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Entry version 182 (11 Dec 2019)
Sequence version 1 (01 Jun 1994)
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Protein

Prostaglandin G/H synthase 2

Gene

Ptgs2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs), especially 15-R-lipoxin A4, that regulates phagocytic microglia (By similarity).By similarity

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

heme bBy similarityNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: prostaglandin biosynthesis

This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei106SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei193Proton acceptorPROSITE-ProRule annotation1
Binding sitei341SubstrateBy similarity1
Active sitei371For cyclooxygenase activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi374Iron (heme axial ligand)PROSITE-ProRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei516Aspirin-acetylated serineBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDioxygenase, Oxidoreductase, Peroxidase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.99.1 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-197264 Nicotinamide salvaging
R-RNO-2142770 Synthesis of 15-eicosatetraenoic acid derivatives
R-RNO-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
R-RNO-9018677 Biosynthesis of DHA-derived SPMs
R-RNO-9018679 Biosynthesis of EPA-derived SPMs
R-RNO-9025094 Biosynthesis of DPAn-3 SPMs
R-RNO-9027604 Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00662

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
3975 RnoPGHS02-A

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ptgs2
Synonyms:Cox-2, Cox2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Rat genome database

More...
RGDi
620349 Ptgs2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2977

DrugCentral

More...
DrugCentrali
P35355

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 171 PublicationAdd BLAST17
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002387918 – 604Prostaglandin G/H synthase 2Add BLAST587

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi21 ↔ 32By similarity
Disulfide bondi22 ↔ 145By similarity
Disulfide bondi26 ↔ 42By similarity
Disulfide bondi44 ↔ 54By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi130N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi396N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi555 ↔ 561By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei565O-acetylserineBy similarity1
Glycosylationi580N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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).By similarity
Acetylated at Ser-565 by SPHK1. During neuroinflammation, acetylation by SPHK1 promotes neuronal secretion of specialized preresolving mediators (SPMs), especially 15-R-lipoxin A4, which results in an increase of phagocytic microglia.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, S-nitrosylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P35355

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P35355

PRoteomics IDEntifications database

More...
PRIDEi
P35355

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P35355

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P35355

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed throughout the forebrain in discrete populations of neurons and is enriched in the cortex and hippocampus.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By cytokines and mitogens.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000002525 Expressed in 9 organ(s), highest expression level in Ammon's horn

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P35355 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
248163, 6 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P35355

Protein interaction database and analysis system

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IntActi
P35355, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000003567

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P35355

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P35355

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini18 – 55EGF-likePROSITE-ProRule annotationAdd BLAST38

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the prostaglandin G/H synthase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2408 Eukaryota
ENOG410XPZ3 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000010743

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000013149

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35355

KEGG Orthology (KO)

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KOi
K11987

Identification of Orthologs from Complete Genome Data

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OMAi
PTYNVHY

Database of Orthologous Groups

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OrthoDBi
324380at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P35355

TreeFam database of animal gene trees

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TreeFami
TF329675

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.640.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029576 COX-2
IPR000742 EGF-like_dom
IPR019791 Haem_peroxidase_animal
IPR010255 Haem_peroxidase_sf
IPR037120 Haem_peroxidase_sf_animal

The PANTHER Classification System

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PANTHERi
PTHR11903:SF8 PTHR11903:SF8, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF03098 An_peroxidase, 2 hits
PF00008 EGF, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00457 ANPEROXIDASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48113 SSF48113, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50026 EGF_3, 1 hit
PS50292 PEROXIDASE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P35355-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLFRAVLLCA ALALSHAANP CCSNPCQNRG ECMSIGFDQY KCDCTRTGFY
60 70 80 90 100
GENCTTPEFL TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRNSIMR
110 120 130 140 150
YVLTSRSHLI DSPPTYNVHY GYKSWEAFSN LSYYTRALPP VADDCPTPMG
160 170 180 190 200
VKGNKELPDS KEVLEKVLLR REFIPDPQGT NMMFAFFAQH FTHQFFKTDQ
210 220 230 240 250
KRGPGFTRGL GHGVDLNHVY GETLDRQHKL RLFQDGKLKY QVIGGEVYPP
260 270 280 290 300
TVKDTQVDMI YPPHVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD
310 320 330 340 350
ILKQEHPEWD DERLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE
360 370 380 390 400
LLFNQQFQYQ NRIASEFNTL YHWHPLLPDT FNIEDQEYTF KQFLYNNSIL
410 420 430 440 450
LEHGLAHFVE SFTRQIAGRV AGGRNVPIAV QAVAKASIDQ SREMKYQSLN
460 470 480 490 500
EYRKRFSLKP YTSFEELTGE KEMAAELKAL YHDIDAMELY PALLVEKPRP
510 520 530 540 550
DAIFGETMVE LGAPFSLKGL MGNPICSPQY WKPSTFGGEV GFRIINTASI
560 570 580 590 600
QSLICNNVKG CPFASFNVQD PQPTKTATIN ASASHSRLDD INPTVLIKRR

STEL
Length:604
Mass (Da):69,164
Last modified:June 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i98E418825D98FF0C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti11 – 13ALA → CPG (PubMed:8274023).Curated3
Sequence conflicti11 – 13ALA → CPG (PubMed:10816563).Curated3
Sequence conflicti58E → R (PubMed:8274023).Curated1
Sequence conflicti58E → R (PubMed:10816563).Curated1
Sequence conflicti66L → P (PubMed:8274023).Curated1
Sequence conflicti66L → P (PubMed:10816563).Curated1
Sequence conflicti96 – 98NSI → IQS (PubMed:8274023).Curated3
Sequence conflicti96 – 98NSI → IQS (PubMed:10816563).Curated3
Sequence conflicti339S → R (PubMed:8274023).Curated1
Sequence conflicti339S → R (PubMed:10816563).Curated1
Sequence conflicti344K → Q (PubMed:8274023).Curated1
Sequence conflicti344K → Q (PubMed:10816563).Curated1
Sequence conflicti350E → D (PubMed:8274023).Curated1
Sequence conflicti350E → D (PubMed:10816563).Curated1
Sequence conflicti368N → K (PubMed:8274023).Curated1
Sequence conflicti368N → K (PubMed:10816563).Curated1
Sequence conflicti573P → A (PubMed:8274023).Curated1
Sequence conflicti573P → A (PubMed:10816563).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L25925 mRNA Translation: AAA16477.1
U04300 mRNA Translation: AAA20246.1
U03389 mRNA Translation: AAA03466.1
S67722 mRNA Translation: AAB29401.1
AF233596 mRNA Translation: AAF36986.1

Protein sequence database of the Protein Information Resource

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PIRi
JC2030

NCBI Reference Sequences

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RefSeqi
NP_058928.3, NM_017232.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000003567; ENSRNOP00000003567; ENSRNOG00000002525

Database of genes from NCBI RefSeq genomes

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GeneIDi
29527

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:29527

UCSC genome browser

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UCSCi
RGD:620349 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25925 mRNA Translation: AAA16477.1
U04300 mRNA Translation: AAA20246.1
U03389 mRNA Translation: AAA03466.1
S67722 mRNA Translation: AAB29401.1
AF233596 mRNA Translation: AAF36986.1
PIRiJC2030
RefSeqiNP_058928.3, NM_017232.3

3D structure databases

SMRiP35355
ModBaseiSearch...

Protein-protein interaction databases

BioGridi248163, 6 interactors
CORUMiP35355
IntActiP35355, 1 interactor
STRINGi10116.ENSRNOP00000003567

Chemistry databases

BindingDBiP35355
ChEMBLiCHEMBL2977
DrugCentraliP35355

Protein family/group databases

PeroxiBasei3975 RnoPGHS02-A

PTM databases

iPTMnetiP35355
PhosphoSitePlusiP35355

Proteomic databases

jPOSTiP35355
PaxDbiP35355
PRIDEiP35355

Genome annotation databases

EnsembliENSRNOT00000003567; ENSRNOP00000003567; ENSRNOG00000002525
GeneIDi29527
KEGGirno:29527
UCSCiRGD:620349 rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5743
RGDi620349 Ptgs2

Phylogenomic databases

eggNOGiKOG2408 Eukaryota
ENOG410XPZ3 LUCA
GeneTreeiENSGT00390000010743
HOGENOMiHOG000013149
InParanoidiP35355
KOiK11987
OMAiPTYNVHY
OrthoDBi324380at2759
PhylomeDBiP35355
TreeFamiTF329675

Enzyme and pathway databases

UniPathwayiUPA00662
BRENDAi1.14.99.1 5301
ReactomeiR-RNO-197264 Nicotinamide salvaging
R-RNO-2142770 Synthesis of 15-eicosatetraenoic acid derivatives
R-RNO-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
R-RNO-9018677 Biosynthesis of DHA-derived SPMs
R-RNO-9018679 Biosynthesis of EPA-derived SPMs
R-RNO-9025094 Biosynthesis of DPAn-3 SPMs
R-RNO-9027604 Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives

Miscellaneous databases

Protein Ontology

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PROi
PR:P35355

Gene expression databases

BgeeiENSRNOG00000002525 Expressed in 9 organ(s), highest expression level in Ammon's horn
GenevisibleiP35355 RN

Family and domain databases

Gene3Di1.10.640.10, 1 hit
InterProiView protein in InterPro
IPR029576 COX-2
IPR000742 EGF-like_dom
IPR019791 Haem_peroxidase_animal
IPR010255 Haem_peroxidase_sf
IPR037120 Haem_peroxidase_sf_animal
PANTHERiPTHR11903:SF8 PTHR11903:SF8, 1 hit
PfamiView protein in Pfam
PF03098 An_peroxidase, 2 hits
PF00008 EGF, 1 hit
PRINTSiPR00457 ANPEROXIDASE
SUPFAMiSSF48113 SSF48113, 1 hit
PROSITEiView protein in PROSITE
PS50026 EGF_3, 1 hit
PS50292 PEROXIDASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPGH2_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P35355
Secondary accession number(s): Q64379, Q925V4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: December 11, 2019
This is version 182 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

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