Prostaglandin G/H synthase 2 precursor - Neovison vison (American mink)

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O62725 (PGH2_NEOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. 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

Neovison vison (American mink) (Mustela vison)

Taxonomic identifier

452646 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Mustelidae › Mustelinae › Neovison

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
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_0000023877

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

Sequences

Sequence

Length

Mass (Da)

Tools

O62725 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: E28D19F47CD926F8
Show »

FASTA

604

68,950

        10         20         30         40         50         60 
MLARAGLLCA SLSPPHAANP CCSNPCQNQG VCMSIGFDQY MCDCSRTGFY GENCSTPEFL 

        70         80         90        100        110        120 
TRVKLLLKPT PNTVHYILTH FKGVWNIVNK IPFLADVIMK YVRTSRSHCI EPPPTYNVHY 

       130        140        150        160        170        180 
AYKSWEAFSN LSYYTRALPP VADDCPTPMG VKGKKELPDS KEIVEKFLLR RKFIPDPQGT 

       190        200        210        220        230        240 
NMMFAFFAQH FTHQFFKTDH KRGPGFTKGL GHGVDLSHVY GETLDRQHKL RLFKDGKMKY 

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

       310        320        330        340        350        360 
VLKQEQGEWD DERLFRRSRL ILIGETIKIV IEDYVRHLSG YHFSLKFDPE LLFNQQFQYQ 

       370        380        390        400        410        420 
NRIAAEFNTL YHWHPLLPDT LQIDDQEYNF QQFVYNNSIL LEHGLTQFGE SFSRQIAGRV 

       430        440        450        460        470        480 
AGGRNVPAAV QQEQRASIDQ SRQMKYQSLN EYRKRFSVKP YASFEELTGE KEMAGELKAL 

       490        500        510        520        530        540 
YQDIDAMELY PALLVEKPRP DAIFGETMVE IGAPFSLKGL MGNPICSPDY WKPSHFGGEV 

       550        560        570        580        590        600 
GFKIINTASI QSLICNNVKG CPFTAFSVQD PQLTKTVTIN GSSSHSGLDD INPTVLLKER 


STEL

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References

[1]

"Cloning, developmental expression, and immunohistochemistry of cyclooxygenase 2 in the endometrium during embryo implantation and gestation in the mink (Mustela vison)."
Song J.H., Sirois J., Houde A., Murphy B.D.
Endocrinology 139:3629-3636(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Uterus.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF047841 mRNA. Translation: AAC05637.1.
3D structure databases
ProteinModelPortal	O62725.
SMR	O62725. Positions 18-569.
ModBase	Search...
Protein family/group databases
PeroxiBase	4136. MvPGHS02.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG000366.
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...

Entry information

Entry name

PGH2_NEOVI

Accession

Primary (citable) accession number: O62725

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents