Q99487 (PAFA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

PAFAH2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-alkyl-2-acetylglycerophosphocholine esterase activity Inferred from electronic annotation. Source: EC phospholipid binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 392	392	Platelet-activating factor acetylhydrolase 2, cytoplasmic		PRO_0000090383
Sites
	Active site	236	1	Nucleophile By similarity
	Active site	259	1	Charge relay system By similarity
	Active site	314	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	176	1	N6-acetyllysine Ref.7
Experimental info
	Sequence conflict	212	1	L → F in AAC39707. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q99487 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 690FB7E6F5B68317	FASTA	392	44,036
	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

References

	« Hide 'large scale' referencesShow '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: 8955149] [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: 9494101] [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: 16710414] [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. , 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: 15489334] [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: 9218411] [Abstract] Cited for: REVIEW.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176, MASS SPECTROMETRY.
+	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.
IPI	IPI00015388.
RefSeq	NP_000428.2. NM_000437.3.
UniGene	Hs.477083.
3D structure databases
ProteinModelPortal	Q99487.
SMR	Q99487. Positions 5-388.
ModBase	Search...
Protein-protein interaction databases
STRING	Q99487.
PTM databases
PhosphoSite	Q99487.
Polymorphism databases
DMDM	6647691.
Proteomic databases
PRIDE	Q99487.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374282; ENSP00000363400; ENSG00000158006. ENST00000374284; ENSP00000363402; ENSG00000158006.
GeneID	5051.
KEGG	hsa:5051.
UCSC	uc001bld.2. human.
Organism-specific databases
CTD	5051.
GeneCards	GC01M026286.
H-InvDB	HIX0000282.
HGNC	HGNC:8579. PAFAH2.
HPA	HPA018157.
MIM	602344. gene.
neXtProt	NX_Q99487.
PharmGKB	PA32910.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18496.
GeneTree	ENSGT00390000005233.
HOGENOM	HBG713714.
HOVERGEN	HBG001322.
InParanoid	Q99487.
OMA	SLDPYEG.
OrthoDB	EOG45DWPG.
PhylomeDB	Q99487.
Enzyme and pathway databases
BRENDA	3.1.1.47. 2681.
Gene expression databases
ArrayExpress	Q99487.
Bgee	Q99487.
CleanEx	HS_PAFAH2.
Genevestigator	Q99487.
GermOnline	ENSG00000158006. Homo sapiens.
Family and domain databases
InterPro	IPR016715. Ac_Ohase_PAF. IPR005065. PAF_acetylhydro_II. [Graphical view]
KO	K01062.
PANTHER	PTHR10272. PAF_acetylhydro_II. 1 hit.
PIRSF	PIRSF018169. PAF_acetylhydrolase. 1 hit.
PROSITE	PS00120. LIPASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	19464.
SOURCE	Search...

Entry information

Entry name

PAFA2_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.