GenomeNet

Database: UniProt/SWISS-PROT
Entry: PGH1_HUMAN
LinkDB: PGH1_HUMAN
Original site: PGH1_HUMAN 
ID   PGH1_HUMAN              Reviewed;         599 AA.
AC   P23219; A8K1V7; B4DHQ2; B4E2S5; Q15122; Q3HY28; Q3HY29; Q5T7T6; Q5T7T7;
AC   Q5T7T8;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   24-JAN-2024, entry version 231.
DE   RecName: Full=Prostaglandin G/H synthase 1 {ECO:0000305};
DE            EC=1.14.99.1 {ECO:0000269|PubMed:7947975};
DE   AltName: Full=Cyclooxygenase-1 {ECO:0000303|PubMed:15308583};
DE            Short=COX-1 {ECO:0000303|PubMed:15308583};
DE   AltName: Full=Prostaglandin H2 synthase 1;
DE            Short=PGH synthase 1;
DE            Short=PGHS-1;
DE            Short=PHS 1;
DE   AltName: Full=Prostaglandin-endoperoxide synthase 1;
DE   Flags: Precursor;
GN   Name=PTGS1 {ECO:0000312|HGNC:HGNC:9604};
GN   Synonyms=COX1 {ECO:0000303|PubMed:15308583};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT ARG-8.
RX   PubMed=2512924; DOI=10.1016/s0006-291x(89)80049-x;
RA   Yokoyama C., Tanabe T.;
RT   "Cloning of human gene encoding prostaglandin endoperoxide synthase and
RT   primary structure of the enzyme.";
RL   Biochem. Biophys. Res. Commun. 165:888-894(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF SER-529, AND VARIANT
RP   ARG-8.
RX   PubMed=1907252; DOI=10.1096/fasebj.5.9.1907252;
RA   Funk C.D., Funk L.B., Kennedy M.E., Pong A.S., Fitzgerald G.A.;
RT   "Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA
RT   cloning, expression, and gene chromosomal assignment.";
RL   FASEB J. 5:2304-2312(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-8.
RC   TISSUE=Platelet;
RX   PubMed=1734857; DOI=10.1016/0006-291x(92)91750-k;
RA   Takahashi Y., Ueda N., Yoshimoto T., Yamamoto S., Yokoyama C., Miyata A.,
RA   Tanabe T., Fuse I., Hattori A., Shibata A.;
RT   "Immunoaffinity purification and cDNA cloning of human platelet
RT   prostaglandin endoperoxide synthase (cyclooxygenase).";
RL   Biochem. Biophys. Res. Commun. 182:433-438(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ARG-8.
RC   TISSUE=Lung fibroblast;
RX   PubMed=1587858; DOI=10.1016/s0021-9258(19)50092-8;
RA   Diaz A., Reginato A.M., Jimenez S.A.;
RT   "Alternative splicing of human prostaglandin G/H synthase mRNA and evidence
RT   of differential regulation of the resulting transcripts by transforming
RT   growth factor beta 1, interleukin 1 beta, and tumor necrosis factor
RT   alpha.";
RL   J. Biol. Chem. 267:10816-10822(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
RX   PubMed=16141368; DOI=10.1124/jpet.105.090944;
RA   Qin N., Zhang S.P., Reitz T.L., Mei J.M., Flores C.M.;
RT   "Cloning, expression, and functional characterization of human
RT   cyclooxygenase-1 splicing variants: evidence for intron 1 retention.";
RL   J. Pharmacol. Exp. Ther. 315:1298-1305(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ARG-8 AND
RP   LEU-17.
RX   PubMed=12192304; DOI=10.1097/00001721-200209000-00007;
RA   Scott B.T., Hasstedt S.J., Bovill E.G., Callas P.W., Valliere J.E.,
RA   Wang L.-H., Wu K.K., Long G.L.;
RT   "Characterization of the human prostaglandin H synthase 1 gene (PTGS1):
RT   exclusion by genetic linkage analysis as a second modifier gene in familial
RT   thrombosis.";
RL   Blood Coagul. Fibrinolysis 13:519-531(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANT
RP   ARG-8.
RC   TISSUE=Caudate nucleus, Hippocampus, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ARG-8; LEU-17;
RP   HIS-53; LEU-149 AND MET-237.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-8.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-8.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   CHARACTERIZATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=7947975; DOI=10.1016/0167-4838(94)90148-1;
RA   Barnett J., Chow J., Ives D., Chiou M., Mackenzie R., Osen E., Nguyen B.,
RA   Tsing S., Bach C., Freire J.;
RT   "Purification, characterization and selective inhibition of human
RT   prostaglandin G/H synthase 1 and 2 expressed in the baculovirus system.";
RL   Biochim. Biophys. Acta 1209:130-139(1994).
RN   [13]
RP   REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
RX   PubMed=10966456; DOI=10.1146/annurev.biochem.69.1.145;
RA   Smith W.L., DeWitt D.L., Garavito R.M.;
RT   "Cyclooxygenases: structural, cellular, and molecular biology.";
RL   Annu. Rev. Biochem. 69:145-182(2000).
RN   [14]
RP   REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN COLORECTAL
RP   CANCER.
RX   PubMed=24605250; DOI=10.4292/wjgpt.v5.i1.40;
RA   Sostres C., Gargallo C.J., Lanas A.;
RT   "Aspirin, cyclooxygenase inhibition and colorectal cancer.";
RL   World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [16]
RP   VARIANTS MET-237 AND ILE-481.
RX   PubMed=15308583; DOI=10.1093/carcin/bgh260;
RA   Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C.;
RT   "Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms
RT   and colon cancer risk.";
RL   Carcinogenesis 25:2467-2472(2004).
CC   -!- FUNCTION: Dual cyclooxygenase and peroxidase that plays an important
CC       role in the biosynthesis pathway of prostanoids, a class of C20
CC       oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-
CC       eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the
CC       inflammatory response. The cyclooxygenase activity oxygenates AA to the
CC       hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase
CC       activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2
CC       (PGH2), the precursor of all 2-series prostaglandins and thromboxanes.
CC       This complex transformation is initiated by abstraction of hydrogen at
CC       carbon 13 (with S-stereochemistry), followed by insertion of molecular
CC       O2 to form the endoperoxide bridge between carbon 9 and 11 that defines
CC       prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase
CC       activity) yields a hydroperoxy group in PGG2 that is then reduced to
CC       PGH2 by two electrons (PubMed:7947975). Involved in the constitutive
CC       production of prostanoids in particular in the stomach and platelets.
CC       In gastric epithelial cells, it is a key step in the generation of
CC       prostaglandins, such as prostaglandin E2 (PGE2), which plays an
CC       important role in cytoprotection. In platelets, it is involved in the
CC       generation of thromboxane A2 (TXA2), which promotes platelet activation
CC       and aggregation, vasoconstriction and proliferation of vascular smooth
CC       muscle cells (Probable). Can also use linoleate (LA, (9Z,12Z)-
CC       octadecadienoate, C18:2(n-6)) as substrate and produce
CC       hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner,
CC       being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-
CC       HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By
CC       similarity). {ECO:0000250|UniProtKB:P05979, ECO:0000269|PubMed:7947975,
CC       ECO:0000305|PubMed:10966456, ECO:0000305|PubMed:24605250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O +
CC         prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1;
CC         Evidence={ECO:0000269|PubMed:7947975};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729;
CC         Evidence={ECO:0000305|PubMed:7947975};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2;
CC         Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:82629; Evidence={ECO:0000269|PubMed:7947975};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597;
CC         Evidence={ECO:0000305|PubMed:7947975};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2;
CC         Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629;
CC         Evidence={ECO:0000269|PubMed:7947975};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601;
CC         Evidence={ECO:0000305|PubMed:7947975};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-
CC         octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:77895;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-
CC         octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:77852;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-
CC         octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:90850;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-
CC         octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:136655;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000250};
CC   -!- ACTIVITY REGULATION: The cyclooxygenase activity is inhibited by
CC       nonsteroidal anti-inflammatory drugs (NSAIDs) including ibuprofen,
CC       flurbiprofen, ketoprofen, naproxen, flurbiprofen, anirolac, fenclofenac
CC       and diclofenac. {ECO:0000269|PubMed:7947975}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.1 uM for arachidonate {ECO:0000269|PubMed:7947975};
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000269|PubMed:7947975}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P23219; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-6655935, EBI-2875816;
CC       P23219; P48645: NMU; NbExp=3; IntAct=EBI-6655935, EBI-10210351;
CC       P23219; P53801: PTTG1IP; NbExp=3; IntAct=EBI-6655935, EBI-3906138;
CC       P23219; Q8WZ73-3: RFFL; NbExp=3; IntAct=EBI-6655935, EBI-25839575;
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein.
CC       Endoplasmic reticulum membrane; Peripheral membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Long;
CC         IsoId=P23219-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P23219-2; Sequence=VSP_004673;
CC       Name=3;
CC         IsoId=P23219-3; Sequence=VSP_053936, VSP_004673;
CC       Name=4;
CC         IsoId=P23219-4; Sequence=VSP_046932;
CC       Name=5; Synonyms=1b3;
CC         IsoId=P23219-5; Sequence=VSP_054862;
CC       Name=6; Synonyms=1b2;
CC         IsoId=P23219-6; Sequence=VSP_054863;
CC   -!- MISCELLANEOUS: The conversion of arachidonate to prostaglandin H2 is a
CC       2 step reaction: a cyclooxygenase (COX) reaction which converts
CC       arachidonate to prostaglandin G2 (PGG2) and a peroxidase reaction in
CC       which PGG2 is reduced to prostaglandin H2 (PGH2). The cyclooxygenase
CC       reaction occurs in a hydrophobic channel in the core of the enzyme. The
CC       peroxidase reaction occurs at a heme-containing active site located
CC       near the protein surface. The nonsteroidal anti-inflammatory drugs
CC       (NSAIDs) binding site corresponds to the cyclooxygenase active site.
CC   -!- MISCELLANEOUS: Conversion of arachidonate to prostaglandin H2 is
CC       mediated by 2 different isozymes: the constitutive PTGS1 and the
CC       inducible PTGS2. PTGS1 is expressed constitutively and generally
CC       produces prostanoids acutely in response to hormonal stimuli to fine-
CC       tune physiological processes requiring instantaneous, continuous
CC       regulation (e.g. hemostasis). PTGS2 is inducible and typically produces
CC       prostanoids that mediate responses to physiological stresses such as
CC       infection and inflammation.
CC   -!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal anti-
CC       inflammatory drugs (NSAIDs) including aspirin and ibuprofen. Aspirin is
CC       able to produce an irreversible inactivation of the enzyme through a
CC       serine acetylation. Inhibition of the PGHSs with NSAIDs acutely reduces
CC       inflammation, pain, and fever, and long-term use of these drugs reduces
CC       fatal thrombotic events, as well as the development of colon cancer and
CC       Alzheimer's disease. PTGS2 is the principal isozyme responsible for
CC       production of inflammatory prostaglandins. New generation PTGSs
CC       inhibitors strive to be selective for PTGS2, to avoid side effects such
CC       as gastrointestinal complications and ulceration.
CC   -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/ptgs1/";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M31822; AAA36439.1; -; Genomic_DNA.
DR   EMBL; M31812; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31813; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31814; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31815; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31816; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31817; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31818; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31819; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31820; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31821; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M59979; AAA03630.1; -; mRNA.
DR   EMBL; S78220; AAB21215.1; -; mRNA.
DR   EMBL; S36219; AAB22216.1; -; mRNA.
DR   EMBL; S36271; AAB22217.1; -; mRNA.
DR   EMBL; DQ180741; ABA60098.1; -; mRNA.
DR   EMBL; DQ180742; ABA60099.1; -; mRNA.
DR   EMBL; AF440204; AAL33601.1; -; Genomic_DNA.
DR   EMBL; AK290022; BAF82711.1; -; mRNA.
DR   EMBL; AK295221; BAG58214.1; -; mRNA.
DR   EMBL; AK304403; BAG65237.1; -; mRNA.
DR   EMBL; AY449688; AAR08907.1; -; Genomic_DNA.
DR   EMBL; AL162424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471090; EAW87530.1; -; Genomic_DNA.
DR   EMBL; BC029840; AAH29840.1; -; mRNA.
DR   CCDS; CCDS59520.1; -. [P23219-3]
DR   CCDS; CCDS59521.1; -. [P23219-4]
DR   CCDS; CCDS6842.1; -. [P23219-1]
DR   CCDS; CCDS6843.1; -. [P23219-2]
DR   PIR; JH0259; JH0259.
DR   RefSeq; NP_000953.2; NM_000962.3. [P23219-1]
DR   RefSeq; NP_001258094.1; NM_001271165.1. [P23219-4]
DR   RefSeq; NP_001258095.1; NM_001271166.1.
DR   RefSeq; NP_001258297.1; NM_001271368.1. [P23219-3]
DR   RefSeq; NP_542158.1; NM_080591.2. [P23219-2]
DR   RefSeq; XP_011517178.1; XM_011518876.2.
DR   PDB; 6Y3C; X-ray; 3.36 A; A=24-599.
DR   PDBsum; 6Y3C; -.
DR   AlphaFoldDB; P23219; -.
DR   SMR; P23219; -.
DR   BioGRID; 111714; 12.
DR   CORUM; P23219; -.
DR   IntAct; P23219; 7.
DR   MINT; P23219; -.
DR   STRING; 9606.ENSP00000354612; -.
DR   BindingDB; P23219; -.
DR   ChEMBL; CHEMBL221; -.
DR   DrugBank; DB02047; (+)-2-(4-biphenyl)propionic acid.
DR   DrugBank; DB02773; (3-Chloro-4-Propoxy-Phenyl)-Acetic Acid.
DR   DrugBank; DB07983; 1-(4-IODOBENZOYL)-5-METHOXY-2-METHYL INDOLE-3-ACETIC ACID.
DR   DrugBank; DB07981; 2-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]-n-[(1R)-1-(hydroxymethyl)propyl]acetamide.
DR   DrugBank; DB07984; 2-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]-n-[(1S)-1-(hydroxymethyl)propyl]acetamide.
DR   DrugBank; DB02198; 2-Bromoacetyl Group.
DR   DrugBank; DB06736; Aceclofenac.
DR   DrugBank; DB13783; Acemetacin.
DR   DrugBank; DB00316; Acetaminophen.
DR   DrugBank; DB03667; Acetic Acid Salicyloyl-Amino-Ester.
DR   DrugBank; DB00945; Acetylsalicylic acid.
DR   DrugBank; DB01435; Antipyrine.
DR   DrugBank; DB01419; Antrafenine.
DR   DrugBank; DB04557; Arachidonic Acid.
DR   DrugBank; DB01014; Balsalazide.
DR   DrugBank; DB13501; Bendazac.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   DrugBank; DB00963; Bromfenac.
DR   DrugBank; DB13346; Bufexamac.
DR   DrugBank; DB13919; Candesartan.
DR   DrugBank; DB00796; Candesartan cilexetil.
DR   DrugBank; DB09061; Cannabidiol.
DR   DrugBank; DB00821; Carprofen.
DR   DrugBank; DB00672; Chlorpropamide.
DR   DrugBank; DB01401; Choline magnesium trisalicylate.
DR   DrugBank; DB00250; Dapsone.
DR   DrugBank; DB00035; Desmopressin.
DR   DrugBank; DB09213; Dexibuprofen.
DR   DrugBank; DB09214; Dexketoprofen.
DR   DrugBank; DB00829; Diazepam.
DR   DrugBank; DB00586; Diclofenac.
DR   DrugBank; DB00711; Diethylcarbamazine.
DR   DrugBank; DB00861; Diflunisal.
DR   DrugBank; DB00154; Dihomo-gamma-linolenic acid.
DR   DrugBank; DB01075; Diphenhydramine.
DR   DrugBank; DB00470; Dronabinol.
DR   DrugBank; DB09215; Droxicam.
DR   DrugBank; DB00216; Eletriptan.
DR   DrugBank; DB00749; Etodolac.
DR   DrugBank; DB00773; Etoposide.
DR   DrugBank; DB00573; Fenoprofen.
DR   DrugBank; DB02266; Flufenamic acid.
DR   DrugBank; DB00712; Flurbiprofen.
DR   DrugBank; DB03753; Flurbiprofen Methyl Ester.
DR   DrugBank; DB11323; Glycol salicylate.
DR   DrugBank; DB01355; Hexobarbital.
DR   DrugBank; DB01892; Hyperforin.
DR   DrugBank; DB01050; Ibuprofen.
DR   DrugBank; DB00159; Icosapent.
DR   DrugBank; DB01181; Ifosfamide.
DR   DrugBank; DB00328; Indomethacin.
DR   DrugBank; DB01029; Irbesartan.
DR   DrugBank; DB01221; Ketamine.
DR   DrugBank; DB06738; Ketobemidone.
DR   DrugBank; DB01009; Ketoprofen.
DR   DrugBank; DB00465; Ketorolac.
DR   DrugBank; DB06725; Lornoxicam.
DR   DrugBank; DB09212; Loxoprofen.
DR   DrugBank; DB01283; Lumiracoxib.
DR   DrugBank; DB01397; Magnesium salicylate.
DR   DrugBank; DB00939; Meclofenamic acid.
DR   DrugBank; DB14009; Medical Cannabis.
DR   DrugBank; DB00784; Mefenamic acid.
DR   DrugBank; DB00814; Meloxicam.
DR   DrugBank; DB11201; Menthyl salicylate.
DR   DrugBank; DB00244; Mesalazine.
DR   DrugBank; DB04817; Metamizole.
DR   DrugBank; DB00350; Minoxidil.
DR   DrugBank; DB00471; Montelukast.
DR   DrugBank; DB14011; Nabiximols.
DR   DrugBank; DB00461; Nabumetone.
DR   DrugBank; DB00788; Naproxen.
DR   DrugBank; DB00731; Nateglinide.
DR   DrugBank; DB06802; Nepafenac.
DR   DrugBank; DB04552; Niflumic acid.
DR   DrugBank; DB12445; Nitroaspirin.
DR   DrugBank; DB01837; O-acetyl-L-serine.
DR   DrugBank; DB00991; Oxaprozin.
DR   DrugBank; DB03752; P-(2'-Iodo-5'-Thenoyl)Hydrotropic Acid.
DR   DrugBank; DB03783; Phenacetin.
DR   DrugBank; DB11071; Phenyl salicylate.
DR   DrugBank; DB00812; Phenylbutazone.
DR   DrugBank; DB00554; Piroxicam.
DR   DrugBank; DB13514; Pranoprofen.
DR   DrugBank; DB09288; Propacetamol.
DR   DrugBank; DB02110; Protoporphyrin Ix Containing Co.
DR   DrugBank; DB02709; Resveratrol.
DR   DrugBank; DB00533; Rofecoxib.
DR   DrugBank; DB00412; Rosiglitazone.
DR   DrugBank; DB00936; Salicylic acid.
DR   DrugBank; DB01399; Salsalate.
DR   DrugBank; DB06739; Seratrodast.
DR   DrugBank; DB00795; Sulfasalazine.
DR   DrugBank; DB00605; Sulindac.
DR   DrugBank; DB00870; Suprofen.
DR   DrugBank; DB09295; Talniflumate.
DR   DrugBank; DB00469; Tenoxicam.
DR   DrugBank; DB00857; Terbinafine.
DR   DrugBank; DB01041; Thalidomide.
DR   DrugBank; DB01600; Tiaprofenic acid.
DR   DrugBank; DB09216; Tolfenamic acid.
DR   DrugBank; DB00500; Tolmetin.
DR   DrugBank; DB05109; Trabectedin.
DR   DrugBank; DB08814; Triflusal.
DR   DrugBank; DB11079; Trolamine salicylate.
DR   DrugBank; DB00313; Valproic acid.
DR   DrugBank; DB00582; Voriconazole.
DR   DrugBank; DB00549; Zafirlukast.
DR   DrugBank; DB06737; Zaltoprofen.
DR   DrugBank; DB00744; Zileuton.
DR   DrugBank; DB01198; Zopiclone.
DR   DrugCentral; P23219; -.
DR   GuidetoPHARMACOLOGY; 1375; -.
DR   SwissLipids; SLP:000001103; -.
DR   MoonDB; P23219; Curated.
DR   PeroxiBase; 3320; HsPGHS01.
DR   GlyConnect; 1648; 1 N-Linked glycan (1 site).
DR   GlyCosmos; P23219; 3 sites, 1 glycan.
DR   GlyGen; P23219; 3 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; P23219; -.
DR   PhosphoSitePlus; P23219; -.
DR   BioMuta; PTGS1; -.
DR   DMDM; 317373262; -.
DR   EPD; P23219; -.
DR   jPOST; P23219; -.
DR   MassIVE; P23219; -.
DR   MaxQB; P23219; -.
DR   PaxDb; 9606-ENSP00000354612; -.
DR   PeptideAtlas; P23219; -.
DR   ProteomicsDB; 4239; -.
DR   ProteomicsDB; 54063; -. [P23219-1]
DR   ProteomicsDB; 54064; -. [P23219-2]
DR   Pumba; P23219; -.
DR   Antibodypedia; 775; 773 antibodies from 45 providers.
DR   DNASU; 5742; -.
DR   Ensembl; ENST00000223423.8; ENSP00000223423.4; ENSG00000095303.17. [P23219-2]
DR   Ensembl; ENST00000362012.7; ENSP00000354612.2; ENSG00000095303.17. [P23219-1]
DR   Ensembl; ENST00000373698.7; ENSP00000362802.5; ENSG00000095303.17. [P23219-4]
DR   Ensembl; ENST00000540753.6; ENSP00000437709.1; ENSG00000095303.17. [P23219-3]
DR   GeneID; 5742; -.
DR   KEGG; hsa:5742; -.
DR   MANE-Select; ENST00000362012.7; ENSP00000354612.2; NM_000962.4; NP_000953.2.
DR   UCSC; uc004bmf.3; human. [P23219-1]
DR   AGR; HGNC:9604; -.
DR   CTD; 5742; -.
DR   DisGeNET; 5742; -.
DR   GeneCards; PTGS1; -.
DR   HGNC; HGNC:9604; PTGS1.
DR   HPA; ENSG00000095303; Tissue enhanced (intestine, skin, urinary bladder).
DR   MIM; 176805; gene.
DR   neXtProt; NX_P23219; -.
DR   OpenTargets; ENSG00000095303; -.
DR   PharmGKB; PA24346; -.
DR   VEuPathDB; HostDB:ENSG00000095303; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00390000010743; -.
DR   HOGENOM; CLU_022428_0_0_1; -.
DR   InParanoid; P23219; -.
DR   OMA; LFGSQFQ; -.
DR   OrthoDB; 1086441at2759; -.
DR   PhylomeDB; P23219; -.
DR   TreeFam; TF329675; -.
DR   BioCyc; MetaCyc:HS01815-MONOMER; -.
DR   BRENDA; 1.14.99.1; 2681.
DR   PathwayCommons; P23219; -.
DR   Reactome; R-HSA-140180; COX reactions.
DR   Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   SABIO-RK; P23219; -.
DR   SignaLink; P23219; -.
DR   SIGNOR; P23219; -.
DR   UniPathway; UPA00662; -.
DR   BioGRID-ORCS; 5742; 6 hits in 1175 CRISPR screens.
DR   ChiTaRS; PTGS1; human.
DR   GeneWiki; PTGS1; -.
DR   GenomeRNAi; 5742; -.
DR   Pharos; P23219; Tclin.
DR   PRO; PR:P23219; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; P23219; Protein.
DR   Bgee; ENSG00000095303; Expressed in stromal cell of endometrium and 180 other cell types or tissues.
DR   ExpressionAtlas; P23219; baseline and differential.
DR   Genevisible; P23219; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IDA:BHF-UCL.
DR   GO; GO:0019371; P:cyclooxygenase pathway; IDA:BHF-UCL.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd09816; prostaglandin_endoperoxide_synthase; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   PANTHER; PTHR11903:SF6; PROSTAGLANDIN G/H SYNTHASE 1; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Dioxygenase; Disulfide bond;
KW   EGF-like domain; Endoplasmic reticulum; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Metal-binding; Microsome; Oxidoreductase;
KW   Peroxidase; Prostaglandin biosynthesis; Prostaglandin metabolism;
KW   Reference proteome; Signal.
FT   SIGNAL          1..23
FT   CHAIN           24..599
FT                   /note="Prostaglandin G/H synthase 1"
FT                   /id="PRO_0000023868"
FT   DOMAIN          31..69
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   ACT_SITE        206
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   ACT_SITE        384
FT                   /note="For cyclooxygenase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         387
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   SITE            529
FT                   /note="Aspirin-acetylated serine"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        36..158
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..56
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        568..574
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..109
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046932"
FT   VAR_SEQ         1..32
FT                   /note="MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPV -> MRKPRLM (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_053936"
FT   VAR_SEQ         1..3
FT                   /note="MSR -> MSRECDPGARWGIFLASGGALNARLSPSSLSSAG (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141368"
FT                   /id="VSP_054862"
FT   VAR_SEQ         1..3
FT                   /note="MSR -> MSRECDPGARWGIFLASWWSLECQLSPSSLSSAG (in
FT                   isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:16141368"
FT                   /id="VSP_054863"
FT   VAR_SEQ         396..432
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:1587858"
FT                   /id="VSP_004673"
FT   VARIANT         8
FT                   /note="W -> R (in dbSNP:rs1236913)"
FT                   /evidence="ECO:0000269|PubMed:12192304,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:1587858, ECO:0000269|PubMed:1734857,
FT                   ECO:0000269|PubMed:1907252, ECO:0000269|PubMed:2512924,
FT                   ECO:0000269|Ref.10, ECO:0000269|Ref.8"
FT                   /id="VAR_013451"
FT   VARIANT         17
FT                   /note="P -> L (in dbSNP:rs3842787)"
FT                   /evidence="ECO:0000269|PubMed:12192304, ECO:0000269|Ref.8"
FT                   /id="VAR_013452"
FT   VARIANT         53
FT                   /note="R -> H (in dbSNP:rs3842789)"
FT                   /evidence="ECO:0000269|Ref.8"
FT                   /id="VAR_019161"
FT   VARIANT         149
FT                   /note="R -> L (in dbSNP:rs10306140)"
FT                   /evidence="ECO:0000269|Ref.8"
FT                   /id="VAR_019162"
FT   VARIANT         185
FT                   /note="K -> T (in dbSNP:rs3842792)"
FT                   /id="VAR_056663"
FT   VARIANT         237
FT                   /note="L -> M (in dbSNP:rs5789)"
FT                   /evidence="ECO:0000269|PubMed:15308583, ECO:0000269|Ref.8"
FT                   /id="VAR_019163"
FT   VARIANT         341
FT                   /note="K -> R (in dbSNP:rs3842799)"
FT                   /id="VAR_056664"
FT   VARIANT         359
FT                   /note="K -> R (in dbSNP:rs5791)"
FT                   /id="VAR_013453"
FT   VARIANT         443
FT                   /note="I -> V (in dbSNP:rs5792)"
FT                   /id="VAR_013454"
FT   VARIANT         481
FT                   /note="V -> I (in dbSNP:rs5794)"
FT                   /evidence="ECO:0000269|PubMed:15308583"
FT                   /id="VAR_028017"
FT   MUTAGEN         529
FT                   /note="S->N: Abolishes cyclooxygenase activity."
FT                   /evidence="ECO:0000269|PubMed:1907252"
FT   CONFLICT        12
FT                   /note="F -> L (in Ref. 1; AAA36439)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="R -> L (in Ref. 1; AAA36439)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="M -> T (in Ref. 1; AAA36439)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        423
FT                   /note="D -> G (in Ref. 7; BAG65237)"
FT                   /evidence="ECO:0000305"
FT   HELIX           34..37
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          45..49
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   TURN            50..52
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   TURN            65..68
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           73..79
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           85..91
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           96..103
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           107..120
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           138..142
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          148..151
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          163..166
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           173..179
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           195..205
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   TURN            206..208
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   TURN            213..215
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          217..221
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           230..233
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           238..243
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          259..261
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   TURN            265..267
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   TURN            280..282
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          287..290
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           291..293
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           295..318
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           324..345
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           347..352
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           362..365
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           378..383
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           387..389
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          392..394
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           403..406
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           412..425
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          427..429
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           441..443
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           444..456
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           462..468
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          475..477
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           478..481
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           484..494
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           497..499
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           502..507
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          516..518
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           519..533
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           537..539
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   TURN            541..543
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   TURN            546..550
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           552..558
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   HELIX           564..567
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          570..573
FT                   /evidence="ECO:0007829|PDB:6Y3C"
FT   STRAND          578..580
FT                   /evidence="ECO:0007829|PDB:6Y3C"
SQ   SEQUENCE   599 AA;  68686 MW;  1F4F734BCD00346D CRC64;
     MSRSLLLWFL LFLLLLPPLP VLLADPGAPT PVNPCCYYPC QHQGICVRFG LDRYQCDCTR
     TGYSGPNCTI PGLWTWLRNS LRPSPSFTHF LLTHGRWFWE FVNATFIREM LMRLVLTVRS
     NLIPSPPTYN SAHDYISWES FSNVSYYTRI LPSVPKDCPT PMGTKGKKQL PDAQLLARRF
     LLRRKFIPDP QGTNLMFAFF AQHFTHQFFK TSGKMGPGFT KALGHGVDLG HIYGDNLERQ
     YQLRLFKDGK LKYQVLDGEM YPPSVEEAPV LMHYPRGIPP QSQMAVGQEV FGLLPGLMLY
     ATLWLREHNR VCDLLKAEHP TWGDEQLFQT TRLILIGETI KIVIEEYVQQ LSGYFLQLKF
     DPELLFGVQF QYRNRIAMEF NHLYHWHPLM PDSFKVGSQE YSYEQFLFNT SMLVDYGVEA
     LVDAFSRQIA GRIGGGRNMD HHILHVAVDV IRESREMRLQ PFNEYRKRFG MKPYTSFQEL
     VGEKEMAAEL EELYGDIDAL EFYPGLLLEK CHPNSIFGES MIEIGAPFSL KGLLGNPICS
     PEYWKPSTFG GEVGFNIVKT ATLKKLVCLN TKTCPYVSFR VPDASQDDGP AVERPSTEL
//
DBGET integrated database retrieval system