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Protein

Platelet-activating factor acetylhydrolase 2, cytoplasmic

Gene

PAFAH2

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

Functioni

Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position. May share a common physiologic function with the plasma-type enzyme.

Catalytic activityi

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

Enzyme regulationi

Inhibited by phenylmethanesulfonyl fluoride, 3,4,dichloroisocoumarin, diisopropyl fluorophosphate (DFP) and diethyl p-nitrophenyl phosphate (DENP).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei236 – 2361NucleophileBy similarity
Active sitei259 – 2591Charge relay systemPROSITE-ProRule annotation
Active sitei314 – 3141Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  1. 1-alkyl-2-acetylglycerophosphocholine esterase activity Source: UniProtKB-EC
  2. phospholipid binding Source: ProtInc

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
  2. lipid metabolic process Source: ProtInc
  3. negative regulation of apoptotic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.47. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-activating factor acetylhydrolase 2, cytoplasmic (EC:3.1.1.47)
Alternative name(s):
Serine-dependent phospholipase A2
Short name:
SD-PLA2
Short name:
hSD-PLA2
Gene namesi
Name:PAFAH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:8579. PAFAH2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392Platelet-activating factor acetylhydrolase 2, cytoplasmicPRO_0000090383Add
BLAST

Proteomic databases

MaxQBiQ99487.
PaxDbiQ99487.
PRIDEiQ99487.

PTM databases

PhosphoSiteiQ99487.

Expressioni

Tissue specificityi

Broadly expressed in different tissues, but high in B- and T-lymphocytes. In brain, expression is restricted to amygdala and frontal cortex.

Gene expression databases

BgeeiQ99487.
CleanExiHS_PAFAH2.
ExpressionAtlasiQ99487. baseline and differential.
GenevestigatoriQ99487.

Organism-specific databases

HPAiHPA018157.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9606.ENSP00000363400.

Structurei

3D structure databases

ProteinModelPortaliQ99487.
SMRiQ99487. Positions 10-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the serine esterase family.Curated

Phylogenomic databases

eggNOGiCOG4188.
GeneTreeiENSGT00390000005233.
HOGENOMiHOG000008053.
HOVERGENiHBG001322.
InParanoidiQ99487.
KOiK01062.
OMAiCMELASR.
OrthoDBiEOG7MSMQ5.
PhylomeDBiQ99487.
TreeFamiTF313831.

Family and domain databases

Gene3Di3.40.50.1820. 2 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. 2 hits.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVNQSVGFP PVTGPHLVGC GDVMEGQNLQ GSFFRLFYPC QKAEETMEQP
60 70 80 90 100
LWIPRYEYCT GLAEYLQFNK RCGGLLFNLA VGSCRLPVSW NGPFKTKDSG
110 120 130 140 150
YPLIIFSHGL GAFRTLYSAF CMELASRGFV VAVPEHRDRS AATTYFCKQA
160 170 180 190 200
PEENQPTNES LQEEWIPFRR VEEGEKEFHV RNPQVHQRVS ECLRVLKILQ
210 220 230 240 250
EVTAGQTVFN ILPGGLDLMT LKGNIDMSRV AVMGHSFGGA TAILALAKET
260 270 280 290 300
QFRCAVALDA WMFPLERDFY PKARGPVFFI NTEKFQTMES VNLMKKICAQ
310 320 330 340 350
HEQSRIITVL GSVHRSQTDF AFVTGNLIGK FFSTETRGSL DPYEGQEVMV
360 370 380 390
RAMLAFLQKH LDLKEDYNQW NNLIEGIGPS LTPGAPHHLS SL
Length:392
Mass (Da):44,036
Last modified:May 1, 1997 - v1
Checksum:i690FB7E6F5B68317
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121L → F in AAC39707 (PubMed:9494101).Curated

Mass spectrometryi

Molecular mass is 44162 Da from positions 1 - 392. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87845 mRNA. Translation: BAA13468.1.
U89386 mRNA. Translation: AAC39707.1.
AL592064 Genomic DNA. Translation: CAI10970.1.
CH471059 Genomic DNA. Translation: EAX07852.1.
CH471059 Genomic DNA. Translation: EAX07853.1.
BC001158 mRNA. Translation: AAH01158.1.
CCDSiCCDS270.1.
RefSeqiNP_000428.2. NM_000437.3.
XP_006710733.1. XM_006710670.1.
UniGeneiHs.477083.

Genome annotation databases

EnsembliENST00000374282; ENSP00000363400; ENSG00000158006.
ENST00000374284; ENSP00000363402; ENSG00000158006.
GeneIDi5051.
KEGGihsa:5051.
UCSCiuc001bld.4. human.

Polymorphism databases

DMDMi6647691.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87845 mRNA. Translation: BAA13468.1.
U89386 mRNA. Translation: AAC39707.1.
AL592064 Genomic DNA. Translation: CAI10970.1.
CH471059 Genomic DNA. Translation: EAX07852.1.
CH471059 Genomic DNA. Translation: EAX07853.1.
BC001158 mRNA. Translation: AAH01158.1.
CCDSiCCDS270.1.
RefSeqiNP_000428.2. NM_000437.3.
XP_006710733.1. XM_006710670.1.
UniGeneiHs.477083.

3D structure databases

ProteinModelPortaliQ99487.
SMRiQ99487. Positions 10-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000363400.

PTM databases

PhosphoSiteiQ99487.

Polymorphism databases

DMDMi6647691.

Proteomic databases

MaxQBiQ99487.
PaxDbiQ99487.
PRIDEiQ99487.

Protocols and materials databases

DNASUi5051.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374282; ENSP00000363400; ENSG00000158006.
ENST00000374284; ENSP00000363402; ENSG00000158006.
GeneIDi5051.
KEGGihsa:5051.
UCSCiuc001bld.4. human.

Organism-specific databases

CTDi5051.
GeneCardsiGC01M026286.
HGNCiHGNC:8579. PAFAH2.
HPAiHPA018157.
MIMi602344. gene.
neXtProtiNX_Q99487.
PharmGKBiPA32910.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4188.
GeneTreeiENSGT00390000005233.
HOGENOMiHOG000008053.
HOVERGENiHBG001322.
InParanoidiQ99487.
KOiK01062.
OMAiCMELASR.
OrthoDBiEOG7MSMQ5.
PhylomeDBiQ99487.
TreeFamiTF313831.

Enzyme and pathway databases

BRENDAi3.1.1.47. 2681.

Miscellaneous databases

ChiTaRSiPAFAH2. human.
GeneWikiiPAFAH2.
GenomeRNAii5051.
NextBioi19464.
PROiQ99487.
SOURCEiSearch...

Gene expression databases

BgeeiQ99487.
CleanExiHS_PAFAH2.
ExpressionAtlasiQ99487. baseline and differential.
GenevestigatoriQ99487.

Family and domain databases

Gene3Di3.40.50.1820. 2 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. 2 hits.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of intracellular platelet-activating factor (PAF) acetylhydrolase II. Its homology with plasma PAF acetylhydrolase."
    Hattori K., Adachi H., Matsuzawa A., Yamamoto K., Tsujimoto M., Aoki J., Hattori M., Arai H., Inoue K.
    J. Biol. Chem. 271:33032-33038(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Expression, purification and characterization of a human serine-dependent phospholipase A2 with high specificity for oxidized phospholipids and platelet activating factor."
    Rice S.Q.J., Southan C., Boyd H.F., Terrett J.A., Macphee C.H., Moores K., Gloger I.S., Tew D.G.
    Biochem. J. 330:1309-1315(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-5, MASS SPECTROMETRY.
    Tissue: Prostate.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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].
    Tissue: Eye.
  6. Cited for: REVIEW.

Entry informationi

Entry nameiPAFA2_HUMAN
AccessioniPrimary (citable) accession number: Q99487
Secondary accession number(s): D3DPK1, O15458, Q5SY02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: January 7, 2015
This is version 128 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.