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O62698 (PGH2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prostaglandin G/H synthase 2

EC=1.14.99.1
Alternative name(s):
Cyclooxygenase-2
Short name=COX-2
PHS II
Prostaglandin H2 synthase 2
Short name=PGH synthase 2
Short name=PGHS-2
Prostaglandin-endoperoxide synthase 2
Gene names
Name:PTGS2
Synonyms:COX2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length604 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Mediates the formation of prostaglandins from arachidonate. May have a role as a major mediator of inflammation and/or a role for prostanoid signaling in activity-dependent plasticity. Critical component of colonic mucosal wound repair 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.

Post-translational modification

S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526 By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 604587Prostaglandin G/H synthase 2
PRO_0000023872

Regions

Domain18 – 5538EGF-like

Sites

Active site1931Proton acceptor By similarity
Active site3711For cyclooxygenase activity By similarity
Metal binding3741Iron (heme axial ligand) By similarity
Binding site1061Substrate By similarity
Binding site3411Substrate By similarity
Binding site3711Substrate By similarity
Site5161Aspirin-acetylated serine By similarity

Amino acid modifications

Modified residue5261S-nitrosocysteine By similarity
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation5801N-linked (GlcNAc...) Potential
Disulfide bond21 ↔ 32 By similarity
Disulfide bond22 ↔ 145 By similarity
Disulfide bond26 ↔ 42 By similarity
Disulfide bond44 ↔ 54 By similarity
Disulfide bond555 ↔ 561 By similarity

Experimental info

Sequence conflict61L → M in AAC28562. Ref.1
Sequence conflict1111E → D in AAC05592. Ref.2
Sequence conflict4581V → L in AAC28562. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O62698 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 16EA2E51D0A01A45

FASTA60469,163
        10         20         30         40         50         60 
MLARALLLCA AVALSGAANP CCSHPCQNRG VCMSVGFDQY KCDCTRTGFY GENCTTPEFL 

        70         80         90        100        110        120 
TRIKLLLKPT PNTVHYILTH FKGVWNIVNK ISFLRNMIMR YVLTSRSHLI ESPPTYNVHY 

       130        140        150        160        170        180 
SYKSWEAFSN LSYYTRALPP VPDDCPTPMG VKGRKELPDS KEVVKKVLLR RKFIPDPQGT 

       190        200        210        220        230        240 
NLMFAFFAQH FTHQFFKTDF ERGPAFTKGK NHGVDLSHIY GESLERQHKL RLFKDGKMKY 

       250        260        270        280        290        300 
QMINGEMYPP TVKDTQVEMI YPPHVPEHLK FAVGQEVFGL VPGLMMYATI WLREHNRVCD 

       310        320        330        340        350        360 
VLKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNQQFQYQ 

       370        380        390        400        410        420 
NRIAAEFNTL YHWHPLLPDV FQIDGQEYNY QQFIYNNSVL LEHGLTQFVE SFTRQRAGRV 

       430        440        450        460        470        480 
AGGRNLPVAV EKVSKASIDQ SREMKYQSFN EYRKRFLVKP YESFEELTGE KEMAAELEAL 

       490        500        510        520        530        540 
YGDIDAMEFY PALLVEKPRP DAIFGETMVE AGAPFSLKGL MGNPICSPEY WKPSTFGGEV 

       550        560        570        580        590        600 
GFKIINTASI QSLICSNVKG CPFTSFSVQD THLTKTVTIN ASSSHSGLDD INPTVLLKER 


STEL 

« Hide

References

[1]"Molecular characterization of bovine prostaglandin G/H synthase-2 and regulation in uterine stromal cells."
Liu J., Antaya M., Goff A.K., Boerboom D., Silversides D.W., Lussier J.G., Sirois J.
Biol. Reprod. 64:983-991(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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 105-253.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF031698 mRNA. Translation: AAC04702.1.
AF031699 Genomic DNA. Translation: AAC28562.1.
AF004944 mRNA. Translation: AAC05592.1.
RefSeqNP_776870.1. NM_174445.2.
UniGeneBt.15758.

3D structure databases

ProteinModelPortalO62698.
SMRO62698. Positions 18-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000018774.

Chemistry

BindingDBO62698.
ChEMBLCHEMBL2096674.

Protein family/group databases

PeroxiBase3330. BtPGHS02.

Proteomic databases

PRIDEO62698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID282023.
KEGGbta:282023.

Organism-specific databases

CTD5743.

Phylogenomic databases

eggNOGNOG39991.
HOGENOMHOG000013149.
HOVERGENHBG000366.
InParanoidO62698.
KOK11987.

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. 2 hits.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF48113. SSF48113. 1 hit.
PROSITEPS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805887.

Entry information

Entry namePGH2_BOVIN
AccessionPrimary (citable) accession number: O62698
Secondary accession number(s): O46517, O62665
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways