Database: RefSeq
Entry: NP_032995
LinkDB: NP_032995
Original site: NP_032995 
LOCUS       NP_032995                602 aa            linear   ROD 24-FEB-2019
DEFINITION  prostaglandin G/H synthase 1 precursor [Mus musculus].
VERSION     NP_032995.1
DBSOURCE    REFSEQ: accession NM_008969.4
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
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
  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
  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.
            Transcript exon combination :: BC005573.1, AK159907.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
            multifunctional gene product(s) :: PMID: 8121489
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Mus musculus"
                     /map="2 24.19 cM"
     Protein         1..602
                     /product="prostaglandin G/H synthase 1 precursor"
                     /note="prostaglandin G/H synthase 1; PGH synthase 1;
                     cyclooxygenase-1; prostaglandin H2 synthase 1"
     sig_peptide     1..26
                     /experiment="experimental evidence, no additional details
                     /note="propagated from UniProtKB/Swiss-Prot (P22437.1)"
     mat_peptide     27..602
                     /product="Prostaglandin G/H synthase 1"
                     /experiment="experimental evidence, no additional details
                     /note="propagated from UniProtKB/Swiss-Prot (P22437.1)"
     Region          35..72
                     /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"
     Site            70
                     /experiment="experimental evidence, no additional details
                     /note="N-linked (GlcNAc...) asparagine. {ECO:0000255};
                     propagated from UniProtKB/Swiss-Prot (P22437.1)"
     Region          92..578
                     /note="Animal prostaglandin endoperoxide synthase and
                     related bacterial proteins; cd09816"
     Site            106
                     /experiment="experimental evidence, no additional details
                     /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,
                     /note="substrate binding site [chemical binding]"
     Site            order(127,129..131,138..142,144,231,321..325,328..329,332,
                     /note="homodimer interface [polypeptide binding]"
     Site            146
                     /experiment="experimental evidence, no additional details
                     /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,
                     /note="heme binding site [chemical binding]"
     Site            532
                     /experiment="experimental evidence, no additional details
                     /note="Aspirin-acetylated serine; propagated from
                     UniProtKB/Swiss-Prot (P22437.1)"
     CDS             1..602
                     /gene_synonym="Cox-1; Cox-3; COX1; PGHS-1; Pghs1; PHS 1"
        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
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