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Q16647

- PTGIS_HUMAN

UniProt

Q16647 - PTGIS_HUMAN

Protein

Prostacyclin synthase

Gene

PTGIS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    (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.

    Cofactori

    Heme group.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi441 – 4411Iron (heme axial ligand)

    GO - Molecular functioni

    1. heme binding Source: UniProtKB
    2. iron ion binding Source: InterPro
    3. monooxygenase activity Source: InterPro
    4. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Source: InterPro
    5. prostaglandin-I synthase activity Source: UniProtKB
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic signaling pathway Source: UniProtKB
    2. arachidonic acid metabolic process Source: Reactome
    3. cellular response to hypoxia Source: UniProtKB
    4. cellular response to interleukin-1 Source: UniProtKB
    5. cellular response to interleukin-6 Source: UniProtKB
    6. cyclooxygenase pathway Source: Reactome
    7. icosanoid metabolic process Source: Reactome
    8. negative regulation of inflammatory response Source: UniProtKB
    9. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    10. negative regulation of nitric oxide biosynthetic process Source: UniProtKB
    11. positive regulation of angiogenesis Source: UniProtKB
    12. positive regulation of execution phase of apoptosis Source: UniProtKB
    13. positive regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
    14. prostaglandin biosynthetic process Source: UniProtKB
    15. small molecule metabolic process Source: Reactome
    16. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04738-MONOMER.
    ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_13438. Sterols are 12-hydroxylated by CYP8B1.
    REACT_13645. Eicosanoids.
    REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prostacyclin synthase (EC:5.3.99.4)
    Alternative name(s):
    Prostaglandin I2 synthase
    Gene namesi
    Name:PTGIS
    Synonyms:CYP8, CYP8A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:9603. PTGIS.

    Subcellular locationi

    GO - Cellular componenti

    1. caveola Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. endoplasmic reticulum membrane Source: Reactome
    4. extracellular space Source: UniProtKB
    5. integral component of membrane Source: UniProtKB-KW
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA292.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 500500Prostacyclin synthasePRO_0000051910Add
    BLAST

    Proteomic databases

    MaxQBiQ16647.
    PaxDbiQ16647.
    PRIDEiQ16647.

    PTM databases

    PhosphoSiteiQ16647.

    Expressioni

    Tissue specificityi

    Widely expressed; particularly abundant in ovary, heart, skeletal muscle, lung and prostate.

    Gene expression databases

    ArrayExpressiQ16647.
    BgeeiQ16647.
    CleanExiHS_PTGIS.
    GenevestigatoriQ16647.

    Organism-specific databases

    HPAiCAB009517.
    HPA014193.

    Interactioni

    Protein-protein interaction databases

    BioGridi111712. 4 interactions.
    STRINGi9606.ENSP00000244043.

    Structurei

    Secondary structure

    1
    500
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni38 – 403
    Helixi43 – 486
    Helixi50 – 6112
    Beta strandi63 – 697
    Beta strandi72 – 776
    Helixi80 – 823
    Helixi83 – 875
    Turni91 – 933
    Beta strandi94 – 963
    Helixi98 – 1069
    Helixi117 – 1259
    Helixi130 – 15526
    Beta strandi160 – 1634
    Helixi164 – 18118
    Helixi190 – 21930
    Helixi224 – 24017
    Helixi243 – 2464
    Helixi254 – 26512
    Helixi270 – 28516
    Helixi288 – 30013
    Helixi303 – 31816
    Helixi333 – 3364
    Helixi339 – 35214
    Beta strandi357 – 3615
    Beta strandi365 – 3684
    Beta strandi374 – 3774
    Beta strandi382 – 3854
    Helixi388 – 3925
    Turni395 – 3973
    Beta strandi398 – 4003
    Turni406 – 4094
    Beta strandi414 – 4163
    Helixi444 – 46017
    Beta strandi462 – 4687
    Helixi478 – 4803
    Beta strandi482 – 4854
    Beta strandi488 – 4903
    Beta strandi493 – 4986

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IAGX-ray2.15A/B23-500[»]
    3B6HX-ray1.62A/B18-500[»]
    ProteinModelPortaliQ16647.
    SMRiQ16647. Positions 23-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16647.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1 – 2020HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2124.
    HOVERGENiHBG051100.
    InParanoidiQ16647.
    KOiK01831.
    OMAiSQMTTLP.
    OrthoDBiEOG7J9VP6.
    PhylomeDBiQ16647.
    TreeFamiTF105090.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR024204. Cyt_P450_CYP7A1-type.
    IPR002403. Cyt_P450_E_grp-IV.
    IPR027286. PTGIS.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000047. Cytochrome_CYPVIIA1. 1 hit.
    PIRSF500628. PTGIS. 1 hit.
    PRINTSiPR00465. EP450IV.
    SUPFAMiSSF48264. SSF48264. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q16647-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAWAALLGLL AALLLLLLLS RRRTRRPGEP PLDLGSIPWL GYALDFGKDA    50
    ASFLTRMKEK HGDIFTILVG GRYVTVLLDP HSYDAVVWEP RTRLDFHAYA 100
    IFLMERIFDV QLPHYSPSDE KARMKLTLLH RELQALTEAM YTNLHAVLLG 150
    DATEAGSGWH EMGLLDFSYS FLLRAGYLTL YGIEALPRTH ESQAQDRVHS 200
    ADVFHTFRQL DRLLPKLARG SLSVGDKDHM CSVKSRLWKL LSPARLARRA 250
    HRSKWLESYL LHLEEMGVSE EMQARALVLQ LWATQGNMGP AAFWLLLFLL 300
    KNPEALAAVR GELESILWQA EQPVSQTTTL PQKVLDSTPV LDSVLSESLR 350
    LTAAPFITRE VVVDLAMPMA DGREFNLRRG DRLLLFPFLS PQRDPEIYTD 400
    PEVFKYNRFL NPDGSEKKDF YKDGKRLKNY NMPWGAGHNH CLGRSYAVNS 450
    IKQFVFLVLV HLDLELINAD VEIPEFDLSR YGFGLMQPEH DVPVRYRIRP 500
    Length:500
    Mass (Da):57,104
    Last modified:November 1, 1996 - v1
    Checksum:i39595442BFC0B625
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381P → L in allele CYP8A1*2. 1 Publication
    VAR_010915
    Natural varianti118 – 1181S → R in allele CYP8A1*3. 1 Publication
    Corresponds to variant rs5622 [ dbSNP | Ensembl ].
    VAR_010916
    Natural varianti154 – 1541E → A.
    Corresponds to variant rs5623 [ dbSNP | Ensembl ].
    VAR_014634
    Natural varianti171 – 1711F → L.
    Corresponds to variant rs5624 [ dbSNP | Ensembl ].
    VAR_014635
    Natural varianti236 – 2361R → C.
    Corresponds to variant rs5626 [ dbSNP | Ensembl ].
    VAR_014636
    Natural varianti379 – 3791R → S in allele CYP8A1*4. 1 Publication
    Corresponds to variant rs56195291 [ dbSNP | Ensembl ].
    VAR_010917
    Natural varianti500 – 5001P → S.
    Corresponds to variant rs5584 [ dbSNP | Ensembl ].
    VAR_014637

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38145 mRNA. Translation: BAA07343.1.
    AF297048 mRNA. Translation: AAG31781.1.
    AF297049 mRNA. Translation: AAG31782.1.
    AF297050 mRNA. Translation: AAG31783.1.
    AF297051 mRNA. Translation: AAG31784.1.
    AF297052 mRNA. Translation: AAG31785.1.
    AL118525 Genomic DNA. Translation: CAC14162.1.
    BC101809 mRNA. Translation: AAI01810.1.
    BC101811 mRNA. Translation: AAI01812.1.
    CCDSiCCDS13419.1.
    PIRiJC2231.
    RefSeqiNP_000952.1. NM_000961.3.
    UniGeneiHs.302085.

    Genome annotation databases

    EnsembliENST00000244043; ENSP00000244043; ENSG00000124212.
    GeneIDi5740.
    KEGGihsa:5740.
    UCSCiuc002xut.3. human.

    Polymorphism databases

    DMDMi2493373.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Cytochrome P450 Allele Nomenclature Committee

    CYP8A1 alleles

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38145 mRNA. Translation: BAA07343.1 .
    AF297048 mRNA. Translation: AAG31781.1 .
    AF297049 mRNA. Translation: AAG31782.1 .
    AF297050 mRNA. Translation: AAG31783.1 .
    AF297051 mRNA. Translation: AAG31784.1 .
    AF297052 mRNA. Translation: AAG31785.1 .
    AL118525 Genomic DNA. Translation: CAC14162.1 .
    BC101809 mRNA. Translation: AAI01810.1 .
    BC101811 mRNA. Translation: AAI01812.1 .
    CCDSi CCDS13419.1.
    PIRi JC2231.
    RefSeqi NP_000952.1. NM_000961.3.
    UniGenei Hs.302085.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IAG X-ray 2.15 A/B 23-500 [» ]
    3B6H X-ray 1.62 A/B 18-500 [» ]
    ProteinModelPortali Q16647.
    SMRi Q16647. Positions 23-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111712. 4 interactions.
    STRINGi 9606.ENSP00000244043.

    Chemistry

    BindingDBi Q16647.
    ChEMBLi CHEMBL4428.
    DrugBanki DB00812. Phenylbutazone.

    PTM databases

    PhosphoSitei Q16647.

    Polymorphism databases

    DMDMi 2493373.

    Proteomic databases

    MaxQBi Q16647.
    PaxDbi Q16647.
    PRIDEi Q16647.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244043 ; ENSP00000244043 ; ENSG00000124212 .
    GeneIDi 5740.
    KEGGi hsa:5740.
    UCSCi uc002xut.3. human.

    Organism-specific databases

    CTDi 5740.
    GeneCardsi GC20M048120.
    HGNCi HGNC:9603. PTGIS.
    HPAi CAB009517.
    HPA014193.
    MIMi 601699. gene.
    neXtProti NX_Q16647.
    PharmGKBi PA292.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2124.
    HOVERGENi HBG051100.
    InParanoidi Q16647.
    KOi K01831.
    OMAi SQMTTLP.
    OrthoDBi EOG7J9VP6.
    PhylomeDBi Q16647.
    TreeFami TF105090.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04738-MONOMER.
    Reactomei REACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_13438. Sterols are 12-hydroxylated by CYP8B1.
    REACT_13645. Eicosanoids.
    REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

    Miscellaneous databases

    EvolutionaryTracei Q16647.
    GeneWikii Prostacyclin_synthase.
    GenomeRNAii 5740.
    NextBioi 22344.
    PROi Q16647.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16647.
    Bgeei Q16647.
    CleanExi HS_PTGIS.
    Genevestigatori Q16647.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR024204. Cyt_P450_CYP7A1-type.
    IPR002403. Cyt_P450_E_grp-IV.
    IPR027286. PTGIS.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000047. Cytochrome_CYPVIIA1. 1 hit.
    PIRSF500628. PTGIS. 1 hit.
    PRINTSi PR00465. EP450IV.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Aorta.
    2. "Characterization of new mutations in the coding sequence and 5'-untranslated region of the human prostacyclin synthase gene (CYP8A1)."
      Chevalier D., Cauffiez C., Bernard C., Lo-Guidice J.-M., Allorge D., Fazio F., Ferrari N., Libersa C., Lhermitte M., D'Halluin J.C., Broly F.
      Hum. Genet. 108:148-155(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-38; ARG-118 AND SER-379.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain.
    5. "Crystal structure of the human prostacyclin synthase."
      Chiang C.W., Yeh H.C., Wang L.H., Chan N.L.
      J. Mol. Biol. 364:266-274(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 23-500 IN COMPLEX WITH HEME, COFACTOR.

    Entry informationi

    Entry nameiPTGIS_HUMAN
    AccessioniPrimary (citable) accession number: Q16647
    Secondary accession number(s): Q3MII8
    , Q9HAX2, Q9HAX3, Q9HAX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 146 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3