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Q63921

- PGH1_RAT

UniProt

Q63921 - PGH1_RAT

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Protein
Prostaglandin G/H synthase 1
Gene
Ptgs1, Cox-1, Cox1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells.

Catalytic activityi

Arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O.

Cofactori

Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei209 – 2091Proton acceptor By similarity
Active sitei387 – 3871For cyclooxygenase activity By similarity
Metal bindingi390 – 3901Iron (heme axial ligand) By similarity
Sitei532 – 5321Aspirin-acetylated serine

GO - Molecular functioni

  1. dioxygenase activity Source: UniProtKB-KW
  2. heme binding Source: InterPro
  3. lipid binding Source: RGD
  4. metal ion binding Source: UniProtKB-KW
  5. peroxidase activity Source: UniProtKB-KW
  6. prostaglandin-endoperoxide synthase activity Source: RGD
Complete GO annotation...

GO - Biological processi

  1. aging Source: RGD
  2. learning Source: RGD
  3. maintenance of blood-brain barrier Source: RGD
  4. memory Source: RGD
  5. negative regulation of epinephrine secretion Source: RGD
  6. negative regulation of norepinephrine secretion Source: RGD
  7. positive regulation of smooth muscle contraction Source: RGD
  8. positive regulation of vasoconstriction Source: RGD
  9. prostaglandin biosynthetic process Source: UniProtKB
  10. regulation of blood pressure Source: UniProtKB
  11. response to corticosterone Source: RGD
  12. response to fatty acid Source: RGD
  13. response to organonitrogen compound Source: RGD
  14. response to oxidative stress Source: InterPro
  15. sensory perception of pain Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase, Peroxidase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00662.

Protein family/group databases

PeroxiBasei3974. RnoPGHS01.

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin G/H synthase 1 (EC:1.14.99.1)
Alternative name(s):
Cyclooxygenase-1
Short name:
COX-1
Prostaglandin H2 synthase 1
Short name:
PGH synthase 1
Short name:
PGHS-1
Short name:
PHS 1
Prostaglandin-endoperoxide synthase 1
Gene namesi
Name:Ptgs1
Synonyms:Cox-1, Cox1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3439. Ptgs1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. intracellular membrane-bounded organelle Source: UniProtKB
  4. nuclear envelope Source: RGD
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626 By similarity
Add
BLAST
Chaini27 – 602576Prostaglandin G/H synthase 1
PRO_0000023870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi38 ↔ 49 By similarity
Disulfide bondi39 ↔ 161 By similarity
Disulfide bondi43 ↔ 59 By similarity
Disulfide bondi61 ↔ 71 By similarity
Glycosylationi70 – 701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi106 – 1061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi146 – 1461N-linked (GlcNAc...) Reviewed prediction
Glycosylationi412 – 4121N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi571 ↔ 577 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ63921.
PRIDEiQ63921.

Expressioni

Gene expression databases

GenevestigatoriQ63921.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010218.

Structurei

3D structure databases

ProteinModelPortaliQ63921.
SMRiQ63921. Positions 34-586.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 7239EGF-like
Add
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.

Keywords - Domaini

EGF-like domain, Signal

Phylogenomic databases

eggNOGiNOG39991.
HOGENOMiHOG000013149.
HOVERGENiHBG000366.
InParanoidiQ63921.
PhylomeDBiQ63921.

Family and domain databases

Gene3Di1.10.640.10. 1 hit.
InterProiIPR029580. COX-1.
IPR000742. EG-like_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view]
PANTHERiPTHR11903:SF6. PTHR11903:SF6. 1 hit.
PfamiPF03098. An_peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q63921-1 [UniParc]FASTAAdd to Basket

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MSRRSLSLQF PLLLLLLLLP PPPVLLTDAG VPSPVNPCCY YPCQNQGVCV    50
RFGLDHYQCD CTRTGYSGPN CTIPEIWTWL RSSLRPSPSF THFLLTHGYW 100
IWEFVNATFI REVLMRLVIT VRSNLIPSPP TYNTAHDYIS WESFSNVSYY 150
TRILPSVPKD CPTPMGTKGK KQLPDIHLLA QRLLLRREFI PGPQGTNVLF 200
AFFAQHFTHQ FFKTSGKMGP GFTKALGHGV DLGHIYGDSL ERQYHLRLFK 250
DGKLKYQVLD GEVYPPSVEQ ASVLMRYPPG VPPEKQMAVG QEVFGLLPGL 300
MLFSTIWLRE HNRVCDLLKE EHPTWDDEQL FQTTRLILIG ETIKIIIEEY 350
VQHLSGYFLQ LKFDPELLFR AQFQYRNRIA LEFNHLYHWH PLMPDSFQVG 400
SQEYSYEQFL FNTSMLVDYG VEALVDAFSR QRAGRIGGGR NFDYHVLHVA 450
EDVIKESREM RLQSFNEYRK RFGLKPYTSF QEFTGEKEMA AELEELYGDI 500
DALEFYPGLM LEKCQPNSLF GESMIEMGAP FSLKGLLGNP ICSPEYWKPS 550
TFGGDVGFNI VNTASLKKLV CLNTKTCPYV SFRVPDYPGD DGSVFVRPST 600
EL 602
Length:602
Mass (Da):69,032
Last modified:December 15, 1998 - v2
Checksum:i0BFAF7EBFDA0C7C2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361N → I in AAA03465. 1 Publication
Sequence conflicti36 – 361N → I in AAB29400. 1 Publication
Sequence conflicti116 – 1172RL → GW1 Publication
Sequence conflicti119 – 1191I → L1 Publication
Sequence conflicti192 – 1921G → A in AAA03465. 1 Publication
Sequence conflicti192 – 1921G → A in AAB29400. 1 Publication
Sequence conflicti263 – 2631V → L in AAA03465. 1 Publication
Sequence conflicti263 – 2631V → L in AAB29400. 1 Publication
Sequence conflicti274 – 2741L → K in AAA03465. 1 Publication
Sequence conflicti274 – 2741L → K in AAB29400. 1 Publication
Sequence conflicti290 – 2901G → A in AAA03465. 1 Publication
Sequence conflicti290 – 2901G → A in AAB29400. 1 Publication
Sequence conflicti339 – 3391I → R in AAB29400. 1 Publication
Sequence conflicti344 – 3441K → E in AAA03465. 1 Publication
Sequence conflicti344 – 3441K → E in AAB29400. 1 Publication
Sequence conflicti381 – 3811L → M in AAA03465. 1 Publication
Sequence conflicti381 – 3811L → M in AAB29400. 1 Publication
Sequence conflicti392 – 3921L → F in AAA03465. 1 Publication
Sequence conflicti392 – 3921L → F in AAB29400. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03388 mRNA. Translation: AAA03465.1.
S67721 mRNA. Translation: AAB29400.2.
U18060 mRNA. Translation: AAA85823.1.
PIRiS39782.
S69198.
UniGeneiRn.44404.

Genome annotation databases

UCSCiRGD:3439. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03388 mRNA. Translation: AAA03465.1 .
S67721 mRNA. Translation: AAB29400.2 .
U18060 mRNA. Translation: AAA85823.1 .
PIRi S39782.
S69198.
UniGenei Rn.44404.

3D structure databases

ProteinModelPortali Q63921.
SMRi Q63921. Positions 34-586.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000010218.

Chemistry

BindingDBi Q63921.
ChEMBLi CHEMBL2095157.

Protein family/group databases

PeroxiBasei 3974. RnoPGHS01.

Proteomic databases

PaxDbi Q63921.
PRIDEi Q63921.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:3439. rat.

Organism-specific databases

RGDi 3439. Ptgs1.

Phylogenomic databases

eggNOGi NOG39991.
HOGENOMi HOG000013149.
HOVERGENi HBG000366.
InParanoidi Q63921.
PhylomeDBi Q63921.

Enzyme and pathway databases

UniPathwayi UPA00662 .

Miscellaneous databases

NextBioi 604139.
PROi Q63921.

Gene expression databases

Genevestigatori Q63921.

Family and domain databases

Gene3Di 1.10.640.10. 1 hit.
InterProi IPR029580. COX-1.
IPR000742. EG-like_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view ]
PANTHERi PTHR11903:SF6. PTHR11903:SF6. 1 hit.
Pfami PF03098. An_peroxidase. 2 hits.
[Graphical view ]
PRINTSi PR00457. ANPEROXIDASE.
SMARTi SM00181. EGF. 1 hit.
[Graphical view ]
SUPFAMi SSF48113. SSF48113. 1 hit.
PROSITEi PS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning two isoforms of rat cyclooxygenase: differential regulation of their expression."
    Feng L., Sun W., Xia Y., Tang W.W., Chanmugam P., Soyoola E., Wilson C.B., Hwang D.
    Arch. Biochem. Biophys. 307:361-368(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "Analysis and quantitation of splicing variants of the TPA-inducible PGHS-1 mRNA in rat tracheal epithelial cells."
    Kitzler J., Hill E., Hardman R., Reddy N., Philpot R., Eling T.E.
    Arch. Biochem. Biophys. 316:856-863(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer 344.
    Tissue: Trachea.
  3. "Cyclooxygenases: structural, cellular, and molecular biology."
    Smith W.L., DeWitt D.L., Garavito R.M.
    Annu. Rev. Biochem. 69:145-182(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
  4. "Aspirin, cyclooxygenase inhibition and colorectal cancer."
    Sostres C., Gargallo C.J., Lanas A.
    World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN COLORECTAL CANCER.

Entry informationi

Entry nameiPGH1_RAT
AccessioniPrimary (citable) accession number: Q63921
Secondary accession number(s): Q62731, Q63684
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: September 3, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The conversion of arachidonate to prostaglandin H2 is a 2 step reaction: a cyclooxygenase (COX) reaction which converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The cyclooxygenase reaction occurs in a hydrophobic channel in the core of the enzyme. The peroxidase reaction occurs at a heme-containing active site located near the protein surface. The nonsteroidal anti-inflammatory drugs (NSAIDs) binding site corresponds to the cyclooxygenase active site.
Conversion of arachidonate to prostaglandin H2 is mediated by 2 different isozymes: the constitutive PTGS1 and the inducible PTGS2. PGHS1 is expressed constitutively and generally produces prostanoids acutely in response to hormonal stimuli to fine-tune physiological processes requiring instantaneous, continuous regulation (e.g. hemostasis). PGHS2 is inducible and typically produces prostanoids that mediate responses to physiological stresses such as infection and inflammation.
PTGS1 and PTGS2 are the targets of nonsteroidal anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen. Aspirin is able to produce an irreversible inactivation of the enzyme through a serine acetylation. Inhibition of the PGHSs with NSAIDs acutely reduces inflammation, pain, and fever, and long-term use of these drugs reduces fatal thrombotic events, as well as the development of colon cancer and Alzheimer's disease. PTGS2 is the principal isozyme responsible for production of inflammatory prostaglandins. New generation PTGSs inhibitors strive to be selective for PTGS2, to avoid side effects such as gastrointestinal complications and ulceration.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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