ID U3JH32_FICAL Unreviewed; 586 AA.
AC U3JH32;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 57.
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|Ensembl:ENSFALP00000002086.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000002086.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000002086.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000002086.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- 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_005055763.1; XM_005055706.2.
DR AlphaFoldDB; U3JH32; -.
DR STRING; 59894.ENSFALP00000002086; -.
DR GlyCosmos; U3JH32; 3 sites, No reported glycans.
DR Ensembl; ENSFALT00000002098.2; ENSFALP00000002086.2; ENSFALG00000001991.2.
DR GeneID; 101806256; -.
DR KEGG; fab:101806256; -.
DR CTD; 5742; -.
DR eggNOG; KOG2408; Eukaryota.
DR GeneTree; ENSGT00390000010743; -.
DR HOGENOM; CLU_022428_0_0_1; -.
DR OMA; LFGSQFQ; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000016665; Chromosome 17.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0001750; C:photoreceptor outer segment; 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:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..586
FT /note="Prostaglandin G/H synthase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032525695"
FT DOMAIN 18..56
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 586 AA; 66658 MW; FE2F8C0230E010FF CRC64;
MQGCGGWMMM CLSLSLPAVN PCCYFPCQNQ GVCVRVGLRG YECDCTRTGY YGVNCTSPEF
WTHLHNLLKP SPAFYHFILT HFKWFWDIIN STFIRDTLMR LVLTVRANLI PSPPTFNSDY
GYISWEAYAN VSYYTRVLPP VPDDCPTPMG TKGKMQLPDP QLLAERFLLR QKFEADPRGT
NMMFAFFAQH FTHQFFKTSG KMGRGFTKAL GHGVDLGHLY GDNLQRQHQL RLFRDGKLKF
QVVDGEVYPP MVSEAPVHMV YPSGVPKEQQ LAVGQEVFGL LPGLCVYATL WLREHNRVCD
LLKRDHPTWS DEQLFQTARL ILIGETIKIV VEDYVQHLSG YYLSLKFDPE LLFGSQFQYR
NRIAVEFNQL YHWHGLMPDS FVIQGQEYSY KQFLYNTSML MDYGVEALVE SFSKQIAGRI
GGGQTINANV LHVAVGVIKE SRQLRLQPFN EYRKRFGMKP YKSFQELTGE EEKAAELEEL
YGDIDALEFY PGLLLEKPQP NGIFGESMVE IGAPFSLKGL FGNPICSPEY WKPSTFGGET
GFEIVKTASL EKLVCLNVKK CPYVAFHVPD TAEHGSPRAG GSSTEL
//
