GenomeNet

Database: UniProt/SWISS-PROT
Entry: PGH1_RABIT
LinkDB: PGH1_RABIT
Original site: PGH1_RABIT 
ID   PGH1_RABIT              Reviewed;         606 AA.
AC   O97554;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   23-MAY-2018, entry version 110.
DE   RecName: Full=Prostaglandin G/H synthase 1;
DE            EC=1.14.99.1;
DE   AltName: Full=Cyclooxygenase-1;
DE            Short=COX-1;
DE   AltName: Full=Prostaglandin H2 synthase 1;
DE            Short=PGH synthase 1;
DE            Short=PGHS-1;
DE            Short=PHS 1;
DE   AltName: Full=Prostaglandin-endoperoxide synthase 1;
DE   Flags: Precursor;
GN   Name=PTGS1; Synonyms=COX1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white;
RA   Guan Y., Zhang Y., Breyer R.M., Davis L., Redha R., Chang S.,
RA   Breyer M.D.;
RT   "Intrarenal localization of cyclooxygenase-1 and -2 and their
RT   differential expression in acute hydronephrotic kidney.";
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
CC       committed step in prostanoid synthesis. Involved in the
CC       constitutive production of prostanoids in particular in the
CC       stomach and platelets. In gastric epithelial cells, it is a key
CC       step in the generation of prostaglandins, such as prostaglandin E2
CC       (PGE2), which plays an important role in cytoprotection. In
CC       platelets, it is involved in the generation of thromboxane A2
CC       (TXA2), which promotes platelet activation and aggregation,
CC       vasoconstriction and proliferation of vascular smooth muscle cells
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
CC       H(2) + A + H(2)O.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
CC       subunit. {ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: The conversion of arachidonate to prostaglandin H2
CC       is a 2 step reaction: a cyclooxygenase (COX) reaction which
CC       converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase
CC       reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The
CC       cyclooxygenase reaction occurs in a hydrophobic channel in the
CC       core of the enzyme. The peroxidase reaction occurs at a heme-
CC       containing active site located near the protein surface. The
CC       nonsteroidal anti-inflammatory drugs (NSAIDs) binding site
CC       corresponds to the cyclooxygenase active site.
CC   -!- MISCELLANEOUS: Conversion of arachidonate to prostaglandin H2 is
CC       mediated by 2 different isozymes: the constitutive PTGS1 and the
CC       inducible PTGS2. PGHS1 is expressed constitutively and generally
CC       produces prostanoids acutely in response to hormonal stimuli to
CC       fine-tune physiological processes requiring instantaneous,
CC       continuous regulation (e.g. hemostasis). PGHS2 is inducible and
CC       typically produces prostanoids that mediate responses to
CC       physiological stresses such as infection and inflammation.
CC   -!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal
CC       anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen.
CC       Aspirin is able to produce an irreversible inactivation of the
CC       enzyme through a serine acetylation. Inhibition of the PGHSs with
CC       NSAIDs acutely reduces inflammation, pain, and fever, and long-
CC       term use of these drugs reduces fatal thrombotic events, as well
CC       as the development of colon cancer and Alzheimer's disease. PTGS2
CC       is the principal isozyme responsible for production of
CC       inflammatory prostaglandins. New generation PTGSs inhibitors
CC       strive to be selective for PTGS2, to avoid side effects such as
CC       gastrointestinal complications and ulceration.
CC   -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
CC       {ECO:0000305}.
DR   EMBL; AF026008; AAD01796.1; -; mRNA.
DR   RefSeq; NP_001076150.1; NM_001082681.1.
DR   UniGene; Ocu.2320; -.
DR   ProteinModelPortal; O97554; -.
DR   SMR; O97554; -.
DR   STRING; 9986.ENSOCUP00000002186; -.
DR   BindingDB; O97554; -.
DR   ChEMBL; CHEMBL3334; -.
DR   PeroxiBase; 4131; OcuPGHS01.
DR   PRIDE; O97554; -.
DR   GeneID; 100009407; -.
DR   KEGG; ocu:100009407; -.
DR   CTD; 5742; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   eggNOG; ENOG410XPZ3; LUCA.
DR   HOGENOM; HOG000013149; -.
DR   HOVERGEN; HBG000366; -.
DR   InParanoid; O97554; -.
DR   KO; K00509; -.
DR   UniPathway; UPA00662; -.
DR   PRO; PR:O97554; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031090; C:organelle 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:0019371; P:cyclooxygenase pathway; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 1.10.640.10; -; 1.
DR   InterPro; IPR029580; COX-1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR010255; Haem_peroxidase.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR037120; Haem_peroxidase_sf.
DR   PANTHER; PTHR11903:SF6; PTHR11903:SF6; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00008; EGF; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Dioxygenase; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Glycoprotein; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Metal-binding; Microsome; Oxidoreductase; Peroxidase;
KW   Prostaglandin biosynthesis; Prostaglandin metabolism;
KW   Reference proteome; Signal.
FT   SIGNAL        1     30       {ECO:0000255}.
FT   CHAIN        31    606       Prostaglandin G/H synthase 1.
FT                                /FTId=PRO_0000041818.
FT   DOMAIN       38     76       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   ACT_SITE    213    213       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   ACT_SITE    391    391       For cyclooxygenase activity.
FT                                {ECO:0000250}.
FT   METAL       394    394       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   SITE        536    536       Aspirin-acetylated serine. {ECO:0000250}.
FT   CARBOHYD     74     74       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    110    110       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    150    150       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    416    416       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     42     53       {ECO:0000250}.
FT   DISULFID     43    165       {ECO:0000250}.
FT   DISULFID     47     63       {ECO:0000250}.
FT   DISULFID     65     75       {ECO:0000250}.
FT   DISULFID    575    581       {ECO:0000250}.
SQ   SEQUENCE   606 AA;  69076 MW;  DB751FD1E2F1CD77 CRC64;
     MSRSSPSLRL PVLLLLLLLL LLPPPPPVLP ADPGAPAPVN PCCYFPCQHQ GVCVRVALDR
     YQCDCTRTGY SGPNCTVPDL WTWLRSSLRP SPTFVHYLLT HVRWFWEFVN ATFIRDTLMR
     LVLTVRSNLI PSPPTYNLDY DYISWEAFSN VSYYTRVLPS VPKDCPTPMG TKGKKQLPDA
     QVLAHRFLLR RTFIPDPQGT NLMFAFFAQH FTHQFFKTSG KMGPGFTKAL GHGVDLGHIY
     GDSLERQYHL RLFKDGKLKY QVLDGEVYPP SVEEAPVLMH YPRGVPPRSQ MAVGQEVFGL
     LPGLMLYATL WLREHNRVCD LLKAEHPTWD DEQLFQTTRL ILIGETIKIV IEEYVQQLSG
     YFLQLKFDPE MLFSVQFQYR NRIAMEFNHL YHWHPLMPDS FQVGSQEYSY EQFLFNTSML
     VDYGVEALVD AFSRQSAGRI GGGRNIDHHV LHVAVEVIKE SREMRLQPFN EYRKRFGLKP
     YASFQELTGE TEMAAELEEL YGDIDALEFY PGLLLEKCQP NSIFGESMIE IGAPFSLKGL
     LGNPICSPEY WKPSTFGGEV GSNLIKTATL KKLVCLNTKT CPYVSFRVPR SSGDDGPAAE
     RRSTEL
//
DBGET integrated database retrieval system