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Q62969 (PTGIS_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Prostacyclin synthase

EC=5.3.99.4
Alternative name(s):
Prostaglandin I2 synthase
Gene names
Name:Ptgis
Synonyms:Cyp8
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2) By similarity.

Catalytic activity

(5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-6,9-alpha-epoxy-11-alpha,15-dihydroxyprosta-5,13-dienoate.

Cofactor

Heme group By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Prostaglandin biosynthesis
Prostaglandin metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandHeme
Iron
Metal-binding
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to interleukin-1

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to interleukin-6

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of nitric oxide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peroxisome proliferator activated receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

prostaglandin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcaveola

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from direct assay PubMed 15684702. Source: RGD

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

monooxygenase activity

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen

Inferred from electronic annotation. Source: InterPro

prostaglandin-I synthase activity

Inferred from mutant phenotype PubMed 10359560. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Prostacyclin synthase
PRO_0000051912

Regions

Transmembrane1 – 2121Helical; Potential

Sites

Metal binding4421Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q62969 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D2D85ADF3C464863

FASTA50157,128
        10         20         30         40         50         60 
MSWAALLGLL AVLLLLLLLL SRRRARRPGE PPLDLGSIPW LGHALEFGKD AASFLTRMKE 

        70         80         90        100        110        120 
KHGDIFTVLV GGRYVTVLLD PHSYDTVVWD LRTRLDFHPY AIFLMERIFD LQLPNFNPSE 

       130        140        150        160        170        180 
EKARMKPTLM HKDLQALTEA MYTNLRTVLL GDSTEGGSGW QEKGLLEFSY SSLLSAGYLT 

       190        200        210        220        230        240 
LYGVEASPRT HESQALDRDH SADVFRTFRQ LDLMLPKLAR GSLSVGDKDH ACSVKSRLWK 

       250        260        270        280        290        300 
LLSPAGLASR ADRSSWLESY LRHLEEMGVS EDMQARALVL QLWATQGNMG PTAFWLLLFL 

       310        320        330        340        350        360 
LKNPEALDAV HAELKRIVWQ AEKPVLQMTA LPQKILDSMP VLDSVLNETL RLTAAPFITR 

       370        380        390        400        410        420 
EVMADLALPM ADRREFSLRR GDRLLLFPFL SPQKDPEIYT EPEVFKYNRF LNPDGSEKKD 

       430        440        450        460        470        480 
FYKDGKRLKN YNMPWGAGHN QCLGKSYAIN SIKQFVVLLL THFDLELVSE DTEVPEFDLS 

       490        500 
RYGFGLMQPE EDVPIRYRTR L 

« Hide

References

« Hide 'large scale' references
[1]Geraci M.W., Gao B., Shepherd D., Moore M., Vernon J., Miller Y.E., Voelkel N.F.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U53855 mRNA. Translation: AAB02322.1.
BC061814 mRNA. Translation: AAH61814.1.
IPIIPI00210318.
RefSeqNP_113745.1. NM_031557.2.
UniGeneRn.73051.

3D structure databases

ProteinModelPortalQ62969.
SMRQ62969. Positions 24-500.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000045949.

PTM databases

PhosphoSiteQ62969.

Proteomic databases

PRIDEQ62969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25527.
KEGGrno:25527.
UCSCRGD:3438. rat.

Organism-specific databases

CTD5740.
RGD3438. Ptgis.

Phylogenomic databases

eggNOGNOG288195.
HOGENOMHOG000231026.
HOVERGENHBG051100.
InParanoidQ62969.
KOK01831.

Enzyme and pathway databases

BRENDA5.3.99.4. 5301.

Gene expression databases

ArrayExpressQ62969.
GenevestigatorQ62969.
GermOnlineENSRNOG00000008245. Rattus norvegicus.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR024204. Cyt_P450_CYP7A1-type.
IPR002403. Cyt_P450_E_grp-IV.
IPR027286. PTGIS.
[Graphical view]
PfamPF00067. p450. 2 hits.
[Graphical view]
PIRSFPIRSF000047. Cytochrome_CYPVIIA1. 1 hit.
PIRSF500628. PTGIS. 1 hit.
PRINTSPR00465. EP450IV.
PR00385. P450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio607011.

Entry information

Entry namePTGIS_RAT
AccessionPrimary (citable) accession number: Q62969
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families