ID Q501R2_XENTR Unreviewed; 604 AA. AC Q501R2; F6SAU9; DT 07-JUN-2005, integrated into UniProtKB/TrEMBL. DT 07-JUN-2005, sequence version 1. DT 27-MAR-2024, entry version 149. 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=ptgs2 {ECO:0000313|EMBL:CAJ83938.1, GN ECO:0000313|Ensembl:ENSXETP00000037831, GN ECO:0000313|RefSeq:NP_001025697.1, GN ECO:0000313|Xenbase:XB-GENE-482133}; GN Synonyms=cox-2 {ECO:0000313|RefSeq:NP_001025697.1}, cox2 GN {ECO:0000313|RefSeq:NP_001025697.1}, gripghs GN {ECO:0000313|RefSeq:NP_001025697.1}, hcox-2 GN {ECO:0000313|RefSeq:NP_001025697.1}, MGC97821 GN {ECO:0000313|EMBL:AAH95912.1}, pgg/hs GN {ECO:0000313|RefSeq:NP_001025697.1}, pghs-2 GN {ECO:0000313|RefSeq:NP_001025697.1}, phs-2 GN {ECO:0000313|RefSeq:NP_001025697.1}; GN ORFNames=TGas066j02.1-001 {ECO:0000313|EMBL:CAJ83938.1}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAH95912.1}; RN [1] {ECO:0000313|RefSeq:NP_001025697.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12454917; DOI=10.1002/dvdy.10174; RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W., RA Richardson P.; RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus RT initiative."; RL Dev. Dyn. 225:384-391(2002). RN [2] {ECO:0000313|EMBL:AAH95912.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo {ECO:0000313|EMBL:AAH95912.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CAJ83938.1} RP NUCLEOTIDE SEQUENCE. RA Amaya E., Ashurst J.L., Bonfield J.K., Croning M.D.R., Chen C-K., RA Davies R.M., Francis M.D., Garrett N., Gilchrist M.J., Grafham D.V., RA McLaren S.R., Papalopulu N., Rogers J., Smith J.C., Taylor R.G., Voigt J., RA Zorn A.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSXETP00000037831} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000037831}; RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L., RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R., RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J., RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H., RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K., RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A., RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T., RA Khokha M.K., Richardson P.M., Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [5] {ECO:0000313|Ensembl:ENSXETP00000037831} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. RN [6] {ECO:0000313|RefSeq:NP_001025697.1} 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}. 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; BC095912; AAH95912.1; -; mRNA. DR EMBL; CR942339; CAJ83938.1; -; mRNA. DR RefSeq; NP_001025697.1; NM_001030526.1. DR PeroxiBase; 4266; XtPGHS02. DR Ensembl; ENSXETT00000037831; ENSXETP00000037831; ENSXETG00000017378. DR GeneID; 595089; -. DR KEGG; xtr:595089; -. DR AGR; Xenbase:XB-GENE-482133; -. DR CTD; 5743; -. DR Xenbase; XB-GENE-482133; ptgs2. DR eggNOG; KOG2408; Eukaryota. DR HOGENOM; CLU_022428_0_0_1; -. DR OMA; NVHYGYK; -. DR OrthoDB; 1086441at2759; -. DR TreeFam; TF329675; -. DR Reactome; R-XTR-197264; Nicotinamide salvaging. DR Reactome; R-XTR-2142770; Synthesis of 15-eicosatetraenoic acid derivatives. DR Reactome; R-XTR-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX). DR Reactome; R-XTR-9018677; Biosynthesis of DHA-derived SPMs. DR Reactome; R-XTR-9018679; Biosynthesis of EPA-derived SPMs. DR Reactome; R-XTR-9025094; Biosynthesis of DPAn-3 SPMs. DR Reactome; R-XTR-9027604; Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives. DR UniPathway; UPA00662; -. DR Proteomes; UP000008143; Chromosome 4. DR Bgee; ENSXETG00000017378; Expressed in gastrula and 12 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. 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:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway. 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:UP000008143}; KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001025697.1}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..604 FT /note="Prostaglandin G/H synthase 2" FT /evidence="ECO:0000256|SAM:SignalP, FT ECO:0000313|RefSeq:NP_001025697.1" FT /id="PRO_5033206274" FT DOMAIN 18..56 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT ACT_SITE 194 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1" FT ACT_SITE 372 FT /note="For cyclooxygenase activity" FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1" FT BINDING 107 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2" FT BINDING 375 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 604 AA; 69100 MW; 6333B374EA926B0C CRC64; MIVLPAAVFL SLLVFSQAAN PCCSNPCQNR GVCMTVGHDR YECDCTRTGF YGENCTKPEF LSWLRLKLKP APNTVHYILT HFKGLWNIVN NISFLRDAIM RYVLTSRSHL IDSPPTYNSH YGYKSWEAFS NLSYYTRTLP PVERDCPTPM GVKGMKELPS AKLVVEKFLM RRKFIPDPQG SNVMFAFFAQ HFTHQFFRTD MAKGAAFTKA LGHGVDLNHI YGESLERQHK LRLMKGGKLK YQMISGEMYP PTVKTTGVDM VYPPHIPDHL QFAVGQEVFG LVPGLMMYST IWLREHNRVC DILSNEHPEW DDERIFQTAR LILIGETIKI VIEDYVQHLS GYHFKLKFDP ELLFNQKFQY QNRISAEFNT LYHWHPLLPD TFAISEKEYS YPQFLYNNSV MLNHGLTEMV ESFSRQTAGR VAGGRNFPAA ITRVAVASIE HSREMRYQSL NEYRKRFMLK PFESFEELTG EKEMSAELEK LYGDIDAMEF YPGLLVEQPR PGAIFGETMV EIGAPFSLKG LMGNPICSPE YWKPSTFGGS VGFDIVNSAS LQKLICNNVR DCPYTAFHVL KSKPSEKDFI NASSDSTLEN VKPSLILKEH ASEL //