ID   Q543T1_MOUSE            Unreviewed;       602 AA.
AC   Q543T1; Q8CIL6;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Prostaglandin G/H synthase 1 {ECO:0000256|ARBA:ARBA00020404};
DE            EC=1.14.99.1 {ECO:0000256|ARBA:ARBA00012440};
DE   AltName: Full=Cyclooxygenase-1 {ECO:0000256|ARBA:ARBA00031217};
DE   AltName: Full=Prostaglandin H2 synthase 1 {ECO:0000256|ARBA:ARBA00031794};
DE   AltName: Full=Prostaglandin-endoperoxide synthase 1 {ECO:0000256|ARBA:ARBA00033143};
GN   Name=Ptgs1 {ECO:0000313|EMBL:AAH23322.2, ECO:0000313|MGI:MGI:97797};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAC32737.1};
RN   [1] {ECO:0000313|EMBL:BAC32737.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32737.1}, and NOD
RC   {ECO:0000313|EMBL:BAE41780.1};
RC   TISSUE=Adipose {ECO:0000313|EMBL:BAE37419.1}, Corpora quadrigemina
RC   {ECO:0000313|EMBL:BAC32737.1}, Heart {ECO:0000313|EMBL:BAE25179.1},
RC   and Hypothalamus {ECO:0000313|EMBL:BAE23660.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAC32737.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32737.1}, and NOD
RC   {ECO:0000313|EMBL:BAE41780.1};
RC   TISSUE=Adipose {ECO:0000313|EMBL:BAE37419.1}, Corpora quadrigemina
RC   {ECO:0000313|EMBL:BAC32737.1}, Heart {ECO:0000313|EMBL:BAE25179.1},
RC   and Hypothalamus {ECO:0000313|EMBL:BAE23660.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAC32737.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32737.1}, and NOD
RC   {ECO:0000313|EMBL:BAE41780.1};
RC   TISSUE=Adipose {ECO:0000313|EMBL:BAE37419.1}, Corpora quadrigemina
RC   {ECO:0000313|EMBL:BAC32737.1}, Heart {ECO:0000313|EMBL:BAE25179.1},
RC   and Hypothalamus {ECO:0000313|EMBL:BAE23660.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAC32737.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32737.1}, and NOD
RC   {ECO:0000313|EMBL:BAE41780.1};
RC   TISSUE=Adipose {ECO:0000313|EMBL:BAE37419.1}, Corpora quadrigemina
RC   {ECO:0000313|EMBL:BAC32737.1}, Heart {ECO:0000313|EMBL:BAE25179.1},
RC   and Hypothalamus {ECO:0000313|EMBL:BAE23660.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAC32737.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32737.1};
RC   TISSUE=Corpora quadrigemina {ECO:0000313|EMBL:BAC32737.1};
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K.,
RA   Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y.,
RA   Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T.,
RA   Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R.,
RA   Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K.,
RA   Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S.,
RA   Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M.,
RA   Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:BAC32737.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32737.1}, and NOD
RC   {ECO:0000313|EMBL:BAE41780.1};
RC   TISSUE=Adipose {ECO:0000313|EMBL:BAE37419.1}, Corpora quadrigemina
RC   {ECO:0000313|EMBL:BAC32737.1}, Heart {ECO:0000313|EMBL:BAE25179.1},
RC   and Hypothalamus {ECO:0000313|EMBL:BAE23660.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7] {ECO:0000313|EMBL:AAH23322.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000313|EMBL:AAH23322.2};
RC   TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old
RC   virgin mouse. Taken by biopsy. {ECO:0000313|EMBL:AAH23322.2};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [8] {ECO:0000313|EMBL:BAE23660.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23660.1}, and NOD
RC   {ECO:0000313|EMBL:BAE41780.1};
RC   TISSUE=Adipose {ECO:0000313|EMBL:BAE37419.1}, Heart
RC   {ECO:0000313|EMBL:BAE25179.1}, and Hypothalamus
RC   {ECO:0000313|EMBL:BAE23660.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:BAC32737.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32737.1}, and NOD
RC   {ECO:0000313|EMBL:BAE41780.1};
RC   TISSUE=Adipose {ECO:0000313|EMBL:BAE37419.1}, Corpora quadrigemina
RC   {ECO:0000313|EMBL:BAC32737.1}, Heart {ECO:0000313|EMBL:BAE25179.1},
RC   and Hypothalamus {ECO:0000313|EMBL:BAE23660.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [10] {ECO:0000313|EMBL:BAC32737.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32737.1}, and NOD
RC   {ECO:0000313|EMBL:BAE41780.1};
RC   TISSUE=Adipose {ECO:0000313|EMBL:BAE37419.1}, Corpora quadrigemina
RC   {ECO:0000313|EMBL:BAC32737.1}, Heart {ECO:0000313|EMBL:BAE25179.1},
RC   and Hypothalamus {ECO:0000313|EMBL:BAE23660.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [11] {ECO:0000313|EMBL:CAJ18522.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA   Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12] {ECO:0000313|EMBL:ABA19088.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/J {ECO:0000313|EMBL:ABA19089.1}, and C3H/HeJ
RC   {ECO:0000313|EMBL:ABA19088.1};
RX   PubMed=17454003; DOI=10.1080/10425170701207166;
RA   Li X., Fleis R.I., Shubitowski D.M., Ramadas R.A., Ewart S.L.;
RT   "Fine mapping of murine asthma quantitative trait loci and analyses of
RT   Ptgs1 and Mrc1 as positional candidate genes.";
RL   DNA Seq. 18:190-195(2007).
RN   [13] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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:0000256|ARBA:ARBA00000144};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597;
CC         Evidence={ECO:0000256|ARBA:ARBA00000144};
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:0000256|ARBA:ARBA00001779};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729;
CC         Evidence={ECO:0000256|ARBA:ARBA00001779};
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:0000256|ARBA:ARBA00036409};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456;
CC         Evidence={ECO:0000256|ARBA:ARBA00036409};
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:0000256|ARBA:ARBA00036358};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452;
CC         Evidence={ECO:0000256|ARBA:ARBA00036358};
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:0000256|ARBA:ARBA00036313};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448;
CC         Evidence={ECO:0000256|ARBA:ARBA00036313};
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:0000256|ARBA:ARBA00035976};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460;
CC         Evidence={ECO:0000256|ARBA:ARBA00035976};
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:0000256|ARBA:ARBA00000489};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601;
CC         Evidence={ECO:0000256|ARBA:ARBA00000489};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004702}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004174}.
CC   -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
CC       {ECO:0000256|ARBA:ARBA00008928}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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; BC023322; AAH23322.2; -; mRNA.
DR   EMBL; AH015269; ABA19088.1; -; Genomic_DNA.
DR   EMBL; DQ173708; ABA19088.1; JOINED; Genomic_DNA.
DR   EMBL; DQ173710; ABA19088.1; JOINED; Genomic_DNA.
DR   EMBL; DQ173711; ABA19088.1; JOINED; Genomic_DNA.
DR   EMBL; DQ173712; ABA19088.1; JOINED; Genomic_DNA.
DR   EMBL; DQ173713; ABA19088.1; JOINED; Genomic_DNA.
DR   EMBL; DQ173714; ABA19088.1; JOINED; Genomic_DNA.
DR   EMBL; AH015270; ABA19089.1; -; Genomic_DNA.
DR   EMBL; DQ173699; ABA19089.1; JOINED; Genomic_DNA.
DR   EMBL; DQ173700; ABA19089.1; JOINED; Genomic_DNA.
DR   EMBL; DQ173701; ABA19089.1; JOINED; Genomic_DNA.
DR   EMBL; DQ173702; ABA19089.1; JOINED; Genomic_DNA.
DR   EMBL; DQ173703; ABA19089.1; JOINED; Genomic_DNA.
DR   EMBL; DQ173704; ABA19089.1; JOINED; Genomic_DNA.
DR   EMBL; AK046457; BAC32737.1; -; mRNA.
DR   EMBL; AK138432; BAE23660.1; -; mRNA.
DR   EMBL; AK142741; BAE25179.1; -; mRNA.
DR   EMBL; AK159907; BAE35471.1; -; mRNA.
DR   EMBL; AK163609; BAE37419.1; -; mRNA.
DR   EMBL; AK170414; BAE41780.1; -; mRNA.
DR   EMBL; AK170664; BAE41945.1; -; mRNA.
DR   EMBL; CT010314; CAJ18522.1; -; mRNA.
DR   RefSeq; NP_032995.1; NM_008969.4.
DR   RefSeq; XP_006497853.1; XM_006497790.3.
DR   RefSeq; XP_006497854.1; XM_006497791.3.
DR   RefSeq; XP_011237338.1; XM_011239036.2.
DR   RefSeq; XP_017171985.1; XM_017316496.1.
DR   AlphaFoldDB; Q543T1; -.
DR   SMR; Q543T1; -.
DR   GlyCosmos; Q543T1; 3 sites, No reported glycans.
DR   MaxQB; Q543T1; -.
DR   Antibodypedia; 775; 774 antibodies from 45 providers.
DR   DNASU; 19224; -.
DR   GeneID; 19224; -.
DR   KEGG; mmu:19224; -.
DR   AGR; MGI:97797; -.
DR   CTD; 5742; -.
DR   MGI; MGI:97797; Ptgs1.
DR   VEuPathDB; HostDB:ENSMUSG00000047250; -.
DR   HOGENOM; CLU_022428_0_0_1; -.
DR   OMA; LFGSQFQ; -.
DR   OrthoDB; 1086441at2759; -.
DR   UniPathway; UPA00662; -.
DR   BioGRID-ORCS; 19224; 5 hits in 81 CRISPR screens.
DR   ChiTaRS; Ptgs1; mouse.
DR   ExpressionAtlas; Q543T1; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019371; P:cyclooxygenase pathway; 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   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585};
KW   Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..602
FT                   /note="Prostaglandin G/H synthase 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014309561"
FT   DOMAIN          34..72
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   ACT_SITE        209
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT   ACT_SITE        387
FT                   /note="For cyclooxygenase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT   BINDING         390
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:0000256|PIRSR:PIRSR619791-2"
SQ   SEQUENCE   602 AA;  69042 MW;  634C0E602045C3A0 CRC64;
     MSRRSLSLWF PLLLLLLLPP TPSVLLADPG VPSPVNPCCY YPCQNQGVCV RFGLDNYQCD
     CTRTGYSGPN CTIPEIWTWL RNSLRPSPSF THFLLTHGYW LWEFVNATFI REVLMRLVLT
     VRSNLIPSPP TYNSAHDYIS WESFSNVSYY TRILPSVPKD CPTPMGTKGK KQLPDVQLLA
     QQLLLRREFI PAPQGTNILF AFFAQHFTHQ FFKTSGKMGP GFTKALGHGV DLGHIYGDNL
     ERQYHLRLFK DGKLKYQVLD GEVYPPSVEQ ASVLMRYPPG VPPERQMAVG QEVFGLLPGL
     MLFSTIWLRE HNRVCDLLKE EHPTWDDEQL FQTTRLILIG ETIKIVIEEY VQHLSGYFLQ
     LKFDPELLFR AQFQYRNRIA MEFNHLYHWH PLMPNSFQVG SQEYSYEQFL FNTSMLVDYG
     VEALVDAFSR QRAGRIGGGR NFDYHVLHVA VDVIKESREM RLQPFNEYRK RFGLKPYTSF
     QELTGEKEMA AELEELYGDI DALEFYPGLL LEKCQPNSIF GESMIEMGAP FSLKGLLGNP
     ICSPEYWKPS TFGGDVGFNL VNTASLKKLV CLNTKTCPYV SFRVPDYPGD DGSVLVRRST
     EL
//