ID   H3AHY9_LATCH            Unreviewed;       620 AA.
AC   H3AHY9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
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:ENSLACP00000009260.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000009260.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000009260.1}
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}.
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DR   EMBL; AFYH01205147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006009311.1; XM_006009249.2.
DR   AlphaFoldDB; H3AHY9; -.
DR   STRING; 7897.ENSLACP00000009260; -.
DR   GlyCosmos; H3AHY9; 4 sites, No reported glycans.
DR   Ensembl; ENSLACT00000009331.1; ENSLACP00000009260.1; ENSLACG00000008168.2.
DR   GeneID; 102352257; -.
DR   KEGG; lcm:102352257; -.
DR   CTD; 5743; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00390000010743; -.
DR   InParanoid; H3AHY9; -.
DR   OMA; NVHYGYK; -.
DR   OrthoDB; 1086441at2759; -.
DR   TreeFam; TF329675; -.
DR   UniPathway; UPA00662; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000008168; Expressed in pectoral fin and 6 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   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:UP000008672};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..620
FT                   /note="Prostaglandin G/H synthase 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003579225"
FT   DOMAIN          32..70
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   ACT_SITE        208
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT   ACT_SITE        386
FT                   /note="For cyclooxygenase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT   BINDING         389
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   620 AA;  71066 MW;  093A841D8DB7CD02 CRC64;
     MDFKSRQKAF IIPTRMFIYG TLLFVCVSLS HAANPCCSNP CQNRGVCMTV GFDNYECDCT
     RTGFYGKNCT TPEFWTWVKR ALKPSPNTVH YILTHYKGFW NIVNSIPFLR DAIMRYVLTS
     RSHLIDSPPT YNSHYDYKSW EAYSNLSYYT RTLPPVPEDC PTPMGVKGKN SLPDSKMIAE
     KFLLRRKFIP DPQGTSLMFA FFAQHFTHQF FKTDQIRGPA FTTGLGHGVD LNHIYGETLD
     RQHKLRLFKD GKLKYQMING EMYPPTVKDV QVAMTYPPHI AEDFKFAVGQ EVFGLVPGLM
     MYSVIWLREH NRVCDILKQE HPEWDDERLF QTTRLILIGE TIKIVIEDYV QHLSGYHFKL
     KFDPELLFHQ QFQYQNRIAA EFNTLYHWHP LMPDSFLIQG KEYGYHQFLF NNSIVTEHGI
     RNLVESFSKQ IAGRVAGGRN VAPGVLRVAI ASIDQSRKMR YQSLNEYRKR FQMRPYKSFE
     DLTGEKEMAA ELQELYGDVD AVELYPGLMV EKPRPGAIFG ETMVEMGAPF SLKGLIGNPI
     CSPEYWKPST FGGNVGFQIV NTASLQKLVC SNVKGTCPFT SFHIPEPNPT KTSTSNASTS
     NSALKDINPS LLLKKHSTEL
//