Prostaglandin G/H synthase 1 precursor - Oryctolagus cuniculus (Rabbit)

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O97554 (PGH1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. 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 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:	COX1

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	606 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 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 By similarity. Endoplasmic reticulum membrane; Peripheral membrane protein 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	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	prostaglandin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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 electronic annotation. Source: InterPro 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 electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

Potential

Chain

31 – 606

576

Prostaglandin G/H synthase 1

PRO_0000041818

Regions

Domain

38 – 76

EGF-like

Sites

Active site

213

Proton acceptor By similarity

Active site

391

For cyclooxygenase activity By similarity

Metal binding

394

Iron (heme axial ligand) By similarity

Site

536

Aspirin-acetylated serine By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

110

N-linked (GlcNAc...) Potential

Glycosylation

150

N-linked (GlcNAc...) Potential

Glycosylation

416

N-linked (GlcNAc...) Potential

Disulfide bond

42 ↔ 53

By similarity

Disulfide bond

43 ↔ 165

By similarity

Disulfide bond

47 ↔ 63

By similarity

Disulfide bond

65 ↔ 75

By similarity

Disulfide bond

575 ↔ 581

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O97554 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: DB751FD1E2F1CD77
Show »

FASTA

606

69,076

        10         20         30         40         50         60 
MSRSSPSLRL PVLLLLLLLL LLPPPPPVLP ADPGAPAPVN PCCYFPCQHQ GVCVRVALDR 

        70         80         90        100        110        120 
YQCDCTRTGY SGPNCTVPDL WTWLRSSLRP SPTFVHYLLT HVRWFWEFVN ATFIRDTLMR 

       130        140        150        160        170        180 
LVLTVRSNLI PSPPTYNLDY DYISWEAFSN VSYYTRVLPS VPKDCPTPMG TKGKKQLPDA 

       190        200        210        220        230        240 
QVLAHRFLLR RTFIPDPQGT NLMFAFFAQH FTHQFFKTSG KMGPGFTKAL GHGVDLGHIY 

       250        260        270        280        290        300 
GDSLERQYHL RLFKDGKLKY QVLDGEVYPP SVEEAPVLMH YPRGVPPRSQ MAVGQEVFGL 

       310        320        330        340        350        360 
LPGLMLYATL WLREHNRVCD LLKAEHPTWD DEQLFQTTRL ILIGETIKIV IEEYVQQLSG 

       370        380        390        400        410        420 
YFLQLKFDPE MLFSVQFQYR NRIAMEFNHL YHWHPLMPDS FQVGSQEYSY EQFLFNTSML 

       430        440        450        460        470        480 
VDYGVEALVD AFSRQSAGRI GGGRNIDHHV LHVAVEVIKE SREMRLQPFN EYRKRFGLKP 

       490        500        510        520        530        540 
YASFQELTGE TEMAAELEEL YGDIDALEFY PGLLLEKCQP NSIFGESMIE IGAPFSLKGL 

       550        560        570        580        590        600 
LGNPICSPEY WKPSTFGGEV GSNLIKTATL KKLVCLNTKT CPYVSFRVPR SSGDDGPAAE 


RRSTEL

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References

[1]

"Intrarenal localization of cyclooxygenase-1 and -2 and their differential expression in acute hydronephrotic kidney."
Guan Y., Zhang Y., Breyer R.M., Davis L., Redha R., Chang S., Breyer M.D.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF026008 mRNA. Translation: AAD01796.1.
RefSeq	NP_001076150.1. NM_001082681.1.
UniGene	Ocu.2320.
3D structure databases
ProteinModelPortal	O97554.
SMR	O97554. Positions 37-589.
ModBase	Search...
Protein-protein interaction databases
STRING	9986.ENSOCUP00000016903.
Protein family/group databases
PeroxiBase	4131. OcuPGHS01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100009407.
Organism-specific databases
CTD	100136038.
Phylogenomic databases
eggNOG	NOG39991.
HOGENOM	HOG000013149.
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. 2 hits. [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	O97554.
ChEMBL	CHEMBL3334.

Entry information

Entry name

PGH1_RABIT

Accession

Primary (citable) accession number: O97554

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 85 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-protein interaction databases

Protein family/group 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