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Database: UniProt/SWISS-PROT
Entry: PGH1_BOVIN
LinkDB: PGH1_BOVIN
Original site: PGH1_BOVIN 
ID   PGH1_BOVIN              Reviewed;         600 AA.
AC   O62664; A7YWD4;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   12-SEP-2018, entry version 143.
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=COX-1, COX1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 121-379.
RX   PubMed=9348208; DOI=10.1210/endo.138.11.5527;
RA   Asselin E., Drolet P., Fortier M.A.;
RT   "Cellular mechanisms involved during oxytocin-induced prostaglandin
RT   F2alpha production in endometrial epithelial cells in vitro: role of
RT   cyclooxygenase-2.";
RL   Endocrinology 138:4798-4805(1997).
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; Peripheral membrane
CC       protein. Endoplasmic reticulum membrane; Peripheral membrane
CC       protein.
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; BC134517; AAI34518.1; -; mRNA.
DR   EMBL; AF004943; AAC05591.1; -; mRNA.
DR   RefSeq; NP_001098793.1; NM_001105323.1.
DR   UniGene; Bt.2151; -.
DR   ProteinModelPortal; O62664; -.
DR   SMR; O62664; -.
DR   STRING; 9913.ENSBTAP00000008833; -.
DR   BindingDB; O62664; -.
DR   ChEMBL; CHEMBL2860; -.
DR   PeroxiBase; 3332; BtPGHS01.
DR   PaxDb; O62664; -.
DR   PRIDE; O62664; -.
DR   Ensembl; ENSBTAT00000008833; ENSBTAP00000008833; ENSBTAG00000006716.
DR   GeneID; 282022; -.
DR   KEGG; bta:282022; -.
DR   CTD; 5742; -.
DR   VGNC; VGNC:33511; PTGS1.
DR   eggNOG; KOG2408; Eukaryota.
DR   eggNOG; ENOG410XPZ3; LUCA.
DR   GeneTree; ENSGT00390000010743; -.
DR   HOGENOM; HOG000013149; -.
DR   HOVERGEN; HBG000366; -.
DR   InParanoid; O62664; -.
DR   KO; K00509; -.
DR   OMA; FKTSGKM; -.
DR   OrthoDB; EOG091G03CD; -.
DR   TreeFam; TF329675; -.
DR   BRENDA; 1.14.99.1; 908.
DR   Reactome; R-BTA-140180; COX reactions.
DR   Reactome; R-BTA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   UniPathway; UPA00662; -.
DR   PRO; PR:O62664; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000006716; Expressed in 9 organ(s), highest expression level in lung.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
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   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     24       {ECO:0000255}.
FT   CHAIN        25    600       Prostaglandin G/H synthase 1.
FT                                /FTId=PRO_0000163113.
FT   DOMAIN       32     70       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   ACT_SITE    207    207       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   ACT_SITE    385    385       For cyclooxygenase activity.
FT                                {ECO:0000250}.
FT   METAL       388    388       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   SITE        530    530       Aspirin-acetylated serine. {ECO:0000250}.
FT   CARBOHYD     68     68       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    144    144       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    410    410       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     36     47       {ECO:0000250}.
FT   DISULFID     37    159       {ECO:0000250}.
FT   DISULFID     41     57       {ECO:0000250}.
FT   DISULFID     59     69       {ECO:0000250}.
FT   DISULFID    569    575       {ECO:0000250}.
FT   CONFLICT    229    229       D -> G (in Ref. 2; AAC05591).
FT                                {ECO:0000305}.
FT   CONFLICT    241    241       Q -> R (in Ref. 2; AAC05591).
FT                                {ECO:0000305}.
FT   CONFLICT    263    263       P -> Q (in Ref. 2; AAC05591).
FT                                {ECO:0000305}.
FT   CONFLICT    320    320       H -> Q (in Ref. 2; AAC05591).
FT                                {ECO:0000305}.
SQ   SEQUENCE   600 AA;  68805 MW;  0B43E65DA9E2A2E9 CRC64;
     MSRQGISLRF PLLLLLLSPS PVLPADPGAP APVNPCCYYP CQHQGICVRF GLDRYQCDCT
     RTGYYGPNCT IPEIWTWLRT TLRPSPSFVH FLLTHGRWLW DFVNATFIRD KLMRLVLTVR
     SNLIPSPPTY NVAHDYISWE SFSNVSYYTR ILPSVPRDCP TPMGTKGKKQ LPDAEFLSRR
     FLLRRKFIPD PQGTNLMFAF FAQHFTHQFF KTSGKMGPGF TKALGHGVDL GHIYGDNLER
     QYQLRLFKDG KLKYQMLNGE VYPPSVEEAP VLMHYPRGIP PQSQMAVGQE VFGLLPGLMV
     YATIWLREHN RVCDLLKAEH PTWGDEQLFQ TARLILIGET IKIVIEEYVQ QLSGYFLQLK
     FDPELLFGAQ FQYRNRIAME FNQLYHWHPL MPDSFRVGPQ DYSYEQFLFN TSMLVDYGVE
     ALVDAFSRQP AGRIGGGRNI DHHILHVAVD VIKESRELRL QPFNEYRKRF GMKPYTSFQE
     LTGEKEMAAE LEELYGDIDA LEFYPGLLLE KCHPNSIFGE SMIEMGAPFS LKGLLGNPIC
     SPEYWKASTF GGDVGFNLVK TATLKKLVCL NTKTCPYVSF HVPDPHREDR PGVERPPTEL
//
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