Prostaglandin G/H synthase 1 precursor - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (?) or add your own

Q63921 (PGH1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 122. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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 1
EC=1.14.99.1

Alternative name(s):
Cyclooxygenase-1
Short name=COX-1
Prostaglandin H2 synthase 1
Short name=PGH synthase 1
Short name=PGHS-1
Short name=PHS 1
Prostaglandin-endoperoxide synthase 1

Gene names

Name:	Ptgs1
Synonyms:	Cox-1, Cox1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	602 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	May play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells.
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.
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	EGF-like domain Signal
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from expression pattern PubMed 17499644. Source: RGD learning Inferred from mutant phenotype PubMed 21701788. Source: RGD maintenance of blood-brain barrier Inferred from mutant phenotype PubMed 17704356. Source: RGD memory Inferred from mutant phenotype PubMed 21701788. Source: RGD negative regulation of epinephrine secretion Inferred from mutant phenotype PubMed 18598693. Source: RGD negative regulation of norepinephrine secretion Inferred from mutant phenotype PubMed 18598693. Source: RGD positive regulation of smooth muscle contraction Inferred from mutant phenotype PubMed 18480553. Source: RGD positive regulation of vasoconstriction Inferred from mutant phenotype PubMed 18456673. Source: RGD prostaglandin biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of blood pressure Inferred from sequence or structural similarity. Source: UniProtKB response to corticosterone stimulus Inferred from expression pattern PubMed 18584335. Source: RGD response to fatty acid Inferred from expression pattern PubMed 16983392. Source: RGD response to organic nitrogen Inferred from expression pattern PubMed 11211925. Source: RGD response to oxidative stress Inferred from electronic annotation. Source: InterPro sensory perception of pain Inferred from mutant phenotype PubMed 21362433. Source: RGD
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear envelope Inferred from direct assay PubMed 12657565. Source: RGD
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro lipid binding Inferred from mutant phenotype PubMed 17245358. Source: RGD 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 Traceable author statement PubMed 12657565. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

By similarity

Chain

27 – 602

576

Prostaglandin G/H synthase 1

PRO_0000023870

Regions

Domain

34 – 72

EGF-like

Sites

Active site

209

Proton acceptor By similarity

Active site

387

For cyclooxygenase activity By similarity

Metal binding

390

Iron (heme axial ligand) By similarity

Site

532

Aspirin-acetylated serine

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

106

N-linked (GlcNAc...) Potential

Glycosylation

146

N-linked (GlcNAc...) Potential

Glycosylation

412

N-linked (GlcNAc...) Potential

Disulfide bond

38 ↔ 49

By similarity

Disulfide bond

39 ↔ 161

By similarity

Disulfide bond

43 ↔ 59

By similarity

Disulfide bond

61 ↔ 71

By similarity

Disulfide bond

571 ↔ 577

By similarity

Experimental info

Sequence conflict

N → I in AAA03465. Ref.1

Sequence conflict

N → I in AAB29400. Ref.1

Sequence conflict

116 – 117

RL → GW Ref.1

Sequence conflict

119

I → L Ref.1

Sequence conflict

192

G → A in AAA03465. Ref.1

Sequence conflict

192

G → A in AAB29400. Ref.1

Sequence conflict

263

V → L in AAA03465. Ref.1

Sequence conflict

263

V → L in AAB29400. Ref.1

Sequence conflict

274

L → K in AAA03465. Ref.1

Sequence conflict

274

L → K in AAB29400. Ref.1

Sequence conflict

290

G → A in AAA03465. Ref.1

Sequence conflict

290

G → A in AAB29400. Ref.1

Sequence conflict

339

I → R in AAB29400. Ref.1

Sequence conflict

344

K → E in AAA03465. Ref.1

Sequence conflict

344

K → E in AAB29400. Ref.1

Sequence conflict

381

L → M in AAA03465. Ref.1

Sequence conflict

381

L → M in AAB29400. Ref.1

Sequence conflict

392

L → F in AAA03465. Ref.1

Sequence conflict

392

L → F in AAB29400. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q63921 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 0BFAF7EBFDA0C7C2
Show »

FASTA

602

69,032

        10         20         30         40         50         60 
MSRRSLSLQF PLLLLLLLLP PPPVLLTDAG VPSPVNPCCY YPCQNQGVCV RFGLDHYQCD 

        70         80         90        100        110        120 
CTRTGYSGPN CTIPEIWTWL RSSLRPSPSF THFLLTHGYW IWEFVNATFI REVLMRLVIT 

       130        140        150        160        170        180 
VRSNLIPSPP TYNTAHDYIS WESFSNVSYY TRILPSVPKD CPTPMGTKGK KQLPDIHLLA 

       190        200        210        220        230        240 
QRLLLRREFI PGPQGTNVLF AFFAQHFTHQ FFKTSGKMGP GFTKALGHGV DLGHIYGDSL 

       250        260        270        280        290        300 
ERQYHLRLFK DGKLKYQVLD GEVYPPSVEQ ASVLMRYPPG VPPEKQMAVG QEVFGLLPGL 

       310        320        330        340        350        360 
MLFSTIWLRE HNRVCDLLKE EHPTWDDEQL FQTTRLILIG ETIKIIIEEY VQHLSGYFLQ 

       370        380        390        400        410        420 
LKFDPELLFR AQFQYRNRIA LEFNHLYHWH PLMPDSFQVG SQEYSYEQFL FNTSMLVDYG 

       430        440        450        460        470        480 
VEALVDAFSR QRAGRIGGGR NFDYHVLHVA EDVIKESREM RLQSFNEYRK RFGLKPYTSF 

       490        500        510        520        530        540 
QEFTGEKEMA AELEELYGDI DALEFYPGLM LEKCQPNSLF GESMIEMGAP FSLKGLLGNP 

       550        560        570        580        590        600 
ICSPEYWKPS TFGGDVGFNI VNTASLKKLV CLNTKTCPYV SFRVPDYPGD DGSVFVRPST 


EL

« Hide

References

[1]	"Cloning two isoforms of rat cyclooxygenase: differential regulation of their expression." Feng L., Sun W., Xia Y., Tang W.W., Chanmugam P., Soyoola E., Wilson C.B., Hwang D. Arch. Biochem. Biophys. 307:361-368(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley.
[2]	"Analysis and quantitation of splicing variants of the TPA-inducible PGHS-1 mRNA in rat tracheal epithelial cells." Kitzler J., Hill E., Hardman R., Reddy N., Philpot R., Eling T.E. Arch. Biochem. Biophys. 316:856-863(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Fischer 344. Tissue: Trachea.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U03388 mRNA. Translation: AAA03465.1. S67721 mRNA. Translation: AAB29400.2. U18060 mRNA. Translation: AAA85823.1.
IPI	IPI00471895.
PIR	S39782. S69198.
RefSeq	NP_058739.3. NM_017043.3.
UniGene	Rn.44404.
3D structure databases
ProteinModelPortal	Q63921.
SMR	Q63921. Positions 34-586.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000010218.
Protein family/group databases
PeroxiBase	3974. RnoPGHS01.
Proteomic databases
PaxDb	Q63921.
PRIDE	Q63921.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	24693.
KEGG	rno:24693.
UCSC	RGD:3439. rat.
Organism-specific databases
CTD	5742.
RGD	3439. Ptgs1.
Phylogenomic databases
eggNOG	NOG39991.
HOGENOM	HOG000013149.
HOVERGEN	HBG000366.
InParanoid	Q63921.
KO	K00509.
OrthoDB	EOG402WRZ.
Enzyme and pathway databases
UniPathway	UPA00662.
Gene expression databases
ArrayExpress	Q63921.
Genevestigator	Q63921.
GermOnline	ENSRNOG00000007415. Rattus norvegicus.
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	Q63921.
ChEMBL	CHEMBL4042.
NextBio	604139.

Entry information

Entry name

PGH1_RAT

Accession

Primary (citable) accession number: Q63921
Secondary accession number(s): Q62731, Q63684

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 15, 1998
Last modified:	April 3, 2013
This is version 122 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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents