LOCUS NP_032995 602 aa linear ROD 04-MAR-2025
DEFINITION prostaglandin G/H synthase 1 precursor [Mus musculus].
ACCESSION NP_032995
VERSION NP_032995.1
DBSOURCE REFSEQ: accession NM_008969.4
KEYWORDS RefSeq; RefSeq Select.
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 Aikawa,S., Matsuo,M., Akaeda,S., Sugimoto,Y., Arita,M., Isobe,Y.,
Sugiura,Y., Taira,S., Maeda,R., Shimizu-Hirota,R., Takeda,N.,
Hiratsuka,D., He,X., Ishizawa,C., Iida,R., Fukui,Y., Hiraoka,T.,
Harada,M., Wada-Hiraike,O., Osuga,Y. and Hirota,Y.
TITLE Spatiotemporally distinct roles of cyclooxygenase-1 and
cyclooxygenase-2 at fetomaternal interface in mice
JOURNAL JCI Insight 9 (19), e181865 (2024)
PUBMED 39377223
REMARK Publication Status: Online-Only
REFERENCE 2 (residues 1 to 602)
AUTHORS Abou Nader,N., Charrier,L., Meisnsohn,M.C., Banville,L.,
Deffrennes,B., St-Jean,G., Boerboom,D., Zamberlam,G.,
Brind'Amour,J., Pepin,D. and Boyer,A.
TITLE Lats1 and Lats2 regulate YAP and TAZ activity to control the
development of mouse Sertoli cells
JOURNAL FASEB J 38 (9), e23633 (2024)
PUBMED 38690712
REFERENCE 3 (residues 1 to 602)
AUTHORS Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
Jackson,S.P. and Balmus,G.
CONSRTM Sanger Mouse Genetics Project
TITLE Genetic determinants of micronucleus formation in vivo
JOURNAL Nature 627 (8002), 130-136 (2024)
PUBMED 38355793
REFERENCE 4 (residues 1 to 602)
AUTHORS Bruno,A., Contursi,A., Tacconelli,S., Sacco,A., Hofling,U.,
Mucci,M., Lamolinara,A., Del Pizzo,F., Ballerini,P., Di
Gregorio,P., Yu,Y. and Patrignani,P.
TITLE The specific deletion of cyclooxygenase-1 in
megakaryocytes/platelets reduces intestinal polyposis in ApcMin/+
mice
JOURNAL Pharmacol Res 185, 106506 (2022)
PUBMED 36241001
REMARK GeneRIF: The specific deletion of cyclooxygenase-1 in
megakaryocytes/platelets reduces intestinal polyposis in
Apc<sup>Min/+</sup> mice.
REFERENCE 5 (residues 1 to 602)
AUTHORS Shionoya,K., Eskilsson,A. and Blomqvist,A.
TITLE Prostaglandin production selectively in brain endothelial cells is
both necessary and sufficient for eliciting fever
JOURNAL Proc Natl Acad Sci U S A 119 (43), e2122562119 (2022)
PUBMED 36252026
REFERENCE 6 (residues 1 to 602)
AUTHORS Picot,D., Loll,P.J. and Garavito,R.M.
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,S.A., Meade,E.A. and DeWitt,D.L.
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,D.A., Fletcher,B.S., Varnum,B.C., Lim,R.W. and
Herschman,H.R.
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,P.B., Shabanowitz,R.B. and Clark,M.R.
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,D.L., el-Harith,E.A., Kraemer,S.A., Andrews,M.J., Yao,E.F.,
Armstrong,R.L. and Smith,W.L.
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 Select criteria :: based on conservation,
expression, longest protein
##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
/note="propagated from UniProtKB/Swiss-Prot (P22437.1)"
/calculated_mol_wt=2977
mat_peptide 27..602
/product="Prostaglandin G/H synthase 1.
/id=PRO_0000023869"
/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"
/note="N-linked (GlcNAc...) asparagine.
/evidence=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"
/note="N-linked (GlcNAc...) asparagine.
/evidence=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"
/note="N-linked (GlcNAc...) asparagine.
/evidence=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"
/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
//
