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Protein

Platelet-activating factor acetylhydrolase

Gene

Pla2g7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 sitei272 – 2721NucleophileBy similarity
Active sitei295 – 2951Charge relay systemPROSITE-ProRule annotation
Active sitei350 – 3501Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. inflammatory response Source: MGI
  2. lipid catabolic process Source: UniProtKB-KW
  3. lipid oxidation Source: MGI
  4. low-density lipoprotein particle remodeling Source: MGI
  5. plasma lipoprotein particle oxidation Source: MGI
  6. positive regulation of monocyte chemotaxis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_233293. Synthesis, secretion, and deacylation of Ghrelin.

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
LDL-associated phospholipase A2
Short name:
LDL-PLA(2)
PAF 2-acylhydrolase
Gene namesi
Name:Pla2g7
Synonyms:Pafah
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1351327. Pla2g7.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. low-density lipoprotein particle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121By similarityAdd
BLAST
Chaini22 – 440419Platelet-activating factor acetylhydrolasePRO_0000017834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ60963.
PaxDbiQ60963.
PRIDEiQ60963.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiQ60963.
ExpressionAtlasiQ60963. baseline and differential.
GenevestigatoriQ60963.

Interactioni

Protein-protein interaction databases

IntActiQ60963. 1 interaction.
STRINGi10090.ENSMUSP00000024706.

Structurei

3D structure databases

ProteinModelPortaliQ60963.
SMRiQ60963. Positions 53-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4188.
GeneTreeiENSGT00390000005233.
HOGENOMiHOG000008053.
HOVERGENiHBG001322.
InParanoidiQ60963.
KOiK01062.
OMAiEYFLGLS.
PhylomeDBiQ60963.
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.

Q60963-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPLKLQALF CLLCCLPWVH PFHWQDTSSF DFRPSVMFHK LQSVMSAAGS
60 70 80 90 100
GHSKIPKGNG SYPVGCTDLM FGYGNESVFV RLYYPAQDQG RLDTVWIPNK
110 120 130 140 150
EYFLGLSIFL GTPSIVGNIL HLLYGSLTTP ASWNSPLRTG EKYPLIVFSH
160 170 180 190 200
GLGAFRTIYS AIGIGLASNG FIVATVEHRD RSASATYFFE DQVAAKVENR
210 220 230 240 250
SWLYLRKVKQ EESESVRKEQ VQQRAIECSR ALSAILDIEH GDPKENVLGS
260 270 280 290 300
AFDMKQLKDA IDETKIALMG HSFGGATVLQ ALSEDQRFRC GVALDPWMYP
310 320 330 340 350
VNEELYSRTL QPLLFINSAK FQTPKDIAKM KKFYQPDKER KMITIKGSVH
360 370 380 390 400
QNFDDFTFVT GKIIGNKLTL KGEIDSRVAI DLTNKASMAF LQKHLGLQKD
410 420 430 440
FDQWDPLVEG DDENLIPGSP FDAVTQVPAQ QHSPGSQTQN
Length:440
Mass (Da):49,258
Last modified:November 2, 2010 - v2
Checksum:i17C8B4D28F1ADC94
GO

Sequence cautioni

The sequence AAC52274.1 differs from that shown. Reason: Frameshift at positions 342 and 349. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti427 – 4271V → A in EDL23404 (PubMed:19468303).Curated
Sequence conflicti427 – 4271V → A in EDL23406 (PubMed:19468303).Curated
Sequence conflicti427 – 4271V → A in AAH10726 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34277 mRNA. Translation: AAC52274.1. Frameshift.
AK051454 mRNA. Translation: BAC34647.1.
CT010585 Genomic DNA. Translation: CAQ11111.1.
CH466559 Genomic DNA. Translation: EDL23404.1.
CH466559 Genomic DNA. Translation: EDL23406.1.
BC010726 mRNA. Translation: AAH10726.1.
CCDSiCCDS28796.1.
RefSeqiNP_038765.2. NM_013737.5.
XP_006524428.1. XM_006524365.1.
XP_006524429.1. XM_006524366.1.
UniGeneiMm.9277.

Genome annotation databases

EnsembliENSMUST00000024706; ENSMUSP00000024706; ENSMUSG00000023913.
GeneIDi27226.
KEGGimmu:27226.
UCSCiuc008cpd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34277 mRNA. Translation: AAC52274.1. Frameshift.
AK051454 mRNA. Translation: BAC34647.1.
CT010585 Genomic DNA. Translation: CAQ11111.1.
CH466559 Genomic DNA. Translation: EDL23404.1.
CH466559 Genomic DNA. Translation: EDL23406.1.
BC010726 mRNA. Translation: AAH10726.1.
CCDSiCCDS28796.1.
RefSeqiNP_038765.2. NM_013737.5.
XP_006524428.1. XM_006524365.1.
XP_006524429.1. XM_006524366.1.
UniGeneiMm.9277.

3D structure databases

ProteinModelPortaliQ60963.
SMRiQ60963. Positions 53-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ60963. 1 interaction.
STRINGi10090.ENSMUSP00000024706.

Chemistry

ChEMBLiCHEMBL5383.

Proteomic databases

MaxQBiQ60963.
PaxDbiQ60963.
PRIDEiQ60963.

Protocols and materials databases

DNASUi27226.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024706; ENSMUSP00000024706; ENSMUSG00000023913.
GeneIDi27226.
KEGGimmu:27226.
UCSCiuc008cpd.1. mouse.

Organism-specific databases

CTDi7941.
MGIiMGI:1351327. Pla2g7.

Phylogenomic databases

eggNOGiCOG4188.
GeneTreeiENSGT00390000005233.
HOGENOMiHOG000008053.
HOVERGENiHBG001322.
InParanoidiQ60963.
KOiK01062.
OMAiEYFLGLS.
PhylomeDBiQ60963.
TreeFamiTF313831.

Enzyme and pathway databases

ReactomeiREACT_233293. Synthesis, secretion, and deacylation of Ghrelin.

Miscellaneous databases

NextBioi305148.
PROiQ60963.
SOURCEiSearch...

Gene expression databases

BgeeiQ60963.
ExpressionAtlasiQ60963. baseline and differential.
GenevestigatoriQ60963.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Spleen.
  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.
    , 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: Spinal ganglion.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiPAFA_MOUSE
AccessioniPrimary (citable) accession number: Q60963
Secondary accession number(s): Q8BKM3, Q921T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 2, 2010
Last modified: February 4, 2015
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.