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O62664 (PGH1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:PTGS1
Synonyms:COX-1, COX1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length600 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells By similarity.

Catalytic activity

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

Cofactor

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

Pathway

Lipid metabolism; prostaglandin biosynthesis.

Subunit structure

Homodimer By similarity.

Subcellular location

Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.

Miscellaneous

This enzyme acts both as a dioxygenase and as a peroxidase.

This enzyme is the target of nonsteroidal anti-inflammatory drugs such as aspirin.

Sequence similarities

Belongs to the prostaglandin G/H synthase family.

Contains 1 EGF-like domain.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Prostaglandin biosynthesis
Prostaglandin metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   DomainEGF-like domain
Signal
   LigandHeme
Iron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcyclooxygenase pathway

Inferred from electronic annotation. Source: Compara

regulation of blood pressure

Inferred from electronic annotation. Source: Compara

regulation of cell proliferation

Inferred from electronic annotation. Source: Compara

response to oxidative stress

Inferred from electronic annotation. Source: InterPro

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

photoreceptor outer segment

Inferred from electronic annotation. Source: Compara

   Molecular_functionheme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen

Inferred from electronic annotation. Source: UniProtKB-KW

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

prostaglandin-endoperoxide synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 600576Prostaglandin G/H synthase 1
PRO_0000163113

Regions

Domain32 – 7039EGF-like

Sites

Active site2071Proton acceptor By similarity
Active site3851For cyclooxygenase activity By similarity
Metal binding3881Iron (heme axial ligand) By similarity
Site5301Aspirin-acetylated serine By similarity

Amino acid modifications

Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 47 By similarity
Disulfide bond37 ↔ 159 By similarity
Disulfide bond41 ↔ 57 By similarity
Disulfide bond59 ↔ 69 By similarity
Disulfide bond569 ↔ 575 By similarity

Experimental info

Sequence conflict2291D → G in AAC05591. Ref.2
Sequence conflict2411Q → R in AAC05591. Ref.2
Sequence conflict2631P → Q in AAC05591. Ref.2
Sequence conflict3201H → Q in AAC05591. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O62664 [UniParc].

Last modified February 5, 2008. Version 2.
Checksum: 0B43E65DA9E2A2E9

FASTA60068,805
        10         20         30         40         50         60 
MSRQGISLRF PLLLLLLSPS PVLPADPGAP APVNPCCYYP CQHQGICVRF GLDRYQCDCT 

        70         80         90        100        110        120 
RTGYYGPNCT IPEIWTWLRT TLRPSPSFVH FLLTHGRWLW DFVNATFIRD KLMRLVLTVR 

       130        140        150        160        170        180 
SNLIPSPPTY NVAHDYISWE SFSNVSYYTR ILPSVPRDCP TPMGTKGKKQ LPDAEFLSRR 

       190        200        210        220        230        240 
FLLRRKFIPD PQGTNLMFAF FAQHFTHQFF KTSGKMGPGF TKALGHGVDL GHIYGDNLER 

       250        260        270        280        290        300 
QYQLRLFKDG KLKYQMLNGE VYPPSVEEAP VLMHYPRGIP PQSQMAVGQE VFGLLPGLMV 

       310        320        330        340        350        360 
YATIWLREHN RVCDLLKAEH PTWGDEQLFQ TARLILIGET IKIVIEEYVQ QLSGYFLQLK 

       370        380        390        400        410        420 
FDPELLFGAQ FQYRNRIAME FNQLYHWHPL MPDSFRVGPQ DYSYEQFLFN TSMLVDYGVE 

       430        440        450        460        470        480 
ALVDAFSRQP AGRIGGGRNI DHHILHVAVD VIKESRELRL QPFNEYRKRF GMKPYTSFQE 

       490        500        510        520        530        540 
LTGEKEMAAE LEELYGDIDA LEFYPGLLLE KCHPNSIFGE SMIEMGAPFS LKGLLGNPIC 

       550        560        570        580        590        600 
SPEYWKASTF GGDVGFNLVK TATLKKLVCL NTKTCPYVSF HVPDPHREDR PGVERPPTEL

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Ascending colon.
[2]"Cellular mechanisms involved during oxytocin-induced prostaglandin F2alpha production in endometrial epithelial cells in vitro: role of cyclooxygenase-2."
Asselin E., Drolet P., Fortier M.A.
Endocrinology 138:4798-4805(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 121-379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC134517 mRNA. Translation: AAI34518.1.
AF004943 mRNA. Translation: AAC05591.1.
IPIIPI00688636.
RefSeqNP_001098793.1. NM_001105323.1.
UniGeneBt.2151.

3D structure databases

ProteinModelPortalO62664.
SMRO62664. Positions 32-584.
ModBaseSearch...

Protein family/group databases

PeroxiBase3332. BtPGHS01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000008833; ENSBTAP00000008833; ENSBTAG00000006716.
GeneID282022.
KEGGbta:282022.

Organism-specific databases

CTD5742.

Phylogenomic databases

eggNOGNOG39991.
GeneTreeENSGT00390000010743.
HOGENOMHOG000013149.
HOVERGENHBG000366.
InParanoidO62664.
KOK00509.
OMAFKTSGKM.
OrthoDBEOG402WRZ.

Enzyme and pathway databases

UniPathwayUPA00662.

Family and domain databases

Gene3D1.10.640.10. 1 hit.
InterProIPR000742. EG-like_dom.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00022. EGF_1. False negative.
PS01186. EGF_2. False negative.
PS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBO62664.
ChEMBLCHEMBL2860.
NextBio20805886.

Entry information

Entry namePGH1_BOVIN
AccessionPrimary (citable) accession number: O62664
Secondary accession number(s): A7YWD4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 5, 2008
Last modified: April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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