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O35074 (PTGIS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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).

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_processapoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

cellular 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 execution phase of apoptosis

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

regulation of apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

   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 sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionheme binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Prostacyclin synthase
PRO_0000051911

Regions

Transmembrane1 – 2121Helical; Potential

Sites

Metal binding4421Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
O35074 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F018F85D3A1B0EBB

FASTA50157,047
        10         20         30         40         50         60 
MSWAALLGLL AVLLLLLLLL SRRRARRPGE PPLDLGSIPW LGHALEFGRD AASFLTRMKE 

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

       130        140        150        160        170        180 
EKARMKPTLM HRDLQALTEA MYTNLRTVLL GDSTEAGSGW QETGLLEFSY NALLSAGYLT 

       190        200        210        220        230        240 
LYGVEASPRT HESQAQDRVH SADVFHTFRQ LDLLLPKLAR GSLSAGDKDH ACSVKNRLWK 

       250        260        270        280        290        300 
LLSPARLASR ADRSSWLESY LRHLEEMGVS EEMQARALVL QLWATQGNMG PTAFWLLLFL 

       310        320        330        340        350        360 
LKNPEALAAV RAELKHTVWQ AEQPVSQMTT LPQKILDSMP VLDSVLNETL RLTAAPFITR 

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

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

       490        500 
RYGFGLMQPE EDVPIRYRAR L 

« Hide

References

« Hide 'large scale' references
[1]"Inverse gene expression of prostacyclin and thromboxane synthases in resident and activated peritoneal macrophages."
Kuwamoto S., Inoue H., Tone Y., Izumi Y., Tanabe T.
FEBS Lett. 409:242-246(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Peritoneal macrophage.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[3]"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: Limb.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB001607 mRNA. Translation: BAA21717.1.
AK076585 mRNA. Translation: BAC36403.1.
BC062151 mRNA. Translation: AAH62151.1.
CCDSCCDS17097.1.
RefSeqNP_032994.1. NM_008968.3.
UniGeneMm.2339.

3D structure databases

ProteinModelPortalO35074.
SMRO35074. Positions 24-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO35074. 1 interaction.
MINTMINT-4109067.
STRING10090.ENSMUSP00000085357.

PTM databases

PhosphoSiteO35074.

Proteomic databases

MaxQBO35074.
PaxDbO35074.
PRIDEO35074.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018113; ENSMUSP00000018113; ENSMUSG00000017969.
GeneID19223.
KEGGmmu:19223.
UCSCuc008nzl.1. mouse.

Organism-specific databases

CTD5740.
MGIMGI:1097156. Ptgis.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00550000074551.
HOGENOMHOG000231026.
HOVERGENHBG051100.
KOK01831.
TreeFamTF105090.

Gene expression databases

ArrayExpressO35074.
BgeeO35074.
CleanExMM_PTGIS.
GenevestigatorO35074.

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. 1 hit.
[Graphical view]
PIRSFPIRSF000047. Cytochrome_CYPVIIA1. 1 hit.
PIRSF500628. PTGIS. 1 hit.
PRINTSPR00465. EP450IV.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
ProtoNetSearch...

Other

NextBio296004.
PROO35074.
SOURCESearch...

Entry information

Entry namePTGIS_MOUSE
AccessionPrimary (citable) accession number: O35074
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 118 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot