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Q13093

- PAFA_HUMAN

UniProt

Q13093 - PAFA_HUMAN

Protein

Platelet-activating factor acetylhydrolase

Gene

PLA2G7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids.

    Catalytic activityi

    1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei273 – 2731Nucleophile1 Publication
    Active sitei296 – 2961Charge relay system1 PublicationPROSITE-ProRule annotation
    Active sitei351 – 3511Charge relay system1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 1-alkyl-2-acetylglycerophosphocholine esterase activity Source: UniProtKB-EC
    2. calcium-independent phospholipase A2 activity Source: BHF-UCL
    3. phospholipid binding Source: BHF-UCL

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. lipid catabolic process Source: UniProtKB-KW
    3. lipid oxidation Source: BHF-UCL
    4. low-density lipoprotein particle remodeling Source: BHF-UCL
    5. plasma lipoprotein particle oxidation Source: BHF-UCL
    6. positive regulation of inflammatory response Source: BHF-UCL
    7. positive regulation of monocyte chemotaxis Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Enzyme and pathway databases

    BRENDAi3.1.1.4. 2681.
    ReactomeiREACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    SABIO-RKQ13093.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet-activating factor acetylhydrolase (EC:3.1.1.47)
    Short name:
    PAF acetylhydrolase
    Alternative name(s):
    1-alkyl-2-acetylglycerophosphocholine esterase
    2-acetyl-1-alkylglycerophosphocholine esterase
    Group-VIIA phospholipase A2
    Short name:
    gVIIA-PLA2
    LDL-associated phospholipase A2
    Short name:
    LDL-PLA(2)
    PAF 2-acylhydrolase
    Gene namesi
    Name:PLA2G7
    Synonyms:PAFAH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9040. PLA2G7.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular region Source: Reactome
    3. low-density lipoprotein particle Source: BHF-UCL

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Platelet-activating factor acetylhydrolase deficiency (PAFAD) [MIM:614278]: An enzymatic deficiency that results in exacerbated bodily response to inflammatory agents. It can be associated with several disease states including inflammatory gastrointestinal disorders, asthma and atopy. Asthmatic individuals with PAFAD may manifest aggravated respiratory symptoms.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti279 – 2791V → F in PAFAD; loss of function; risk factor for coronary arthery disease and stroke. 4 Publications
    Corresponds to variant rs16874954 [ dbSNP | Ensembl ].
    VAR_004268
    Natural varianti281 – 2811Q → R in PAFAD; loss of function. 1 Publication
    VAR_011585
    Asthma (ASTHMA) [MIM:600807]: The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with wheezing due to spasmodic contraction of the bronchi.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Atopic hypersensitivity (ATOPY) [MIM:147050]: A condition characterized by predisposition to develop hypersensitivity reactions. Atopic individuals can develop eczema, allergic rhinitis and allergic asthma.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi108 – 1081S → A: Activity is higher than wild-type. 1 Publication
    Mutagenesisi273 – 2731S → A: Loss of activity. 1 Publication
    Mutagenesisi286 – 2861D → A: Almost no activity. 1 Publication
    Mutagenesisi286 – 2861D → N: Diminishes activity. 1 Publication
    Mutagenesisi296 – 2961D → A: Loss of activity. 1 Publication
    Mutagenesisi296 – 2961D → N: Loss of activity. 1 Publication
    Mutagenesisi304 – 3041D → A: No change in activity. 1 Publication
    Mutagenesisi338 – 3381D → A: Activity is higher than wild-type. 1 Publication
    Mutagenesisi351 – 3511H → A: Loss of activity. 1 Publication

    Keywords - Diseasei

    Asthma, Disease mutation

    Organism-specific databases

    MIMi147050. phenotype.
    600807. phenotype.
    614278. phenotype.
    PharmGKBiPA33368.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 441420Platelet-activating factor acetylhydrolasePRO_0000017833Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi433 – 4331N-linked (GlcNAc...)

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ13093.
    PaxDbiQ13093.
    PRIDEiQ13093.

    Expressioni

    Tissue specificityi

    Plasma.

    Gene expression databases

    ArrayExpressiQ13093.
    BgeeiQ13093.
    CleanExiHS_PLA2G7.
    GenevestigatoriQ13093.

    Organism-specific databases

    HPAiHPA035915.

    Interactioni

    Protein-protein interaction databases

    BioGridi113667. 1 interaction.
    IntActiQ13093. 3 interactions.
    STRINGi9606.ENSP00000274793.

    Structurei

    Secondary structure

    1
    441
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi54 – 563
    Beta strandi61 – 7515
    Beta strandi78 – 8811
    Beta strandi95 – 984
    Helixi101 – 11111
    Helixi115 – 12511
    Beta strandi129 – 1346
    Beta strandi144 – 1507
    Turni157 – 1604
    Helixi161 – 1699
    Beta strandi173 – 1775
    Beta strandi184 – 1896
    Helixi193 – 1986
    Beta strandi202 – 2054
    Helixi211 – 2133
    Helixi214 – 24027
    Helixi255 – 2584
    Beta strandi262 – 27211
    Helixi274 – 28512
    Beta strandi291 – 2966
    Helixi304 – 3085
    Beta strandi314 – 3196
    Turni320 – 3223
    Helixi325 – 3328
    Beta strandi337 – 3393
    Beta strandi341 – 3466
    Helixi351 – 3544
    Helixi356 – 3594
    Helixi363 – 3686
    Helixi377 – 39620
    Helixi402 – 4054
    Helixi406 – 4094
    Beta strandi416 – 4194

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3D59X-ray1.50A/B47-429[»]
    3D5EX-ray2.10A/B47-429[»]
    3F96X-ray2.10A/B47-429[»]
    3F97X-ray1.70A/B47-429[»]
    3F98X-ray1.70A/B/C47-429[»]
    3F9CX-ray2.30A/B47-429[»]
    ProteinModelPortaliQ13093.
    SMRiQ13093. Positions 54-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13093.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. Lipase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4188.
    HOGENOMiHOG000008053.
    HOVERGENiHBG001322.
    InParanoidiQ13093.
    KOiK01062.
    OMAiWLMGNIL.
    OrthoDBiEOG7MSMQ5.
    PhylomeDBiQ13093.
    TreeFamiTF313831.

    Family and domain databases

    Gene3Di3.40.50.1820. 3 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR005065. PAF_acetylhydro.
    IPR016715. PAF_acetylhydro_eukaryote.
    [Graphical view]
    PANTHERiPTHR10272. PTHR10272. 1 hit.
    PfamiPF03403. PAF-AH_p_II. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018169. PAF_acetylhydrolase. 1 hit.
    SUPFAMiSSF53474. SSF53474. 3 hits.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q13093-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVPPKLHVLF CLCGCLAVVY PFDWQYINPV AHMKSSAWVN KIQVLMAAAS    50
    FGQTKIPRGN GPYSVGCTDL MFDHTNKGTF LRLYYPSQDN DRLDTLWIPN 100
    KEYFWGLSKF LGTHWLMGNI LRLLFGSMTT PANWNSPLRP GEKYPLVVFS 150
    HGLGAFRTLY SAIGIDLASH GFIVAAVEHR DRSASATYYF KDQSAAEIGD 200
    KSWLYLRTLK QEEETHIRNE QVRQRAKECS QALSLILDID HGKPVKNALD 250
    LKFDMEQLKD SIDREKIAVI GHSFGGATVI QTLSEDQRFR CGIALDAWMF 300
    PLGDEVYSRI PQPLFFINSE YFQYPANIIK MKKCYSPDKE RKMITIRGSV 350
    HQNFADFTFA TGKIIGHMLK LKGDIDSNVA IDLSNKASLA FLQKHLGLHK 400
    DFDQWDCLIE GDDENLIPGT NINTTNQHIM LQNSSGIEKY N 441
    Length:441
    Mass (Da):50,077
    Last modified:November 1, 1997 - v1
    Checksum:i3BA9EEA9E8094A57
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451L → P.1 Publication
    Corresponds to variant rs45521937 [ dbSNP | Ensembl ].
    VAR_047970
    Natural varianti92 – 921R → H Common polymorphism. 2 Publications
    Corresponds to variant rs1805017 [ dbSNP | Ensembl ].
    VAR_011583
    Natural varianti191 – 1911K → N.1 Publication
    Corresponds to variant rs45454695 [ dbSNP | Ensembl ].
    VAR_047971
    Natural varianti198 – 1981I → T Common polymorphism; associated with asthma and atopy. 2 Publications
    Corresponds to variant rs1805018 [ dbSNP | Ensembl ].
    VAR_011584
    Natural varianti279 – 2791V → F in PAFAD; loss of function; risk factor for coronary arthery disease and stroke. 4 Publications
    Corresponds to variant rs16874954 [ dbSNP | Ensembl ].
    VAR_004268
    Natural varianti281 – 2811Q → R in PAFAD; loss of function. 1 Publication
    VAR_011585
    Natural varianti379 – 3791V → A Common polymorphism. 4 Publications
    Corresponds to variant rs1051931 [ dbSNP | Ensembl ].
    VAR_011586

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20157 mRNA. Translation: AAC50126.1.
    U24577 mRNA. Translation: AAB04170.1.
    EF568110 Genomic DNA. Translation: ABQ01234.1.
    AL591242 Genomic DNA. Translation: CAH73907.1.
    CH471081 Genomic DNA. Translation: EAX04301.1.
    BC038452 mRNA. Translation: AAH38452.1.
    CCDSiCCDS4917.1.
    PIRiS60247.
    RefSeqiNP_001161829.1. NM_001168357.1.
    NP_005075.3. NM_005084.3.
    XP_005249465.1. XM_005249408.2.
    UniGeneiHs.584823.

    Genome annotation databases

    EnsembliENST00000274793; ENSP00000274793; ENSG00000146070.
    ENST00000537365; ENSP00000445666; ENSG00000146070.
    GeneIDi7941.
    KEGGihsa:7941.
    UCSCiuc010jzf.3. human.

    Polymorphism databases

    DMDMi2497687.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20157 mRNA. Translation: AAC50126.1 .
    U24577 mRNA. Translation: AAB04170.1 .
    EF568110 Genomic DNA. Translation: ABQ01234.1 .
    AL591242 Genomic DNA. Translation: CAH73907.1 .
    CH471081 Genomic DNA. Translation: EAX04301.1 .
    BC038452 mRNA. Translation: AAH38452.1 .
    CCDSi CCDS4917.1.
    PIRi S60247.
    RefSeqi NP_001161829.1. NM_001168357.1.
    NP_005075.3. NM_005084.3.
    XP_005249465.1. XM_005249408.2.
    UniGenei Hs.584823.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3D59 X-ray 1.50 A/B 47-429 [» ]
    3D5E X-ray 2.10 A/B 47-429 [» ]
    3F96 X-ray 2.10 A/B 47-429 [» ]
    3F97 X-ray 1.70 A/B 47-429 [» ]
    3F98 X-ray 1.70 A/B/C 47-429 [» ]
    3F9C X-ray 2.30 A/B 47-429 [» ]
    ProteinModelPortali Q13093.
    SMRi Q13093. Positions 54-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113667. 1 interaction.
    IntActi Q13093. 3 interactions.
    STRINGi 9606.ENSP00000274793.

    Chemistry

    BindingDBi Q13093.
    ChEMBLi CHEMBL3514.
    GuidetoPHARMACOLOGYi 1432.

    Polymorphism databases

    DMDMi 2497687.

    Proteomic databases

    MaxQBi Q13093.
    PaxDbi Q13093.
    PRIDEi Q13093.

    Protocols and materials databases

    DNASUi 7941.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274793 ; ENSP00000274793 ; ENSG00000146070 .
    ENST00000537365 ; ENSP00000445666 ; ENSG00000146070 .
    GeneIDi 7941.
    KEGGi hsa:7941.
    UCSCi uc010jzf.3. human.

    Organism-specific databases

    CTDi 7941.
    GeneCardsi GC06M046719.
    HGNCi HGNC:9040. PLA2G7.
    HPAi HPA035915.
    MIMi 147050. phenotype.
    600807. phenotype.
    601690. gene.
    614278. phenotype.
    neXtProti NX_Q13093.
    PharmGKBi PA33368.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4188.
    HOGENOMi HOG000008053.
    HOVERGENi HBG001322.
    InParanoidi Q13093.
    KOi K01062.
    OMAi WLMGNIL.
    OrthoDBi EOG7MSMQ5.
    PhylomeDBi Q13093.
    TreeFami TF313831.

    Enzyme and pathway databases

    BRENDAi 3.1.1.4. 2681.
    Reactomei REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    SABIO-RK Q13093.

    Miscellaneous databases

    EvolutionaryTracei Q13093.
    GeneWikii Lipoprotein-associated_phospholipase_A2.
    GenomeRNAii 7941.
    NextBioi 30458.
    PROi Q13093.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13093.
    Bgeei Q13093.
    CleanExi HS_PLA2G7.
    Genevestigatori Q13093.

    Family and domain databases

    Gene3Di 3.40.50.1820. 3 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR005065. PAF_acetylhydro.
    IPR016715. PAF_acetylhydro_eukaryote.
    [Graphical view ]
    PANTHERi PTHR10272. PTHR10272. 1 hit.
    Pfami PF03403. PAF-AH_p_II. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018169. PAF_acetylhydrolase. 1 hit.
    SUPFAMi SSF53474. SSF53474. 3 hits.
    PROSITEi PS00120. LIPASE_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-57.
      Tissue: Myeloid.
    2. "Purification, properties, sequencing, and cloning of a lipoprotein-associated, serine-dependent phospholipase involved in the oxidative modification of low-density lipoproteins."
      Tew D.G., Southan C., Rice S.Q.J., Lawrence M.P., Li H., Boyd H.F., Moores K., Gloger I.S., Macphee C.H.
      Arterioscler. Thromb. Vasc. Biol. 16:591-599(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Lymphoma.
    3. SeattleSNPs variation discovery resource
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-45; HIS-92; ASN-191; THR-198 AND ALA-379.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-379.
    6. "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], VARIANT ALA-379.
      Tissue: Blood.
    7. "Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad."
      Tjoelker L.W., Eberhardt C., Unger J., le Trong H., Zimmerman G.A., McIntyre T.M., Stafforini D.M., Prescott S.M., Gray P.W.
      J. Biol. Chem. 270:25481-25487(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    8. "Crystal structure of human plasma platelet-activating factor acetylhydrolase: structural implication to lipoprotein binding and catalysis."
      Samanta U., Bahnson B.J.
      J. Biol. Chem. 283:31617-31624(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 47-429 ALONE AND IN COMPLEX WITH PARAOXON, ACTIVE SITE.
    9. "Crystal structures of human group-VIIA phospholipase A2 inhibited by organophosphorus nerve agents exhibit non-aged complexes."
      Samanta U., Kirby S.D., Srinivasan P., Cerasoli D.M., Bahnson B.J.
      Biochem. Pharmacol. 78:420-429(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 47-429 IN COMPLEX WITH ORGANOPHOSPHORUS NERVE AGENTS.
    10. "Platelet-activating factor acetylhydrolase deficiency. A missense mutation near the active site of an anti-inflammatory phospholipase."
      Stafforini D.M., Satoh K., Atkinson D.L., Tjoelker L.W., Eberhardt C., Yoshida H., Imaizumi T., Takamatsu S., Zimmerman G.A., McIntyre T.M., Gray P.W., Prescott S.M.
      J. Clin. Invest. 97:2784-2791(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PAFAD PHE-279.
    11. "Loss of activity of plasma platelet-activating factor acetylhydrolase due to a novel Gln281-->Arg mutation."
      Yamada Y., Yokota M.
      Biochem. Biophys. Res. Commun. 236:772-775(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PAFAD ARG-281.
    12. "A mutation in plasma platelet-activating factor acetylhydrolase (Val279-->Phe) is a genetic risk factor for stroke."
      Hiramoto M., Yoshida H., Imaizumi T., Yoshimizu N., Satoh K.
      Stroke 28:2417-2420(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PAFAD PHE-279.
    13. "Identification of the G994--> T missense in exon 9 of the plasma platelet-activating factor acetylhydrolase gene as an independent risk factor for coronary artery disease in Japanese men."
      Yamada Y., Ichihara S., Fujimura T., Yokota M.
      Metabolism 47:177-181(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PAFAD PHE-279.
    14. "A mutation in plasma platelet-activating factor acetylhydrolase (Val279Phe) is a genetic risk factor for cerebral hemorrhage but not for hypertension."
      Yoshida H., Imaizumi T., Fujimoto K., Itaya H., Hiramoto M., Yoshimizu N., Fukushi K., Satoh K.
      Thromb. Haemost. 80:372-375(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PAFAD PHE-279.
    15. "The Ile198Thr and Ala379Val variants of plasmatic PAF-acetylhydrolase impair catalytical activities and are associated with atopy and asthma."
      Kruse S., Mao X.-Q., Heinzmann A., Blattmann S., Roberts M.H., Braun S., Gao P.-S., Forster J., Kuehr J., Hopkin J.M., Shirakawa T., Deichmann K.A.
      Am. J. Hum. Genet. 66:1522-1530(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIS-92; THR-198 AND ALA-379, INVOLVEMENT IN ASTHMA AND ATOPY.

    Entry informationi

    Entry nameiPAFA_HUMAN
    AccessioniPrimary (citable) accession number: Q13093
    Secondary accession number(s): A5HTT5
    , Q15692, Q5VTT1, Q8IVA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 143 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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