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O62725

- PGH2_NEOVI

UniProt

O62725 - PGH2_NEOVI

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Protein

Prostaglandin G/H synthase 2

Gene
PTGS2, COX2
Organism
Neovison vison (American mink) (Mustela vison)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. In cancer cells, PTGS2 is a key step in the production of prostaglandin E2 (PGE2), which plays important roles in modulating motility, proliferation and resistance to apoptosis By similarity.

Catalytic activityi

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

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061Substrate By similarity
Active sitei193 – 1931Proton acceptor By similarity
Binding sitei341 – 3411Substrate By similarity
Active sitei371 – 3711For cyclooxygenase activity By similarity
Binding sitei371 – 3711Substrate By similarity
Metal bindingi374 – 3741Iron (heme axial ligand) By similarity
Sitei516 – 5161Aspirin-acetylated serine By similarity

GO - Molecular functioni

  1. dioxygenase activity Source: UniProtKB-KW
  2. heme binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. peroxidase activity Source: UniProtKB-KW
  5. prostaglandin-endoperoxide synthase activity Source: UniProtKB

GO - Biological processi

  1. cyclooxygenase pathway Source: UniProtKB
  2. prostaglandin biosynthetic process Source: UniProtKB
  3. response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase, Peroxidase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00662.

Protein family/group databases

PeroxiBasei4136. MvPGHS02.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PTGS2
Synonyms:COX2
OrganismiNeovison vison (American mink) (Mustela vison)
Taxonomic identifieri452646 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaMustelidaeMustelinaeNeovison

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 By similarityAdd
BLAST
Chaini18 – 604587Prostaglandin G/H synthase 2PRO_0000023877Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 32 By similarity
Disulfide bondi22 ↔ 145 By similarity
Disulfide bondi26 ↔ 42 By similarity
Disulfide bondi44 ↔ 54 By similarity
Glycosylationi53 – 531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi130 – 1301N-linked (GlcNAc...) Reviewed prediction
Glycosylationi396 – 3961N-linked (GlcNAc...) Reviewed prediction
Modified residuei526 – 5261S-nitrosocysteine By similarity
Disulfide bondi555 ↔ 561 By similarity
Glycosylationi580 – 5801N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, S-nitrosylation

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliO62725.
SMRiO62725. Positions 18-569.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 5538EGF-likeAdd
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG000366.

Family and domain databases

Gene3Di1.10.640.10. 1 hit.
InterProiIPR029576. COX-2.
IPR000742. EG-like_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view]
PANTHERiPTHR11903:SF8. PTHR11903:SF8. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O62725-1 [UniParc]FASTAAdd to Basket

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MLARAGLLCA SLSPPHAANP CCSNPCQNQG VCMSIGFDQY MCDCSRTGFY    50
GENCSTPEFL TRVKLLLKPT PNTVHYILTH FKGVWNIVNK IPFLADVIMK 100
YVRTSRSHCI EPPPTYNVHY AYKSWEAFSN LSYYTRALPP VADDCPTPMG 150
VKGKKELPDS KEIVEKFLLR RKFIPDPQGT NMMFAFFAQH FTHQFFKTDH 200
KRGPGFTKGL GHGVDLSHVY GETLDRQHKL RLFKDGKMKY QVIDGEVYPP 250
TVKDTQVEMI YPPHVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD 300
VLKQEQGEWD DERLFRRSRL ILIGETIKIV IEDYVRHLSG YHFSLKFDPE 350
LLFNQQFQYQ NRIAAEFNTL YHWHPLLPDT LQIDDQEYNF QQFVYNNSIL 400
LEHGLTQFGE SFSRQIAGRV AGGRNVPAAV QQEQRASIDQ SRQMKYQSLN 450
EYRKRFSVKP YASFEELTGE KEMAGELKAL YQDIDAMELY PALLVEKPRP 500
DAIFGETMVE IGAPFSLKGL MGNPICSPDY WKPSHFGGEV GFKIINTASI 550
QSLICNNVKG CPFTAFSVQD PQLTKTVTIN GSSSHSGLDD INPTVLLKER 600
STEL 604
Length:604
Mass (Da):68,950
Last modified:August 1, 1998 - v1
Checksum:iE28D19F47CD926F8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF047841 mRNA. Translation: AAC05637.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF047841 mRNA. Translation: AAC05637.1 .

3D structure databases

ProteinModelPortali O62725.
SMRi O62725. Positions 18-569.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

PeroxiBasei 4136. MvPGHS02.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG000366.

Enzyme and pathway databases

UniPathwayi UPA00662 .

Family and domain databases

Gene3Di 1.10.640.10. 1 hit.
InterProi IPR029576. COX-2.
IPR000742. EG-like_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view ]
PANTHERi PTHR11903:SF8. PTHR11903:SF8. 1 hit.
Pfami PF03098. An_peroxidase. 1 hit.
[Graphical view ]
PRINTSi PR00457. ANPEROXIDASE.
SMARTi SM00181. EGF. 1 hit.
[Graphical view ]
SUPFAMi SSF48113. SSF48113. 1 hit.
PROSITEi PS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPGH2_NEOVI
AccessioniPrimary (citable) accession number: O62725
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: September 3, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The conversion of arachidonate to prostaglandin H2 is a 2 step reaction: a cyclooxygenase (COX) reaction which converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The cyclooxygenase reaction occurs in a hydrophobic channel in the core of the enzyme. The peroxidase reaction occurs at a heme-containing active site located near the protein surface. The nonsteroidal anti-inflammatory drugs (NSAIDs) binding site corresponds to the cyclooxygenase active site.
Conversion of arachidonate to prostaglandin H2 is mediated by 2 different isozymes: the constitutive PTGS1 and the inducible PTGS2. PGHS1 is expressed constitutively and generally produces prostanoids acutely in response to hormonal stimuli to fine-tune physiological processes requiring instantaneous, continuous regulation (e.g. hemostasis). PGHS2 is inducible and typically produces prostanoids that mediate responses to physiological stresses such as infection and inflammation.
PTGS1 and PTGS2 are the targets of nonsteroidal anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen. Aspirin is able to produce an irreversible inactivation of the enzyme through a serine acetylation. Inhibition of the PGHSs with NSAIDs acutely reduces inflammation, pain, and fever, and long-term use of these drugs reduces fatal thrombotic events, as well as the development of colon cancer and Alzheimer's disease. PTGS2 is the principal isozyme responsible for production of inflammatory prostaglandins. New generation PTGSs inhibitors strive to be selective for PTGS2, to avoid side effects such as gastrointestinal complications and ulceration.

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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