ID   Q5RI06_DANRE            Unreviewed;       606 AA.
AC   Q5RI06; A4QNY4;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Prostaglandin G/H synthase 2 {ECO:0000256|ARBA:ARBA00020406};
DE            EC=1.14.99.1 {ECO:0000256|ARBA:ARBA00012440};
DE   AltName: Full=Cyclooxygenase-2 {ECO:0000256|ARBA:ARBA00031216};
DE   AltName: Full=PHS II {ECO:0000256|ARBA:ARBA00030839};
DE   AltName: Full=Prostaglandin H2 synthase 2 {ECO:0000256|ARBA:ARBA00031793};
DE   AltName: Full=Prostaglandin-endoperoxide synthase 2 {ECO:0000256|ARBA:ARBA00033144};
GN   Name=ptgs2b {ECO:0000313|EMBL:AAI39569.1,
GN   ECO:0000313|Ensembl:ENSDARP00000003684,
GN   ECO:0000313|ZFIN:ZDB-GENE-041014-323};
GN   Synonyms=si:dkey-97o5.6 {ECO:0000313|RefSeq:NP_001020675.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI39569.1};
RN   [1] {ECO:0000313|EMBL:ABF50051.1, ECO:0000313|RefSeq:NP_001020675.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17112475; DOI=10.1016/j.bbrc.2006.11.007;
RA   Ishikawa T.O., Griffin K.J., Banerjee U., Herschman H.R.;
RT   "The zebrafish genome contains two inducible, functional cyclooxygenase-2
RT   genes.";
RL   Biochem. Biophys. Res. Commun. 352:181-187(2007).
RN   [2] {ECO:0000313|RefSeq:NP_001020675.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17471498;
RA   Ishikawa T.O., Herschman H.R.;
RT   "Two inducible, functional cyclooxygenase-2 genes are present in the
RT   rainbow trout genome.";
RL   J. Cell. Biochem. 102:1486-1492(2007).
RN   [3] {ECO:0000313|RefSeq:NP_001020675.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17256142; DOI=10.1007/s00438-007-0207-3;
RA   McPartland J.M., Glass M., Matias I., Norris R.W., Kilpatrick C.W.;
RT   "A shifted repertoire of endocannabinoid genes in the zebrafish (Danio
RT   rerio).";
RL   Mol. Genet. Genomics 277:555-570(2007).
RN   [4] {ECO:0000313|EMBL:AAI39569.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Singapore local strain {ECO:0000313|EMBL:AAI39569.1};
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAI39569.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|RefSeq:NP_001020675.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18272595;
RA   Scherz P.J., Huisken J., Sahai-Hernandez P., Stainier D.Y.;
RT   "High-speed imaging of developing heart valves reveals interplay of
RT   morphogenesis and function.";
RL   Development 135:1179-1187(2008).
RN   [6] {ECO:0000313|RefSeq:NP_001020675.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18718920; DOI=10.1093/molbev/msn183;
RA   Havird J.C., Miyamoto M.M., Choe K.P., Evans D.H.;
RT   "Gene duplications and losses within the cyclooxygenase family of teleosts
RT   and other chordates.";
RL   Mol. Biol. Evol. 25:2349-2359(2008).
RN   [7] {ECO:0000313|Ensembl:ENSDARP00000003684, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000003684};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [8] {ECO:0000313|Ensembl:ENSDARP00000003684}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000003684};
RG   Ensembl;
RL   Submitted (AUG-2013) to UniProtKB.
RN   [9] {ECO:0000313|RefSeq:NP_001020675.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29689525;
RA   Forner-Piquer I., Santangeli S., Maradonna F., Verde R., Piscitelli F.,
RA   di Marzo V., Habibi H.R., Carnevali O.;
RT   "Role of Bisphenol A on the Endocannabinoid System at central and
RT   peripheral levels: Effects on adult female zebrafish.";
RL   Chemosphere 205:118-125(2018).
RN   [10] {ECO:0000313|RefSeq:NP_001020675.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29793103;
RA   Forner-Piquer I., Santangeli S., Maradonna F., Rabbito A., Piscitelli F.,
RA   Habibi H.R., Di Marzo V., Carnevali O.;
RT   "Disruption of the gonadal endocannabinoid system in zebrafish exposed to
RT   diisononyl phthalate.";
RL   Environ. Pollut. 241:1-8(2018).
RN   [11] {ECO:0000313|RefSeq:NP_001020675.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29679858;
RA   Kim E.A., Kim S.Y., Ye B.R., Kim J., Ko S.C., Lee W.W., Kim K.N.,
RA   Choi I.W., Jung W.K., Heo S.J.;
RT   "Anti-inflammatory effect of Apo-9'-fucoxanthinone via inhibition of MAPKs
RT   and NF-kB signaling pathway in LPS-stimulated RAW 264.7 macrophages and
RT   zebrafish model.";
RL   Int. Immunopharmacol. 59:339-346(2018).
RN   [12] {ECO:0000313|RefSeq:NP_001020675.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30143654;
RA   Lopez-Munoz A., Nicolas F.E., Garcia-Moreno D., Perez-Oliva A.B.,
RA   Navarro-Mendoza M.I., Hernandez-Onate M.A., Herrera-Estrella A.,
RA   Torres-Martinez S., Ruiz-Vazquez R.M., Garre V., Mulero V.;
RT   "An Adult Zebrafish Model Reveals that Mucormycosis Induces Apoptosis of
RT   Infected Macrophages.";
RL   Sci. Rep. 8:12802-12802(2018).
RN   [13] {ECO:0000313|RefSeq:NP_001020675.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30685088;
RA   Li W., Jin D., Zhong T.P.;
RT   "Photoreceptor cell development requires prostaglandin signaling in the
RT   zebrafish retina.";
RL   Biochem. Biophys. Res. Commun. 510:230-235(2019).
RN   [14] {ECO:0000313|RefSeq:NP_001020675.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- 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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. 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}.
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DR   EMBL; BX323056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC139568; AAI39569.1; -; mRNA.
DR   EMBL; DQ494791; ABF50051.1; -; mRNA.
DR   RefSeq; NP_001020675.1; NM_001025504.2.
DR   STRING; 7955.ENSDARP00000003684; -.
DR   PaxDb; 7955-ENSDARP00000003684; -.
DR   Ensembl; ENSDART00000010028; ENSDARP00000003684; ENSDARG00000010276.
DR   Ensembl; ENSDART00000010028.10; ENSDARP00000003684.8; ENSDARG00000010276.10.
DR   GeneID; 559020; -.
DR   KEGG; dre:559020; -.
DR   AGR; ZFIN:ZDB-GENE-041014-323; -.
DR   CTD; 559020; -.
DR   ZFIN; ZDB-GENE-041014-323; ptgs2b.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_022428_0_0_1; -.
DR   OMA; NVHYGYK; -.
DR   OrthoDB; 1086441at2759; -.
DR   TreeFam; TF329675; -.
DR   Reactome; R-DRE-197264; Nicotinamide salvaging.
DR   Reactome; R-DRE-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR   Reactome; R-DRE-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   Reactome; R-DRE-9018677; Biosynthesis of DHA-derived SPMs.
DR   Reactome; R-DRE-9018679; Biosynthesis of EPA-derived SPMs.
DR   Reactome; R-DRE-9025094; Biosynthesis of DPAn-3 SPMs.
DR   Reactome; R-DRE-9027604; Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives.
DR   UniPathway; UPA00662; -.
DR   Proteomes; UP000000437; Chromosome 20.
DR   Bgee; ENSDARG00000010276; Expressed in pharyngeal gill and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
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; IDA:ZFIN.
DR   GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IBA:GO_Central.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:ZFIN.
DR   GO; GO:0019371; P:cyclooxygenase pathway; IBA:GO_Central.
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:SF8; PROSTAGLANDIN G_H SYNTHASE 2; 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   2: Evidence at transcript level;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   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   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001020675.1}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..606
FT                   /note="Prostaglandin G/H synthase 2"
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_001020675.1"
FT                   /id="PRO_5035034339"
FT   DOMAIN          19..57
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          582..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT   ACT_SITE        373
FT                   /note="For cyclooxygenase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT   BINDING         376
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   606 AA;  69465 MW;  C0601EA49A06EA6A CRC64;
     MKSSVLFIFL LLGFVVCTGA NPCCSHPCQN RGVCTEMGSD AYECDCTRTG YYGQNCTTPE
     FLTWVKVSLK PSPNTVHYIL THFKSLWNII NNVSFLRNGI MRYVLTSRAH LIDSPPTFNA
     DYGYKSWEAY SNLSYYTRTL PPVPRDCPTP MGVAGKKELP DVKMLAEKLL LRRKFIPDPQ
     RTNLMFAFFA QHFTHQFFKS DMKKGPAFTT ALNHGVDLAH IYGQNLDRQH KLRLFKDGKL
     RYQILDGEVY PPTVSEVQVD MHYPPHVPES RRFAVGHEAF GLVPGLMMYA TIWLREHNRV
     CDILKQEHPD WDDERLFQTS RLILIGETIK IVIEDYVQHL SGYYFKLKFD PELLFNERFQ
     YQNRISSEFN TLYHWHPLMP DDFHIQDEVY NYQQFLFNTS ILTDYGVNSL VESFNKQIAG
     RVAGGRNVAP AVLRVAIKSI ENSRQMRYQS INAYRKRFNM KPYRSFEEMT GEKEMAAELE
     EMYGDVDAVE LYAGLLVEKP RSNAIFGETM VEMGAPYSLK GLMGNPICSP EYWKPSTFGG
     KVGFEIVNSA SLQNLVCNNV NGPCPMASFY VPNVKDSLPT TINASTSQSD RNVNPTVLLK
     ERTSEL
//