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O02768 (PGH2_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. 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 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:COX-2, COX2
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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 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.

Tissue specificity

Highest expression in kidney and urinary bladder.

Post-translational modification

S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-561 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.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Prostaglandin biosynthesis
Prostaglandin metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
S-nitrosylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanagen

Inferred from electronic annotation. Source: Compara

brown fat cell differentiation

Inferred from electronic annotation. Source: Compara

cellular response to hypoxia

Inferred from electronic annotation. Source: Compara

cyclooxygenase pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of brown fat cell differentiation

Inferred from electronic annotation. Source: Compara

positive regulation of fever generation

Inferred from electronic annotation. Source: Compara

regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell proliferation

Inferred from electronic annotation. Source: Compara

response to oxidative stress

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionheme binding

Inferred from sequence or structural similarity. Source: UniProtKB

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 sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 604587Prostaglandin G/H synthase 2
PRO_0000023878

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 residue4371Phosphoserine By similarity
Modified residue4461Phosphotyrosine By similarity
Modified residue5611S-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

Sequences

Sequence LengthMass (Da)Tools
O02768 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: C52F9F5BC1F493D7

FASTA60469,007
        10         20         30         40         50         60 
MLARALLLCA AVALSHAANP CCSNPCQNRG VCMTMGFDQY KCDCTRTGFY GENCSTPEFL 

        70         80         90        100        110        120 
TRIKLLLKPT PDTVHYILTH FKGVWNIVNS IPFLRNSIMK YVLTSRSHMI DSPPTYNVHY 

       130        140        150        160        170        180 
NYKSWEAFSN LSYYTRALPP VADDCPTPMG VKGKKELPDS KDVVEKLLLR RKFIPDPQGT 

       190        200        210        220        230        240 
NMMFAFFAQH FTHQFFKTDL KRGPAFTKGL GHGVDLNHIY GETLDRQHKL RLFKDGKMKY 

       250        260        270        280        290        300 
QVIDGEVYPP TVKDTQVEMI YPPHIPAHLQ FAVGQEVFGL VPGLMMYATI WLREHNRVCD 

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

       370        380        390        400        410        420 
NRIAAEFNTL YHWHPLLPDT FQIDDQQYNY QQFLYNNSIL LEHGLTQFVE SFTRQIAGRV 

       430        440        450        460        470        480 
AGGRNVPPAV QKVAKASIDQ SRQMKYQSLN EYRKRFLLKP YESFEELTGE KEMAAELEAL 

       490        500        510        520        530        540 
YGDIDAVELY PALLVERPRP DAIFGESMVE MGAPFSLKGL MGNPICSPNY WKPSTFGGEV 

       550        560        570        580        590        600 
GFKIVNTASI QSLICNNVKG CPFTSFNVPD PQLTKTVTIN ASASHSRLED INPTVLLKGR 


STEL

« Hide

References

[1]"Cloning, expression, and regulation of rabbit cyclooxygenase-2 in renal medullary interstitial cells."
Guan Y., Chang M., Cho W., Zhang Y., Redha R., Davis L., Chang S., Dubois R.N., Hao C.M., Breyer M.
Am. J. Physiol. 273:F18-F26(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U97696 mRNA. Translation: AAB71222.1.
RefSeqNP_001075857.1. NM_001082388.1.
UniGeneOcu.2173.

3D structure databases

ProteinModelPortalO02768.
SMRO02768. Positions 18-568.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000014415.

Protein family/group databases

PeroxiBase4130. OcuPGHS02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000016770; ENSOCUP00000014415; ENSOCUG00000016771.
GeneID100009248.

Organism-specific databases

CTD5743.

Phylogenomic databases

eggNOGNOG39991.
GeneTreeENSGT00390000010743.
HOGENOMHOG000013149.
HOVERGENHBG000366.
OMATHFKGVW.
OrthoDBEOG4H19VF.

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. 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

BindingDBO02768.
ChEMBLCHEMBL1293198.

Entry information

Entry namePGH2_RABIT
AccessionPrimary (citable) accession number: O02768
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: April 3, 2013
This is version 108 of the entry and version 1 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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