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Q13093

- PAFA_HUMAN

UniProt

Q13093 - PAFA_HUMAN

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Protein

Platelet-activating factor acetylhydrolase

Gene

PLA2G7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ13093.
CleanExiHS_PLA2G7.
GenevestigatoriQ13093.

Organism-specific databases

HPAiHPA035915.

Interactioni

Protein-protein interaction databases

BioGridi113667. 2 interactions.
IntActiQ13093. 3 interactions.
STRINGi9606.ENSP00000274793.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000005233.
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

        10         20         30         40         50
MVPPKLHVLF CLCGCLAVVY PFDWQYINPV AHMKSSAWVN KIQVLMAAAS
60 70 80 90 100
FGQTKIPRGN GPYSVGCTDL MFDHTNKGTF LRLYYPSQDN DRLDTLWIPN
110 120 130 140 150
KEYFWGLSKF LGTHWLMGNI LRLLFGSMTT PANWNSPLRP GEKYPLVVFS
160 170 180 190 200
HGLGAFRTLY SAIGIDLASH GFIVAAVEHR DRSASATYYF KDQSAAEIGD
210 220 230 240 250
KSWLYLRTLK QEEETHIRNE QVRQRAKECS QALSLILDID HGKPVKNALD
260 270 280 290 300
LKFDMEQLKD SIDREKIAVI GHSFGGATVI QTLSEDQRFR CGIALDAWMF
310 320 330 340 350
PLGDEVYSRI PQPLFFINSE YFQYPANIIK MKKCYSPDKE RKMITIRGSV
360 370 380 390 400
HQNFADFTFA TGKIIGHMLK LKGDIDSNVA IDLSNKASLA FLQKHLGLHK
410 420 430 440
DFDQWDCLIE GDDENLIPGT NINTTNQHIM LQNSSGIEKY N
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 2 interactions.
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.
GeneTreei ENSGT00390000005233.
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

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 145 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