc...) asparagine. {ECO:0000255};
propagated from UniProtKB/Swiss-Prot (P22437.1)"
Region 92..578
/region_name="prostaglandin_endoperoxide_synthase"
/note="Animal prostaglandin endoperoxide synthase and
related bacterial proteins; cd09816"
/db_xref="CDD:188648"
Site 106
/site_type="glycosylation"
/experiment="experimental evidence, no additional details
recorded"
/note="N-linked (GlcNAc...) asparagine. {ECO:0000255};
propagated from UniProtKB/Swiss-Prot (P22437.1)"
Site order(119,207,347,350..351,355,357,383,387,389,520,524,
528..529,532..533,536)
/site_type="other"
/note="substrate binding site [chemical binding]"
/db_xref="CDD:188648"
Site order(127,129..131,138..142,144,231,321..325,328..329,332,
335..336,339,369..376,539..540,543..547,549..551,553..554)
/site_type="other"
/note="homodimer interface [polypeptide binding]"
/db_xref="CDD:188648"
Site 146
/site_type="glycosylation"
/experiment="experimental evidence, no additional details
recorded"
/note="N-linked (GlcNAc...) asparagine. {ECO:0000255};
propagated from UniProtKB/Swiss-Prot (P22437.1)"
Site order(150,201,205,209,212..214,297,384,387..390,393,410,
446,448..449,452)
/site_type="other"
/note="heme binding site [chemical binding]"
/db_xref="CDD:188648"
Site 532
/site_type="other"
/experiment="experimental evidence, no additional details
recorded"
/note="Aspirin-acetylated serine; propagated from
UniProtKB/Swiss-Prot (P22437.1)"
CDS 1..602
/gene="Ptgs1"
/gene_synonym="Cox-1; Cox-3; COX1; PGHS-1; Pghs1; PHS 1"
/coded_by="NM_008969.4:138..1946"
/db_xref="CCDS:CCDS15970.1"
/db_xref="GeneID:19224"
/db_xref="MGI:MGI:97797"
ORIGIN
1 msrrslslwf plllllllpp tpsvlladpg vpspvnpccy ypcqnqgvcv rfgldnyqcd
61 ctrtgysgpn ctipeiwtwl rnslrpspsf thfllthgyw lwefvnatfi revlmrlvlt
121 vrsnlipspp tynsahdyis wesfsnvsyy trilpsvpkd cptpmgtkgk kqlpdvqlla
181 qqlllrrefi papqgtnilf affaqhfthq ffktsgkmgp gftkalghgv dlghiygdnl
241 erqyhlrlfk dgklkyqvld gevyppsveq asvlmryppg vpperqmavg qevfgllpgl
301 mlfstiwlre hnrvcdllke ehptwddeql fqttrlilig etikivieey vqhlsgyflq
361 lkfdpellfr aqfqyrnria mefnhlyhwh plmpnsfqvg sqeysyeqfl fntsmlvdyg
421 vealvdafsr qragrigggr nfdyhvlhva vdvikesrem rlqpfneyrk rfglkpytsf
481 qeltgekema aeleelygdi dalefypgll lekcqpnsif gesmiemgap fslkgllgnp
541 icspeywkps tfggdvgfnl vntaslkklv clntktcpyv sfrvpdypgd dgsvlvrrst
601 el
//
