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Prostaglandin G/H synthase 1 (EC 1.14.99.1) (Cyclooxygenase-1) (COX-1) (Prostaglandin H2 synthase 1) (PGH synthase 1) (PGHS-1) (PHS 1) (Prostaglandin-endoperoxide synthase 1)

 PGH1_MOUSE              Reviewed;         602 AA.
P22437;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
22-NOV-2017, entry version 176.
RecName: Full=Prostaglandin G/H synthase 1;
EC=1.14.99.1;
AltName: Full=Cyclooxygenase-1;
Short=COX-1;
AltName: Full=Prostaglandin H2 synthase 1;
Short=PGH synthase 1;
Short=PGHS-1;
Short=PHS 1;
AltName: Full=Prostaglandin-endoperoxide synthase 1;
Flags: Precursor;
Name=Ptgs1; Synonyms=Cox-1, Cox1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2108169;
Dewitt D.L., El-Harith E.A., Kraemer S.A., Andrews M.J., Yao E.F.,
Armstrong R.L., Smith W.L.;
"The aspirin and heme-binding sites of ovine and murine prostaglandin
endoperoxide synthases.";
J. Biol. Chem. 265:5192-5198(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
PubMed=10966456; DOI=10.1146/annurev.biochem.69.1.145;
Smith W.L., DeWitt D.L., Garavito R.M.;
"Cyclooxygenases: structural, cellular, and molecular biology.";
Annu. Rev. Biochem. 69:145-182(2000).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN
COLORECTAL CANCER.
PubMed=24605250; DOI=10.4292/wjgpt.v5.i1.40;
Sostres C., Gargallo C.J., Lanas A.;
"Aspirin, cyclooxygenase inhibition and colorectal cancer.";
World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014).
-!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
committed step in prostanoid synthesis. Involved in the
constitutive production of prostanoids in particular in the
stomach and platelets. In gastric epithelial cells, it is a key
step in the generation of prostaglandins, such as prostaglandin E2
(PGE2), which plays an important role in cytoprotection. In
platelets, it is involved in the generation of thromboxane A2
(TXA2), which promotes platelet activation and aggregation,
vasoconstriction and proliferation of vascular smooth muscle
cells.
-!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
H(2) + A + H(2)O.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000250};
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane
protein. Endoplasmic reticulum membrane; Peripheral membrane
protein.
-!- MISCELLANEOUS: The conversion of arachidonate to prostaglandin H2
is a 2 step reaction: a cyclooxygenase (COX) reaction which
converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase
reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The
cyclooxygenase reaction occurs in a hydrophobic channel in the
core of the enzyme. The peroxidase reaction occurs at a heme-
containing active site located near the protein surface. The
nonsteroidal anti-inflammatory drugs (NSAIDs) binding site
corresponds to the cyclooxygenase active site.
-!- MISCELLANEOUS: Conversion of arachidonate to prostaglandin H2 is
mediated by 2 different isozymes: the constitutive PTGS1 and the
inducible PTGS2. PGHS1 is expressed constitutively and generally
produces prostanoids acutely in response to hormonal stimuli to
fine-tune physiological processes requiring instantaneous,
continuous regulation (e.g. hemostasis). PGHS2 is inducible and
typically produces prostanoids that mediate responses to
physiological stresses such as infection and inflammation.
-!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal
anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen.
Aspirin is able to produce an irreversible inactivation of the
enzyme through a serine acetylation. Inhibition of the PGHSs with
NSAIDs acutely reduces inflammation, pain, and fever, and long-
term use of these drugs reduces fatal thrombotic events, as well
as the development of colon cancer and Alzheimer's disease. PTGS2
is the principal isozyme responsible for production of
inflammatory prostaglandins. New generation PTGSs inhibitors
strive to be selective for PTGS2, to avoid side effects such as
gastrointestinal complications and ulceration.
-!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M34141; AAA39913.1; -; mRNA.
EMBL; BC005573; AAH05573.1; -; mRNA.
CCDS; CCDS15970.1; -.
PIR; A35564; A35564.
RefSeq; NP_032995.1; NM_008969.4.
RefSeq; XP_006497853.1; XM_006497790.3.
RefSeq; XP_006497854.1; XM_006497791.3.
RefSeq; XP_011237338.1; XM_011239036.2.
RefSeq; XP_017171985.1; XM_017316496.1.
UniGene; Mm.275434; -.
ProteinModelPortal; P22437; -.
SMR; P22437; -.
BioGrid; 202462; 2.
IntAct; P22437; 3.
MINT; MINT-4107353; -.
STRING; 10090.ENSMUSP00000059977; -.
BindingDB; P22437; -.
ChEMBL; CHEMBL2649; -.
PeroxiBase; 3361; MmPGHS01.
PhosphoSitePlus; P22437; -.
PaxDb; P22437; -.
PeptideAtlas; P22437; -.
PRIDE; P22437; -.
Ensembl; ENSMUST00000062069; ENSMUSP00000059977; ENSMUSG00000047250.
GeneID; 19224; -.
KEGG; mmu:19224; -.
UCSC; uc008jll.2; mouse.
CTD; 5742; -.
MGI; MGI:97797; Ptgs1.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00390000010743; -.
HOGENOM; HOG000013149; -.
HOVERGEN; HBG000366; -.
InParanoid; P22437; -.
KO; K00509; -.
OMA; FKTSGKM; -.
OrthoDB; EOG091G03CD; -.
PhylomeDB; P22437; -.
TreeFam; TF329675; -.
Reactome; R-MMU-140180; COX reactions.
Reactome; R-MMU-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
UniPathway; UPA00662; -.
ChiTaRS; Ptgs1; mouse.
PRO; PR:P22437; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000047250; -.
CleanEx; MM_PTGS1; -.
ExpressionAtlas; P22437; baseline and differential.
Genevisible; P22437; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; ISO:MGI.
GO; GO:0019371; P:cyclooxygenase pathway; ISO:MGI.
GO; GO:0006954; P:inflammatory response; IEA:InterPro.
GO; GO:0030216; P:keratinocyte differentiation; NAS:UniProtKB.
GO; GO:0001516; P:prostaglandin biosynthetic process; IMP:MGI.
GO; GO:0006693; P:prostaglandin metabolic process; IMP:MGI.
GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
Gene3D; 1.10.640.10; -; 1.
InterPro; IPR029580; COX-1.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
InterPro; IPR037120; Haem_peroxidase_sf.
PANTHER; PTHR11903:SF6; PTHR11903:SF6; 1.
Pfam; PF03098; An_peroxidase; 1.
PRINTS; PR00457; ANPEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50292; PEROXIDASE_3; 1.
1: Evidence at protein level;
Complete proteome; Dioxygenase; Disulfide bond; EGF-like domain;
Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
Glycoprotein; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
Membrane; Metal-binding; Microsome; Oxidoreductase; Peroxidase;
Prostaglandin biosynthesis; Prostaglandin metabolism;
Reference proteome; Signal.
SIGNAL 1 26
CHAIN 27 602 Prostaglandin G/H synthase 1.
/FTId=PRO_0000023869.
DOMAIN 34 72 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
ACT_SITE 209 209 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
ACT_SITE 387 387 For cyclooxygenase activity.
{ECO:0000250}.
METAL 390 390 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00298}.
SITE 532 532 Aspirin-acetylated serine.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 38 49 {ECO:0000250}.
DISULFID 39 161 {ECO:0000250}.
DISULFID 43 59 {ECO:0000250}.
DISULFID 61 71 {ECO:0000250}.
DISULFID 571 577 {ECO:0000250}.
SEQUENCE 602 AA; 69042 MW; 634C0E602045C3A0 CRC64;
MSRRSLSLWF PLLLLLLLPP TPSVLLADPG VPSPVNPCCY YPCQNQGVCV RFGLDNYQCD
CTRTGYSGPN CTIPEIWTWL RNSLRPSPSF THFLLTHGYW LWEFVNATFI REVLMRLVLT
VRSNLIPSPP TYNSAHDYIS WESFSNVSYY TRILPSVPKD CPTPMGTKGK KQLPDVQLLA
QQLLLRREFI PAPQGTNILF AFFAQHFTHQ FFKTSGKMGP GFTKALGHGV DLGHIYGDNL
ERQYHLRLFK DGKLKYQVLD GEVYPPSVEQ ASVLMRYPPG VPPERQMAVG QEVFGLLPGL
MLFSTIWLRE HNRVCDLLKE EHPTWDDEQL FQTTRLILIG ETIKIVIEEY VQHLSGYFLQ
LKFDPELLFR AQFQYRNRIA MEFNHLYHWH PLMPNSFQVG SQEYSYEQFL FNTSMLVDYG
VEALVDAFSR QRAGRIGGGR NFDYHVLHVA VDVIKESREM RLQPFNEYRK RFGLKPYTSF
QELTGEKEMA AELEELYGDI DALEFYPGLL LEKCQPNSIF GESMIEMGAP FSLKGLLGNP
ICSPEYWKPS TFGGDVGFNL VNTASLKKLV CLNTKTCPYV SFRVPDYPGD DGSVLVRRST
EL


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