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 03-AUG-2022, entry version 223.
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 in the biosynthesis
CC pathway of prostanoids, a class of C20 oxylipins mainly derived from
CC arachidonate, with a particular role in the inflammatory response. The
CC cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the
CC hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase
CC activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor
CC of all 2-series prostaglandins and thromboxanes. This complex
CC transformation is initiated by abstraction of hydrogen at carbon 13
CC (with S-stereochemistry), followed by insertion of molecular O2 to form
CC 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). {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 -!- 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/";
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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. [P23219-4]
DR PDB; 6Y3C; X-ray; 3.36 A; A=24-599.
DR PDBsum; 6Y3C; -.
DR AlphaFoldDB; P23219; -.
DR SMR; P23219; -.
DR BioGRID; 111714; 11.
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; DB00619; Imatinib.
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; 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 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; P23219; -.
DR PeptideAtlas; P23219; -.
DR PRIDE; P23219; -.
DR ProteomicsDB; 4239; -.
DR ProteomicsDB; 54063; -. [P23219-1]
DR ProteomicsDB; 54064; -. [P23219-2]
DR Antibodypedia; 775; 704 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 CTD; 5742; -.
DR DisGeNET; 5742; -.
DR GeneCards; PTGS1; -.
DR HGNC; HGNC:9604; PTGS1.
DR HPA; ENSG00000095303; Tissue enhanced (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; YNTSMLM; -.
DR OrthoDB; 324380at2759; -.
DR PhylomeDB; P23219; -.
DR TreeFam; TF329675; -.
DR BioCyc; MetaCyc:HS01815-MON; -.
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; 5 hits in 1084 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 179 other 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:0006954; P:inflammatory response; IEA:InterPro.
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 Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR029580; COX-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:SF6; PTHR11903:SF6; 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; 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
