Prostaglandin G/H synthase 2 precursor

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O62698 (PGH2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	604 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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 process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Prostaglandin biosynthesis Prostaglandin metabolism
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Signal
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein Phosphoprotein S-nitrosylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cyclooxygenase pathway Inferred from sequence or structural similarity. Source: UniProtKB response to oxidative stress Inferred from electronic annotation. Source: InterPro
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	heme 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

By similarity

Chain

18 – 604

587

Prostaglandin G/H synthase 2

PRO_0000023872

Regions

Domain

18 – 55

EGF-like

Sites

Active site

193

Proton acceptor By similarity

Active site

371

For cyclooxygenase activity By similarity

Metal binding

374

Iron (heme axial ligand) By similarity

Binding site

106

Substrate By similarity

Binding site

341

Substrate By similarity

Binding site

371

Substrate By similarity

Site

516

Aspirin-acetylated serine By similarity

Amino acid modifications

Modified residue

437

Phosphoserine By similarity

Modified residue

446

Phosphotyrosine By similarity

Modified residue

561

S-nitrosocysteine By similarity

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

130

N-linked (GlcNAc...) Potential

Glycosylation

396

N-linked (GlcNAc...) Potential

Glycosylation

580

N-linked (GlcNAc...) Potential

Disulfide bond

21 ↔ 32

By similarity

Disulfide bond

22 ↔ 145

By similarity

Disulfide bond

26 ↔ 42

By similarity

Disulfide bond

44 ↔ 54

By similarity

Disulfide bond

555 ↔ 561

By similarity

Experimental info

Sequence conflict

L → M in AAC28562. Ref.1

Sequence conflict

111

E → D in AAC05592. Ref.2

Sequence conflict

458

V → L in AAC28562. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O62698 [UniParc].

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

604

69,163

        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

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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.
IPI	IPI00687682.
RefSeq	NP_776870.1. NM_174445.2.
UniGene	Bt.15758.
3D structure databases
ProteinModelPortal	O62698.
SMR	O62698. Positions 18-569.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000018774.
Protein family/group databases
PeroxiBase	3330. BtPGHS02.
Proteomic databases
PRIDE	O62698.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	282023.
KEGG	bta:282023.
Organism-specific databases
CTD	5743.
Phylogenomic databases
eggNOG	NOG39991.
HOGENOM	HOG000013149.
HOVERGEN	HBG000366.
InParanoid	O62698.
KO	K11987.
OrthoDB	EOG4H19VF.
Enzyme and pathway databases
UniPathway	UPA00662.
Family and domain databases
Gene3D	1.10.640.10. 1 hit.
InterPro	IPR000742. EG-like_dom. IPR010255. Haem_peroxidase. IPR002007. Haem_peroxidase_animal. IPR019791. Haem_peroxidase_animal_subgr. [Graphical view]
Pfam	PF03098. An_peroxidase. 1 hit. [Graphical view]
PRINTS	PR00457. ANPEROXIDASE.
SMART	SM00181. EGF. 1 hit. [Graphical view]
SUPFAM	SSF48113. Peroxidase_super. 1 hit.
PROSITE	PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. PS50026. EGF_3. 1 hit. PS50292. PEROXIDASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O62698.
ChEMBL	CHEMBL3331.
NextBio	20805887.

Entry information

Entry name

PGH2_BOVIN

Accession

Primary (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 3, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents