ID A0A3Q1IX75_ANATE Unreviewed; 608 AA.
AC A0A3Q1IX75;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000026757.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000026757.1}
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}.
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 AlphaFoldDB; A0A3Q1IX75; -.
DR STRING; 64144.ENSATEP00000026757; -.
DR Ensembl; ENSATET00000027182.2; ENSATEP00000026757.1; ENSATEG00000018490.2.
DR GeneTree; ENSGT00390000010743; -.
DR OMA; NVHYGYK; -.
DR OrthoDB; 1086441at2759; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000265040; Unplaced.
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:0048856; P:anatomical structure development; IEA:UniProt.
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 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:UP000265040};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..608
FT /note="Prostaglandin G/H synthase 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018544365"
FT DOMAIN 20..58
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT ACT_SITE 374
FT /note="For cyclooxygenase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT BINDING 377
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 608 AA; 69232 MW; D0DB2F853CF89E49 CRC64;
MNRLTVAVFL LSLAFLVSEG GNPCCSEPCQ NRGVCTALGS DNYQCDCTRT GFYGQNCTTP
EFLTWIKLSL KPSPNTVHYI LTHFKGFWNI INNISFLRDG IMRYVLTSRS HLIDSPPTYN
ADYGYKSWEA YSNLSYYTRT LPPVPEDCPT PMGVAGKKEL PDIKVLAEKL LIRRQFIPDP
QGTSLMFAFF AQHFTHQFFK SDFKKGPGFT QAKGHGVDLN HIYGDTLEKQ HKLRLFKDGK
LKYQIVDGEV YPPTVKEADV EMFYPPHVPD SHRFAVGHEA FGLVPGLIMY ATIWLREHNR
VCDVLKEVHP YWDDERLFQT TRLILIGETI KIVIEDYVQH LSGYHFKLKF DPELLFNQRF
QYQNRIASEF NTLYHWHPLM PDSFHIEEKE YSYKQFVFNT SVVTEHGIGS LVESFTNQIA
GRVAGGRNVP GSILYVAMKS IEHSREMRYQ SLNAYRKRFS MQPYSSFEDL TGDQEMAAIL
EEMYGHIDAV ELYPGLLVEK PRPNAIFGET MVEMGAPFSL KGLMGNPICS PEYWKPSTFG
GSVGFDIINT ASLQKLICNN VRGPCPMASF YVPNVKETGS TIINSSTSHS RGSDINPTVI
LKERTTEL
//
