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Database: UniProt/SWISS-PROT
Entry: PGH2_HUMAN
LinkDB: PGH2_HUMAN
Original site: PGH2_HUMAN 
ID   PGH2_HUMAN              Reviewed;         604 AA.
AC   P35354; A8K802; Q16876;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   20-JUN-2018, entry version 196.
DE   RecName: Full=Prostaglandin G/H synthase 2;
DE            EC=1.14.99.1 {ECO:0000269|PubMed:16373578, ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593};
DE   AltName: Full=Cyclooxygenase-2;
DE            Short=COX-2;
DE   AltName: Full=PHS II;
DE   AltName: Full=Prostaglandin H2 synthase 2;
DE            Short=PGH synthase 2;
DE            Short=PGHS-2;
DE   AltName: Full=Prostaglandin-endoperoxide synthase 2;
DE   Flags: Precursor;
GN   Name=PTGS2; Synonyms=COX2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Endothelial cell;
RX   PubMed=8473346;
RA   Jones D.A., Carlton D.P., McIntyre T.M., Zimmerman G.A.,
RA   Prescott S.M.;
RT   "Molecular cloning of human prostaglandin endoperoxide synthase type
RT   II and demonstration of expression in response to cytokines.";
RL   J. Biol. Chem. 268:9049-9054(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Endothelial cell;
RX   PubMed=1380156; DOI=10.1073/pnas.89.16.7384;
RA   Hla T., Neilson K.;
RT   "Human cyclooxygenase-2 cDNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7384-7388(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Peripheral blood;
RX   PubMed=8181472; DOI=10.1111/j.1432-1033.1994.tb18804.x;
RA   Kosaka T., Miyata A., Ihara H., Hara S., Sugimoto T., Takeda O.,
RA   Takahashi E., Tanabe T.;
RT   "Characterization of the human gene (PTGS2) encoding prostaglandin-
RT   endoperoxide synthase 2.";
RL   Eur. J. Biochem. 221:889-897(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=7945196; DOI=10.1042/bj3020723;
RA   Appleby S.B., Ristimaki A., Neilson K., Narko K., Hla T.;
RT   "Structure of the human cyclo-oxygenase-2 gene.";
RL   Biochem. J. 302:723-727(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RA   Sharma S.V., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction
RT   sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-228; ALA-428;
RP   ALA-511 AND ARG-587.
RG   NIEHS SNPs program;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   SeattleSNPs variation discovery resource;
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Synovium;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   CHARACTERIZATION.
RX   PubMed=7947975; DOI=10.1016/0167-4838(94)90148-1;
RA   Barnett J., Chow J., Ives D., Chiou M., Mackenzie R., Osen E.,
RA   Nguyen B., 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
RT   system.";
RL   Biochim. Biophys. Acta 1209:130-139(1994).
RN   [13]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   S-NITROSYLATION AT CYS-526, AND MUTAGENESIS OF CYS-526; CYS-555 AND
RP   CYS-561.
RX   PubMed=16373578; DOI=10.1126/science.1119407;
RA   Kim S.F., Huri D.A., Snyder S.H.;
RT   "Inducible nitric oxide synthase binds, S-nitrosylates, and activates
RT   cyclooxygenase-2.";
RL   Science 310:1966-1970(2005).
RN   [14]
RP   GLYCOSYLATION AT ASN-580.
RX   PubMed=17113084; DOI=10.1016/j.febslet.2006.10.073;
RA   Sevigny M.B., Li C.F., Alas M., Hughes-Fulford M.;
RT   "Glycosylation regulates turnover of cyclooxygenase-2.";
RL   FEBS Lett. 580:6533-6536(2006).
RN   [15]
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   [16]
RP   REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN
RP   COLORECTAL 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   [17] {ECO:0000244|PDB:5KIR}
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 19-569 IN COMPLEX WITH
RP   PROTOPORPHYRIN IX AND ROFECOXIB, COFACTOR, GLYCOSYLATION AT ASN-130
RP   AND ASN-396, AND DISULFIDE BONDS.
RX   PubMed=27710942; DOI=10.1107/S2053230X16014230;
RA   Orlando B.J., Malkowski M.G.;
RT   "Crystal structure of rofecoxib bound to human cyclooxygenase-2.";
RL   Acta Crystallogr. F 72:772-776(2016).
RN   [18] {ECO:0000244|PDB:5F19, ECO:0000244|PDB:5F1A}
RP   X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 19-569 IN COMPLEX WITH
RP   PROTOPORPHYRIN IX AND SALICYLIC ACID, FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF
RP   SER-516 AND GLY-519, ENZYME REGULATION, GLYCOSYLATION AT ASN-53;
RP   ASN-130 AND ASN-396, AND DISULFIDE BONDS.
RX   PubMed=26859324; DOI=10.1021/acs.biochem.5b01378;
RA   Lucido M.J., Orlando B.J., Vecchio A.J., Malkowski M.G.;
RT   "Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2:
RT   Insight into the Formation of Products with Reversed
RT   Stereochemistry.";
RL   Biochemistry 55:1226-1238(2016).
RN   [19] {ECO:0000244|PDB:5IKQ, ECO:0000244|PDB:5IKR, ECO:0000244|PDB:5IKT, ECO:0000244|PDB:5IKV}
RP   X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 19-569 IN COMPLEX WITH
RP   PROTOPORPHYRIN IX AND FLUFENAMIC ACID, FUNCTION, CATALYTIC ACTIVITY,
RP   ENZYME REGULATION, COFACTOR, SUBUNIT, GLYCOSYLATION AT ASN-53; ASN-130
RP   AND ASN-396, DISULFIDE BONDS, AND MUTAGENESIS OF TYR-371 AND SER-516.
RX   PubMed=27226593; DOI=10.1074/jbc.M116.725713;
RA   Orlando B.J., Malkowski M.G.;
RT   "Substrate-selective Inhibition of Cyclooxygeanse-2 by Fenamic Acid
RT   Derivatives Is Dependent on Peroxide Tone.";
RL   J. Biol. Chem. 291:15069-15081(2016).
RN   [20]
RP   VARIANT ALA-511.
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)
RT   polymorphisms and colon cancer risk.";
RL   Carcinogenesis 25:2467-2472(2004).
CC   -!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
CC       committed step in prostanoid synthesis (PubMed:26859324,
CC       PubMed:27226593). Constitutively expressed in some tissues in
CC       physiological conditions, such as the endothelium, kidney and
CC       brain, and in pathological conditions, such as in cancer. PTGS2 is
CC       responsible for production of inflammatory prostaglandins. Up-
CC       regulation of PTGS2 is also associated with increased cell
CC       adhesion, phenotypic changes, resistance to apoptosis and tumor
CC       angiogenesis. In cancer cells, PTGS2 is a key step in the
CC       production of prostaglandin E2 (PGE2), which plays important roles
CC       in modulating motility, proliferation and resistance to apoptosis.
CC       {ECO:0000269|PubMed:16373578, ECO:0000269|PubMed:26859324,
CC       ECO:0000269|PubMed:27226593}.
CC   -!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
CC       H(2) + A + H(2)O. {ECO:0000269|PubMed:16373578,
CC       ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000269|PubMed:26859324,
CC         ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27710942};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
CC       subunit. {ECO:0000269|PubMed:26859324,
CC       ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27710942};
CC   -!- ENZYME REGULATION: Inhibited by nonsteroidal anti-inflammatory
CC       drugs (NSAIDs) including aspirin, ibuprofen, flurbiprofen and
CC       celecoxib (PubMed:26859324). Inhibited by flufenamic acid,
CC       mefenamic acid and tolfenamic acid (PubMed:27226593).
CC       {ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=16.2 uM for arachidonate (in absence of sodium nitroprusside
CC         NO donor) {ECO:0000269|PubMed:16373578};
CC         KM=12 uM for arachidonic acid {ECO:0000269|PubMed:26859324};
CC         KM=17.0 uM for arachidonate (in presence of sodium nitroprusside
CC         NO donor) {ECO:0000269|PubMed:16373578};
CC         Vmax=81.3 nmol/min/mg enzyme (in absence of sodium nitroprusside
CC         NO donor) {ECO:0000269|PubMed:16373578};
CC         Vmax=132 nmol/min/mg enzyme (in absence of sodium nitroprusside
CC         NO donor) {ECO:0000269|PubMed:16373578};
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26859324,
CC       ECO:0000269|PubMed:27226593}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane
CC       protein. Endoplasmic reticulum membrane; Peripheral membrane
CC       protein.
CC   -!- INDUCTION: By cytokines and mitogens.
CC   -!- PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-
CC       nitrosylation may take place on different Cys residues in addition
CC       to Cys-526. {ECO:0000269|PubMed:16373578}.
CC   -!- MISCELLANEOUS: The conversion of arachidonate to prostaglandin H2
CC       is a 2 step reaction: a cyclooxygenase (COX) reaction which
CC       converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase
CC       reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The
CC       cyclooxygenase reaction occurs in a hydrophobic channel in the
CC       core of the enzyme. The peroxidase reaction occurs at a heme-
CC       containing active site located near the protein surface. The
CC       nonsteroidal anti-inflammatory drugs (NSAIDs) binding site
CC       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. PGHS1 is expressed constitutively and generally
CC       produces prostanoids acutely in response to hormonal stimuli to
CC       fine-tune physiological processes requiring instantaneous,
CC       continuous regulation (e.g. hemostasis). PGHS2 is inducible and
CC       typically produces prostanoids that mediate responses to
CC       physiological stresses such as infection and inflammation.
CC   -!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal
CC       anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen
CC       (PubMed:27710942, PubMed:26859324, PubMed:27226593). Aspirin is
CC       able to produce an irreversible inactivation of the enzyme through
CC       a serine acetylation (PubMed:26859324). Inhibition of the PGHSs
CC       with NSAIDs acutely reduces inflammation, pain, and fever, and
CC       long-term use of these drugs reduces fatal thrombotic events, as
CC       well as the development of colon cancer and Alzheimer's disease.
CC       PTGS2 is the principal isozyme responsible for production of
CC       inflammatory prostaglandins. New generation PTGSs inhibitors
CC       strive to be selective for PTGS2, to avoid side effects such as
CC       gastrointestinal complications and ulceration.
CC       {ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593,
CC       ECO:0000269|PubMed:27710942}.
CC   -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PTGS2ID509ch1q31.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ptgs2/";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/ptgs2/";
DR   EMBL; L15326; AAA35803.1; -; mRNA.
DR   EMBL; M90100; AAA58433.1; -; mRNA.
DR   EMBL; D28235; BAA05698.1; -; Genomic_DNA.
DR   EMBL; U04636; AAA57317.1; -; Genomic_DNA.
DR   EMBL; AY462100; AAR23927.1; -; mRNA.
DR   EMBL; AY229989; AAO38056.1; -; Genomic_DNA.
DR   EMBL; AY382629; AAQ75702.1; -; Genomic_DNA.
DR   EMBL; AK292167; BAF84856.1; -; mRNA.
DR   EMBL; AL033533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW91216.1; -; Genomic_DNA.
DR   EMBL; BC013734; AAH13734.1; -; mRNA.
DR   CCDS; CCDS1371.1; -.
DR   PIR; A46150; A46150.
DR   RefSeq; NP_000954.1; NM_000963.3.
DR   UniGene; Hs.196384; -.
DR   PDB; 1V0X; Model; -; A=1-604.
DR   PDB; 5F19; X-ray; 2.04 A; A/B=19-569.
DR   PDB; 5F1A; X-ray; 2.38 A; A/B=19-570.
DR   PDB; 5IKQ; X-ray; 2.41 A; A/B=19-569.
DR   PDB; 5IKR; X-ray; 2.34 A; A/B=19-569.
DR   PDB; 5IKT; X-ray; 2.45 A; A/B=19-569.
DR   PDB; 5IKV; X-ray; 2.51 A; A/B=19-569.
DR   PDB; 5KIR; X-ray; 2.70 A; A/B=19-569.
DR   PDBsum; 1V0X; -.
DR   PDBsum; 5F19; -.
DR   PDBsum; 5F1A; -.
DR   PDBsum; 5IKQ; -.
DR   PDBsum; 5IKR; -.
DR   PDBsum; 5IKT; -.
DR   PDBsum; 5IKV; -.
DR   PDBsum; 5KIR; -.
DR   ProteinModelPortal; P35354; -.
DR   SMR; P35354; -.
DR   BioGrid; 111715; 36.
DR   CORUM; P35354; -.
DR   DIP; DIP-28131N; -.
DR   IntAct; P35354; 2.
DR   STRING; 9606.ENSP00000356438; -.
DR   BindingDB; P35354; -.
DR   ChEMBL; CHEMBL230; -.
DR   DrugBank; DB03477; 1-Phenylsulfonamide-3-Trifluoromethyl-5-Parabromophenylpyrazole.
DR   DrugBank; DB00316; Acetaminophen.
DR   DrugBank; DB00945; Acetylsalicylic acid.
DR   DrugBank; DB00041; Aldesleukin.
DR   DrugBank; DB00233; Aminosalicylic Acid.
DR   DrugBank; DB01435; Antipyrine.
DR   DrugBank; DB01419; Antrafenine.
DR   DrugBank; DB01014; Balsalazide.
DR   DrugBank; DB00963; Bromfenac.
DR   DrugBank; DB00887; Bumetanide.
DR   DrugBank; DB06774; Capsaicin.
DR   DrugBank; DB00821; Carprofen.
DR   DrugBank; DB00482; Celecoxib.
DR   DrugBank; DB00856; Chlorphenesin.
DR   DrugBank; DB05095; Cimicoxib.
DR   DrugBank; DB00515; Cisplatin.
DR   DrugBank; DB00720; Clodronate.
DR   DrugBank; DB00250; Dapsone.
DR   DrugBank; DB05804; dehydroepiandrosterone sulfate.
DR   DrugBank; DB00035; Desmopressin.
DR   DrugBank; DB00586; Diclofenac.
DR   DrugBank; DB00861; Diflunisal.
DR   DrugBank; DB00154; Dihomo-gamma-linolenic acid.
DR   DrugBank; DB01395; Drospirenone.
DR   DrugBank; DB00005; Etanercept.
DR   DrugBank; DB00749; Etodolac.
DR   DrugBank; DB00773; Etoposide.
DR   DrugBank; DB01628; Etoricoxib.
DR   DrugBank; DB00573; Fenoprofen.
DR   DrugBank; DB09217; Firocoxib.
DR   DrugBank; DB02266; Flufenamic Acid.
DR   DrugBank; DB00712; Flurbiprofen.
DR   DrugBank; DB01404; Ginseng.
DR   DrugBank; DB01050; Ibuprofen.
DR   DrugBank; DB00159; Icosapent.
DR   DrugBank; DB00328; Indomethacin.
DR   DrugBank; DB01009; Ketoprofen.
DR   DrugBank; DB00465; Ketorolac.
DR   DrugBank; DB00480; Lenalidomide.
DR   DrugBank; DB04725; Licofelone.
DR   DrugBank; DB06725; Lornoxicam.
DR   DrugBank; DB01283; Lumiracoxib.
DR   DrugBank; DB01397; Magnesium salicylate.
DR   DrugBank; DB00939; Meclofenamic acid.
DR   DrugBank; DB00784; Mefenamic acid.
DR   DrugBank; DB00814; Meloxicam.
DR   DrugBank; DB00244; Mesalazine.
DR   DrugBank; DB00461; Nabumetone.
DR   DrugBank; DB00788; Naproxen.
DR   DrugBank; DB06802; Nepafenac.
DR   DrugBank; DB04552; Niflumic Acid.
DR   DrugBank; DB04743; Nimesulide.
DR   DrugBank; DB06804; Nonoxynol-9.
DR   DrugBank; DB00991; Oxaprozin.
DR   DrugBank; DB08439; Parecoxib.
DR   DrugBank; DB00812; Phenylbutazone.
DR   DrugBank; DB00554; Piroxicam.
DR   DrugBank; DB08910; Pomalidomide.
DR   DrugBank; DB03866; Prostaglandin G2.
DR   DrugBank; DB02709; Resveratrol.
DR   DrugBank; DB00884; Risedronate.
DR   DrugBank; DB00533; Rofecoxib.
DR   DrugBank; DB00936; Salicylic acid.
DR   DrugBank; DB01399; Salsalate.
DR   DrugBank; DB00360; Sapropterin.
DR   DrugBank; DB05875; substance P.
DR   DrugBank; DB00795; Sulfasalazine.
DR   DrugBank; DB00605; Sulindac.
DR   DrugBank; DB00870; Suprofen.
DR   DrugBank; DB08819; Tafluprost.
DR   DrugBank; DB00469; Tenoxicam.
DR   DrugBank; DB01041; Thalidomide.
DR   DrugBank; DB01600; Tiaprofenic acid.
DR   DrugBank; DB00500; Tolmetin.
DR   DrugBank; DB00620; Triamcinolone.
DR   DrugBank; DB01401; Trisalicylate-choline.
DR   DrugBank; DB00580; Valdecoxib.
DR   GuidetoPHARMACOLOGY; 1376; -.
DR   SwissLipids; SLP:000000830; -.
DR   PeroxiBase; 3321; HsPGHS02.
DR   iPTMnet; P35354; -.
DR   PhosphoSitePlus; P35354; -.
DR   BioMuta; PTGS2; -.
DR   DMDM; 3915797; -.
DR   EPD; P35354; -.
DR   MaxQB; P35354; -.
DR   PaxDb; P35354; -.
DR   PeptideAtlas; P35354; -.
DR   PRIDE; P35354; -.
DR   ProteomicsDB; 55035; -.
DR   DNASU; 5743; -.
DR   Ensembl; ENST00000367468; ENSP00000356438; ENSG00000073756.
DR   GeneID; 5743; -.
DR   KEGG; hsa:5743; -.
DR   UCSC; uc001gsb.4; human.
DR   CTD; 5743; -.
DR   DisGeNET; 5743; -.
DR   EuPathDB; HostDB:ENSG00000073756.11; -.
DR   GeneCards; PTGS2; -.
DR   HGNC; HGNC:9605; PTGS2.
DR   HPA; CAB000113; -.
DR   HPA; HPA001335; -.
DR   MIM; 600262; gene.
DR   neXtProt; NX_P35354; -.
DR   OpenTargets; ENSG00000073756; -.
DR   PharmGKB; PA293; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   eggNOG; ENOG410XPZ3; LUCA.
DR   GeneTree; ENSGT00390000010743; -.
DR   HOGENOM; HOG000013149; -.
DR   HOVERGEN; HBG000366; -.
DR   InParanoid; P35354; -.
DR   KO; K11987; -.
DR   OMA; CNNVKGC; -.
DR   OrthoDB; EOG091G03CD; -.
DR   PhylomeDB; P35354; -.
DR   TreeFam; TF329675; -.
DR   BioCyc; MetaCyc:HS01115-MONOMER; -.
DR   BRENDA; 1.14.99.1; 2681.
DR   Reactome; R-HSA-197264; Nicotinamide salvaging.
DR   Reactome; R-HSA-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR   Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR   Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
DR   Reactome; R-HSA-9018677; Biosynthesis of DHA-derived SPMs.
DR   Reactome; R-HSA-9018679; Biosynthesis of EPA-derived SPMs.
DR   Reactome; R-HSA-9025094; Biosynthesis of DPAn-3 SPMs.
DR   Reactome; R-HSA-9027604; Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives.
DR   SABIO-RK; P35354; -.
DR   SIGNOR; P35354; -.
DR   UniPathway; UPA00662; -.
DR   GeneWiki; Prostaglandin-endoperoxide_synthase_2; -.
DR   GeneWiki; PTGS2; -.
DR   GenomeRNAi; 5743; -.
DR   PRO; PR:P35354; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000073756; -.
DR   CleanEx; HS_PTGS2; -.
DR   ExpressionAtlas; P35354; baseline and differential.
DR   Genevisible; P35354; HS.
DR   GO; GO:0005901; C:caveola; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; TAS:Reactome.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
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; TAS:Reactome.
DR   GO; GO:0004601; F:peroxidase activity; TAS:Reactome.
DR   GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR   GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
DR   GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
DR   GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
DR   GO; GO:0071284; P:cellular response to lead ion; IEA:Ensembl.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0071471; P:cellular response to non-ionic osmotic stress; IEA:Ensembl.
DR   GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR   GO; GO:0019371; P:cyclooxygenase pathway; IDA:BHF-UCL.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0042633; P:hair cycle; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0007612; P:learning; IEA:Ensembl.
DR   GO; GO:0019372; P:lipoxygenase pathway; TAS:Reactome.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; TAS:Reactome.
DR   GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
DR   GO; GO:0097756; P:negative regulation of blood vessel diameter; IEA:Ensembl.
DR   GO; GO:0051926; P:negative regulation of calcium ion transport; IEA:Ensembl.
DR   GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
DR   GO; GO:0045986; P:negative regulation of smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IEA:Ensembl.
DR   GO; GO:0030728; P:ovulation; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:BHF-UCL.
DR   GO; GO:0031622; P:positive regulation of fever generation; ISS:BHF-UCL.
DR   GO; GO:0090271; P:positive regulation of fibroblast growth factor production; ISS:BHF-UCL.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:BHF-UCL.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:0090362; P:positive regulation of platelet-derived growth factor production; ISS:BHF-UCL.
DR   GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; NAS:BHF-UCL.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0031915; P:positive regulation of synaptic plasticity; IEA:Ensembl.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR   GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISS:BHF-UCL.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISS:BHF-UCL.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0050727; P:regulation of inflammatory response; NAS:UniProtKB.
DR   GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
DR   GO; GO:0009750; P:response to fructose; IEA:Ensembl.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
DR   GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR   GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR   Gene3D; 1.10.640.10; -; 1.
DR   InterPro; IPR029576; COX-2.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR010255; Haem_peroxidase.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR037120; Haem_peroxidase_sf.
DR   PANTHER; PTHR11903:SF8; PTHR11903:SF8; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00008; EGF; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Dioxygenase; Disulfide bond;
KW   Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Glycoprotein; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Metal-binding; Microsome; Oxidoreductase; Peroxidase;
KW   Polymorphism; Prostaglandin biosynthesis; Prostaglandin metabolism;
KW   Reference proteome; S-nitrosylation; Signal.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18    604       Prostaglandin G/H synthase 2.
FT                                /FTId=PRO_0000023875.
FT   DOMAIN       18     55       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   ACT_SITE    193    193       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   ACT_SITE    371    371       For cyclooxygenase activity.
FT                                {ECO:0000250|UniProtKB:Q05769}.
FT   METAL       374    374       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   BINDING     106    106       Substrate.
FT                                {ECO:0000250|UniProtKB:Q05769}.
FT   BINDING     341    341       Substrate.
FT                                {ECO:0000250|UniProtKB:Q05769}.
FT   SITE        516    516       Aspirin-acetylated serine.
FT                                {ECO:0000269|PubMed:26859324}.
FT   MOD_RES     526    526       S-nitrosocysteine.
FT                                {ECO:0000305|PubMed:16373578}.
FT   CARBOHYD     53     53       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:5F19,
FT                                ECO:0000244|PDB:5F1A,
FT                                ECO:0000244|PDB:5IKQ,
FT                                ECO:0000244|PDB:5IKT,
FT                                ECO:0000269|PubMed:26859324,
FT                                ECO:0000269|PubMed:27226593}.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:5F19,
FT                                ECO:0000244|PDB:5F1A,
FT                                ECO:0000244|PDB:5IKQ,
FT                                ECO:0000244|PDB:5IKR,
FT                                ECO:0000244|PDB:5IKT,
FT                                ECO:0000244|PDB:5IKV,
FT                                ECO:0000244|PDB:5KIR,
FT                                ECO:0000269|PubMed:26859324,
FT                                ECO:0000269|PubMed:27226593,
FT                                ECO:0000269|PubMed:27710942}.
FT   CARBOHYD    396    396       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:5F19,
FT                                ECO:0000244|PDB:5F1A,
FT                                ECO:0000244|PDB:5IKQ,
FT                                ECO:0000244|PDB:5IKR,
FT                                ECO:0000244|PDB:5IKT,
FT                                ECO:0000244|PDB:5IKV,
FT                                ECO:0000244|PDB:5KIR,
FT                                ECO:0000269|PubMed:26859324,
FT                                ECO:0000269|PubMed:27226593,
FT                                ECO:0000269|PubMed:27710942}.
FT   CARBOHYD    580    580       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17113084}.
FT   DISULFID     21     32       {ECO:0000244|PDB:5F19,
FT                                ECO:0000244|PDB:5F1A,
FT                                ECO:0000244|PDB:5IKQ,
FT                                ECO:0000244|PDB:5IKR,
FT                                ECO:0000244|PDB:5IKT,
FT                                ECO:0000244|PDB:5IKV,
FT                                ECO:0000244|PDB:5KIR,
FT                                ECO:0000269|PubMed:26859324,
FT                                ECO:0000269|PubMed:27226593,
FT                                ECO:0000269|PubMed:27710942}.
FT   DISULFID     22    145       {ECO:0000244|PDB:5F19,
FT                                ECO:0000244|PDB:5F1A,
FT                                ECO:0000244|PDB:5IKQ,
FT                                ECO:0000244|PDB:5IKR,
FT                                ECO:0000244|PDB:5IKT,
FT                                ECO:0000244|PDB:5IKV,
FT                                ECO:0000244|PDB:5KIR,
FT                                ECO:0000269|PubMed:26859324,
FT                                ECO:0000269|PubMed:27226593,
FT                                ECO:0000269|PubMed:27710942}.
FT   DISULFID     26     42       {ECO:0000244|PDB:5F19,
FT                                ECO:0000244|PDB:5F1A,
FT                                ECO:0000244|PDB:5IKQ,
FT                                ECO:0000244|PDB:5IKR,
FT                                ECO:0000244|PDB:5IKT,
FT                                ECO:0000244|PDB:5IKV,
FT                                ECO:0000244|PDB:5KIR,
FT                                ECO:0000269|PubMed:26859324,
FT                                ECO:0000269|PubMed:27226593,
FT                                ECO:0000269|PubMed:27710942}.
FT   DISULFID     44     54       {ECO:0000244|PDB:5F19,
FT                                ECO:0000244|PDB:5F1A,
FT                                ECO:0000244|PDB:5IKQ,
FT                                ECO:0000244|PDB:5IKR,
FT                                ECO:0000244|PDB:5IKT,
FT                                ECO:0000244|PDB:5IKV,
FT                                ECO:0000244|PDB:5KIR,
FT                                ECO:0000269|PubMed:26859324,
FT                                ECO:0000269|PubMed:27226593,
FT                                ECO:0000269|PubMed:27710942}.
FT   DISULFID    555    561       {ECO:0000244|PDB:5F19,
FT                                ECO:0000244|PDB:5F1A,
FT                                ECO:0000244|PDB:5IKQ,
FT                                ECO:0000244|PDB:5IKR,
FT                                ECO:0000244|PDB:5IKT,
FT                                ECO:0000244|PDB:5IKV,
FT                                ECO:0000244|PDB:5KIR,
FT                                ECO:0000269|PubMed:26859324,
FT                                ECO:0000269|PubMed:27226593,
FT                                ECO:0000269|PubMed:27710942}.
FT   VARIANT     228    228       R -> H (in dbSNP:rs3218622).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_016262.
FT   VARIANT     428    428       P -> A (in dbSNP:rs4648279).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_016263.
FT   VARIANT     488    488       E -> G (in dbSNP:rs5272).
FT                                /FTId=VAR_011980.
FT   VARIANT     511    511       V -> A (in dbSNP:rs5273).
FT                                {ECO:0000269|PubMed:15308583,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_011981.
FT   VARIANT     587    587       G -> R (in dbSNP:rs3218625).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_016264.
FT   MUTAGEN     371    371       Y->A: Decreased protein stability.
FT                                Increased decrease of protein stability;
FT                                when associated with A-516.
FT                                {ECO:0000269|PubMed:27226593}.
FT   MUTAGEN     516    516       S->A: No effect on protein stability.
FT                                Increased decrease of protein stability;
FT                                when associated with A-371.
FT                                {ECO:0000269|PubMed:27226593}.
FT   MUTAGEN     516    516       S->T: Decreased enzyme activity with
FT                                arachidonic acid. Loss of cyclooxygenase
FT                                activity; when associated with V-519.
FT                                {ECO:0000269|PubMed:26859324}.
FT   MUTAGEN     519    519       G->V: Loss of cyclooxygenase activity.
FT                                Loss of cyclooxygenase activity; when
FT                                associated with T-516.
FT                                {ECO:0000269|PubMed:26859324}.
FT   MUTAGEN     526    526       C->S: Prevents activation by nitric oxid
FT                                (NO). {ECO:0000269|PubMed:16373578}.
FT   MUTAGEN     555    555       C->S: Abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:16373578}.
FT   MUTAGEN     561    561       C->S: Does not affect activation by
FT                                nitric oxid (NO).
FT                                {ECO:0000269|PubMed:16373578}.
FT   CONFLICT    165    165       E -> G (in Ref. 2; AAA58433).
FT                                {ECO:0000305}.
FT   CONFLICT    438    438       I -> T (in Ref. 1; AAA35803).
FT                                {ECO:0000305}.
FT   TURN         20     23       {ECO:0000244|PDB:5F19}.
FT   STRAND       31     35       {ECO:0000244|PDB:5F19}.
FT   TURN         36     38       {ECO:0000244|PDB:5F19}.
FT   STRAND       39     43       {ECO:0000244|PDB:5F19}.
FT   STRAND       47     50       {ECO:0000244|PDB:5F19}.
FT   TURN         51     54       {ECO:0000244|PDB:5F19}.
FT   HELIX        59     66       {ECO:0000244|PDB:5F19}.
FT   HELIX        71     78       {ECO:0000244|PDB:5F19}.
FT   HELIX        82     89       {ECO:0000244|PDB:5F19}.
FT   HELIX        92    107       {ECO:0000244|PDB:5F19}.
FT   STRAND      120    122       {ECO:0000244|PDB:5F19}.
FT   HELIX       125    129       {ECO:0000244|PDB:5F19}.
FT   STRAND      135    138       {ECO:0000244|PDB:5F19}.
FT   STRAND      150    153       {ECO:0000244|PDB:5F19}.
FT   HELIX       160    167       {ECO:0000244|PDB:5F19}.
FT   HELIX       182    192       {ECO:0000244|PDB:5F19}.
FT   TURN        193    195       {ECO:0000244|PDB:5F19}.
FT   TURN        200    202       {ECO:0000244|PDB:5F19}.
FT   STRAND      206    208       {ECO:0000244|PDB:5F19}.
FT   HELIX       217    220       {ECO:0000244|PDB:5F19}.
FT   HELIX       224    230       {ECO:0000244|PDB:5F19}.
FT   STRAND      241    243       {ECO:0000244|PDB:5F19}.
FT   STRAND      246    248       {ECO:0000244|PDB:5F19}.
FT   HELIX       252    255       {ECO:0000244|PDB:5F19}.
FT   HELIX       267    269       {ECO:0000244|PDB:5F19}.
FT   TURN        276    279       {ECO:0000244|PDB:5F19}.
FT   HELIX       282    305       {ECO:0000244|PDB:5F19}.
FT   HELIX       311    332       {ECO:0000244|PDB:5F19}.
FT   HELIX       334    339       {ECO:0000244|PDB:5F19}.
FT   HELIX       349    352       {ECO:0000244|PDB:5F19}.
FT   HELIX       365    370       {ECO:0000244|PDB:5F19}.
FT   HELIX       374    376       {ECO:0000244|PDB:5F19}.
FT   STRAND      379    383       {ECO:0000244|PDB:5F19}.
FT   STRAND      386    388       {ECO:0000244|PDB:5F19}.
FT   HELIX       390    393       {ECO:0000244|PDB:5F19}.
FT   HELIX       398    414       {ECO:0000244|PDB:5F19}.
FT   STRAND      420    424       {ECO:0000244|PDB:5F19}.
FT   HELIX       428    430       {ECO:0000244|PDB:5F19}.
FT   HELIX       431    443       {ECO:0000244|PDB:5F19}.
FT   HELIX       449    455       {ECO:0000244|PDB:5F19}.
FT   HELIX       464    468       {ECO:0000244|PDB:5F19}.
FT   STRAND      469    471       {ECO:0000244|PDB:5F19}.
FT   HELIX       472    481       {ECO:0000244|PDB:5F19}.
FT   HELIX       484    486       {ECO:0000244|PDB:5F19}.
FT   HELIX       489    495       {ECO:0000244|PDB:5F19}.
FT   STRAND      503    505       {ECO:0000244|PDB:5F19}.
FT   HELIX       506    521       {ECO:0000244|PDB:5F19}.
FT   HELIX       524    526       {ECO:0000244|PDB:5F19}.
FT   TURN        528    530       {ECO:0000244|PDB:5F19}.
FT   HELIX       533    536       {ECO:0000244|PDB:5F19}.
FT   HELIX       539    546       {ECO:0000244|PDB:5F19}.
FT   HELIX       550    557       {ECO:0000244|PDB:5F19}.
SQ   SEQUENCE   604 AA;  68996 MW;  72FBD699F6128519 CRC64;
     MLARALLLCA VLALSHTANP CCSHPCQNRG VCMSVGFDQY KCDCTRTGFY GENCSTPEFL
     TRIKLFLKPT PNTVHYILTH FKGFWNVVNN IPFLRNAIMS YVLTSRSHLI DSPPTYNADY
     GYKSWEAFSN LSYYTRALPP VPDDCPTPLG VKGKKQLPDS NEIVEKLLLR RKFIPDPQGS
     NMMFAFFAQH FTHQFFKTDH KRGPAFTNGL GHGVDLNHIY GETLARQRKL RLFKDGKMKY
     QIIDGEMYPP TVKDTQAEMI YPPQVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD
     VLKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNKQFQYQ
     NRIAAEFNTL YHWHPLLPDT FQIHDQKYNY QQFIYNNSIL LEHGITQFVE SFTRQIAGRV
     AGGRNVPPAV QKVSQASIDQ SRQMKYQSFN EYRKRFMLKP YESFEELTGE KEMSAELEAL
     YGDIDAVELY PALLVEKPRP DAIFGETMVE VGAPFSLKGL MGNVICSPAY WKPSTFGGEV
     GFQIINTASI QSLICNNVKG CPFTSFSVPD PELIKTVTIN ASSSRSGLDD INPTVLLKER
     STEL
//
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