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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_CANLF              Reviewed;         603 AA.
Q8HZR1; F1PBX3; Q8HZR0;
14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
14-MAY-2014, sequence version 2.
25-OCT-2017, entry version 111.
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=COX1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING,
GLYCOSYLATION, AND SUBCELLULAR LOCATION.
TISSUE=Brain cortex;
PubMed=12242329; DOI=10.1073/pnas.162468699;
Chandrasekharan N.V., Dai H., Roos K.L., Evanson N.K., Tomsik J.,
Elton T.S., Simmons D.L.;
"COX-3, a cyclooxygenase-1 variant inhibited by acetaminophen and
other analgesic/antipyretic drugs: cloning, structure, and
expression.";
Proc. Natl. Acad. Sci. U.S.A. 99:13926-13931(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boxer;
PubMed=16341006; DOI=10.1038/nature04338;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
-!- 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
(By similarity). {ECO:0000250}.
-!- 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. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000269|PubMed:12242329}. Endoplasmic
reticulum membrane {ECO:0000269|PubMed:12242329}; Peripheral
membrane protein {ECO:0000269|PubMed:12242329}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=COX-1;
IsoId=Q8HZR1-1; Sequence=Displayed;
Name=2; Synonyms=COX-3;
IsoId=Q8HZR1-2; Sequence=VSP_054856;
Name=3; Synonyms=PCOX-1a;
IsoId=Q8HZR1-3; Sequence=VSP_054856, VSP_054857;
Note=No enzymatic activity. Membrane-bound.;
Name=4; Synonyms=PCOX-1b;
IsoId=Q8HZR1-4; Sequence=VSP_054857;
-!- TISSUE SPECIFICITY: Brain cortex. Isoform 2 is expressed in the
cerebral cortex and heart.
-!- PTM: N-glycosylated. N-linked glycosylation is necessary for
enzymatic activity. {ECO:0000269|PubMed:12242329}.
-!- 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
-----------------------------------------------------------------------
EMBL; AF535138; AAN33049.1; -; mRNA.
EMBL; AF535139; AAN38739.1; -; mRNA.
EMBL; AAEX03006907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001003023.1; NM_001003023.2.
UniGene; Cfa.61; -.
SMR; Q8HZR1; -.
STRING; 9615.ENSCAFP00000030067; -.
BindingDB; Q8HZR1; -.
ChEMBL; CHEMBL4133; -.
PeroxiBase; 3362; CfaPGHS01.
PaxDb; Q8HZR1; -.
Ensembl; ENSCAFT00000032279; ENSCAFP00000030061; ENSCAFG00000020263. [Q8HZR1-3]
Ensembl; ENSCAFT00000032287; ENSCAFP00000030067; ENSCAFG00000020263. [Q8HZR1-1]
GeneID; 403544; -.
KEGG; cfa:403544; -.
CTD; 5742; -.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00390000010743; -.
HOGENOM; HOG000013149; -.
HOVERGEN; HBG000366; -.
KO; K00509; -.
OMA; FKTSGKM; -.
OrthoDB; EOG091G03CD; -.
Reactome; R-CFA-140180; COX reactions.
Reactome; R-CFA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
UniPathway; UPA00662; -.
Proteomes; UP000002254; Chromosome 9.
Bgee; ENSCAFG00000020263; -.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
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; IEA:UniProtKB-EC.
GO; GO:0019371; P:cyclooxygenase pathway; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:InterPro.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
InterPro; IPR029580; COX-1.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
PANTHER; PTHR11903:SF6; PTHR11903:SF6; 1.
Pfam; PF03098; An_peroxidase; 1.
Pfam; PF00008; EGF; 1.
PRINTS; PR00457; ANPEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50292; PEROXIDASE_3; 1.
1: Evidence at protein level;
Alternative splicing; 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 27 {ECO:0000255}.
CHAIN 28 603 Prostaglandin G/H synthase 1.
/FTId=PRO_0000429170.
DOMAIN 35 73 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
ACT_SITE 210 210 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
ACT_SITE 388 388 For cyclooxygenase activity.
{ECO:0000250}.
METAL 391 391 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00298}.
SITE 533 533 Aspirin-acetylated serine. {ECO:0000250}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 50 {ECO:0000250}.
DISULFID 40 162 {ECO:0000250}.
DISULFID 44 60 {ECO:0000250}.
DISULFID 62 72 {ECO:0000250}.
DISULFID 572 578 {ECO:0000250}.
VAR_SEQ 3 3 R -> REFDPEAPRNPLRLPGEPRMPGPALTSRSAG (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:12242329}.
/FTId=VSP_054856.
VAR_SEQ 122 340 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:12242329}.
/FTId=VSP_054857.
CONFLICT 597 597 E -> Q (in Ref. 1; AAN33049/AAN38739).
{ECO:0000305}.
SEQUENCE 603 AA; 69305 MW; 435B3E3A3D5DCCA6 CRC64;
MSRGSRLHRW PLLLLLLLLL PPPPVLPAEA RTPAPVNPCC YYPCQHQGIC VRFGLDRYQC
DCTRTGYSGP NCTIPELWTW LRNSLRPSPS FLHFLLTHGR WFWEFINATF IRDMLMRLVL
TARSNLIPSP PTYNIAHDYI SWESFSNVSY YTRVLPSVPQ DCPTPMGTKG KKQLPDAQLL
GRRFLLRRKF IPDPQGTNLM FAFFAQHFTH QFFKTSGKMG PGFTKALGHG VDLGHIYGDN
LDRQYQLRLF KDGKLKYQVL DGEMYPPSVE EAPVLMHYPR GILPQSQMAV GQEVFGLLPG
LMLYATLWLR EHNRVCDLLK AEHPTWGDEQ LFQTARLILI GETIKIVIEE YVQQLSGYFL
QLKFDPELLF SAQFQYRNRI AMEFNQLYHW HPLMPDSFWV GSQEYSYEQF LFNTSMLTHY
GIEALVDAFS RQSAGRIGGG RNIDHHVLHV AVETIKESRE LRLQPFNEYR KRFGMRPYMS
FQELTGEKEM AAELEELYGD IDALEFYPGL LLEKCHPNSI FGESMIEIGA PFSLKGLLGN
PICSPEYWKP STFGGEMGFN MVKTATLKKL VCLNTKTCPY VSFRVPDPHQ DGGPGVERPS
TEL


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