ID   H9G4Z6_ANOCA            Unreviewed;       602 AA.
AC   H9G4Z6;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   27-MAR-2024, entry version 65.
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|Ensembl:ENSACAP00000001254.3};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000001254.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000001254.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000001254.3};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000001254.3}
RP   IDENTIFICATION.
RG   Ensembl;
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   RefSeq; XP_003223472.1; XM_003223424.3.
DR   AlphaFoldDB; H9G4Z6; -.
DR   STRING; 28377.ENSACAP00000001254; -.
DR   GlyCosmos; H9G4Z6; 4 sites, No reported glycans.
DR   Ensembl; ENSACAT00000001287.4; ENSACAP00000001254.3; ENSACAG00000001178.4.
DR   GeneID; 100560130; -.
DR   KEGG; acs:100560130; -.
DR   CTD; 5743; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00390000010743; -.
DR   HOGENOM; CLU_022428_0_0_1; -.
DR   InParanoid; H9G4Z6; -.
DR   OrthoDB; 1086441at2759; -.
DR   TreeFam; TF329675; -.
DR   UniPathway; UPA00662; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000001178; Expressed in dewlap and 11 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:0005637; C:nuclear inner membrane; IEA:Ensembl.
DR   GO; GO:0005640; C:nuclear outer membrane; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0020037; F:heme binding; IEA:Ensembl.
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; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0071471; P:cellular response to non-ionic osmotic stress; IEA:Ensembl.
DR   GO; GO:0019371; P:cyclooxygenase pathway; IBA:GO_Central.
DR   GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0031622; P:positive regulation of fever generation; IEA:Ensembl.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032310; P:prostaglandin secretion; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0150077; P:regulation of neuroinflammatory response; IEA:Ensembl.
DR   GO; GO:0009624; P:response to nematode; 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:SF8; PROSTAGLANDIN G_H SYNTHASE 2; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00008; EGF; 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   3: Inferred from homology;
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:UP000001646};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..602
FT                   /note="Prostaglandin G/H synthase 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003619179"
FT   DOMAIN          17..55
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT   ACT_SITE        371
FT                   /note="For cyclooxygenase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT   BINDING         374
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;  68947 MW;  46DC4E70ECA8E6FE CRC64;
     MLLPCAVLFA LLALSHAVNP CCSNPCHNRG VCMTTGFDTY ACDCTRTGYY GENCTTPEFL
     TWLKLKLKPT PDMVHYILTH FKGVWNIINN IPFLHRAIMT YILMSRSHLI ESPPTYNGHY
     SYKSWEAYSN LSYYTRSLPP VEHNCPTPMG IKGKKELPDS QIIVEKFLMR RKFIPDPQGT
     NVMFTFFAQH FTHQFFKTDH RKGPEFTKGL GHGVDLSHIY GETLDRQMKL RLLKDGKLKF
     QMIDGEMYPP TVKDTQAEMI YPPHIPEHLR FCVGQEVFGL VPGLMMYATL WLREHNRVCD
     VLKGEHPEWD DEQLFQTTRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNQRFQYQ
     NRIAAEFNTL YHWHPLLPDT FNIQDQEYTY QQFVYNNSIM LDHGLSHMVQ SFSKQIAGRV
     AGGRNVPVAV LKVAKASIDQ SRQMRYQSLN EYRKHFLLKP FQSFEELTGE KEMAAELKEL
     YGDIDAMELY PALLVEKPRP GAIFGETMIE LGAPFSLKGL MGNAICSPEY WKPSTFGGKV
     GFDIVNTASL QRLVCNNVAG CPLTAFHVLT QETKATSNTS TTSASLDEIN PAVLLKERSA
     EL
//