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Q99487 (PAFA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PAFAH2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Enzyme regulation

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

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Tissue specificity

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

Sequence similarities

Belongs to the serine esterase family.

Mass spectrometry

Molecular mass is 44162 Da from positions 1 - 392. Determined by ESI. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392Platelet-activating factor acetylhydrolase 2, cytoplasmic
PRO_0000090383

Sites

Active site2361Nucleophile By similarity
Active site2591Charge relay system By similarity
Active site3141Charge relay system By similarity

Experimental info

Sequence conflict2121L → F in AAC39707. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99487 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 690FB7E6F5B68317

FASTA39244,036
        10         20         30         40         50         60 
MGVNQSVGFP PVTGPHLVGC GDVMEGQNLQ GSFFRLFYPC QKAEETMEQP LWIPRYEYCT 

        70         80         90        100        110        120 
GLAEYLQFNK RCGGLLFNLA VGSCRLPVSW NGPFKTKDSG YPLIIFSHGL GAFRTLYSAF 

       130        140        150        160        170        180 
CMELASRGFV VAVPEHRDRS AATTYFCKQA PEENQPTNES LQEEWIPFRR VEEGEKEFHV 

       190        200        210        220        230        240 
RNPQVHQRVS ECLRVLKILQ EVTAGQTVFN ILPGGLDLMT LKGNIDMSRV AVMGHSFGGA 

       250        260        270        280        290        300 
TAILALAKET QFRCAVALDA WMFPLERDFY PKARGPVFFI NTEKFQTMES VNLMKKICAQ 

       310        320        330        340        350        360 
HEQSRIITVL GSVHRSQTDF AFVTGNLIGK FFSTETRGSL DPYEGQEVMV RAMLAFLQKH 

       370        380        390 
LDLKEDYNQW NNLIEGIGPS LTPGAPHHLS SL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-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].
Tissue: Eye.
[6]"Platelet-activating factor acetylhydrolases."
Stafforini D.M., McIntyre T.M., Zimmerman G.A., Prescott S.M.
J. Biol. Chem. 272:17895-17898(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS270.1.
RefSeqNP_000428.2. NM_000437.3.
XP_006710733.1. XM_006710670.1.
UniGeneHs.477083.

3D structure databases

ProteinModelPortalQ99487.
SMRQ99487. Positions 10-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000363400.

PTM databases

PhosphoSiteQ99487.

Polymorphism databases

DMDM6647691.

Proteomic databases

MaxQBQ99487.
PaxDbQ99487.
PRIDEQ99487.

Protocols and materials databases

DNASU5051.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374282; ENSP00000363400; ENSG00000158006.
ENST00000374284; ENSP00000363402; ENSG00000158006.
GeneID5051.
KEGGhsa:5051.
UCSCuc001bld.4. human.

Organism-specific databases

CTD5051.
GeneCardsGC01M026286.
HGNCHGNC:8579. PAFAH2.
HPAHPA018157.
MIM602344. gene.
neXtProtNX_Q99487.
PharmGKBPA32910.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4188.
HOGENOMHOG000008053.
HOVERGENHBG001322.
InParanoidQ99487.
KOK01062.
OMAQFRCAVA.
OrthoDBEOG7MSMQ5.
PhylomeDBQ99487.
TreeFamTF313831.

Enzyme and pathway databases

BRENDA3.1.1.47. 2681.

Gene expression databases

ArrayExpressQ99487.
BgeeQ99487.
CleanExHS_PAFAH2.
GenevestigatorQ99487.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
IPR005065. PAF_acetylhydro.
IPR016715. PAF_acetylhydro_eukaryote.
[Graphical view]
PANTHERPTHR10272. PTHR10272. 1 hit.
PfamPF03403. PAF-AH_p_II. 1 hit.
[Graphical view]
PIRSFPIRSF018169. PAF_acetylhydrolase. 1 hit.
SUPFAMSSF53474. SSF53474. 2 hits.
PROSITEPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAFAH2. human.
GeneWikiPAFAH2.
GenomeRNAi5051.
NextBio19464.
PROQ99487.
SOURCESearch...

Entry information

Entry namePAFA2_HUMAN
AccessionPrimary (citable) accession number: Q99487
Secondary accession number(s): D3DPK1, O15458, Q5SY02
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM