Full text data of PAFAH1B2
PAFAH1B2
(PAFAHB)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Platelet-activating factor acetylhydrolase IB subunit beta; 3.1.1.47 (PAF acetylhydrolase 30 kDa subunit; PAF-AH 30 kDa subunit; PAF-AH subunit beta; PAFAH subunit beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Platelet-activating factor acetylhydrolase IB subunit beta; 3.1.1.47 (PAF acetylhydrolase 30 kDa subunit; PAF-AH 30 kDa subunit; PAF-AH subunit beta; PAFAH subunit beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00026546
IPI00026546 Platelet-activating factor acetylhydrolase IB beta subunit Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit, ubiquitous soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00026546 Platelet-activating factor acetylhydrolase IB beta subunit Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit, ubiquitous soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P68402
ID PA1B2_HUMAN Reviewed; 229 AA.
AC P68402; A8DPS5; A8DPS6; A8DPS7; E9PEJ5; E9PLP3; O00687; Q29459;
read moreAC Q6IBR6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit beta;
DE EC=3.1.1.47;
DE AltName: Full=PAF acetylhydrolase 30 kDa subunit;
DE Short=PAF-AH 30 kDa subunit;
DE AltName: Full=PAF-AH subunit beta;
DE Short=PAFAH subunit beta;
GN Name=PAFAH1B2; Synonyms=PAFAHB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal liver;
RX PubMed=9144386; DOI=10.1006/bbrc.1997.6383;
RA Adachi H., Tsujimoto M., Hattori M., Arai H., Inoue K.;
RT "Differential tissue distribution of the beta- and gamma-subunits of
RT human cytosolic platelet-activating factor acetylhydrolase (isoform
RT I).";
RL Biochem. Biophys. Res. Commun. 233:10-13(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Testis;
RX PubMed=18155631; DOI=10.1016/j.prostaglandins.2007.10.005;
RA Scott B.T., Olson N., Long G.L., Bovill E.G.;
RT "Novel isoforms of intracellular platelet activating factor
RT acetylhydrolase (PAFAH1b2) in human testis; encoded by alternatively
RT spliced mRNAs.";
RL Prostaglandins Other Lipid Mediat. 85:69-80(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G;);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 61-79, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Inactivates PAF by removing the acetyl group at the sn-2
CC position. This is a catalytic subunit.
CC -!- CATALYTIC ACTIVITY: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine +
CC H(2)O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.
CC -!- SUBUNIT: Cytosolic PAF-AH IB is formed of three subunits of 45 kDa
CC (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity
CC of the enzyme resides in the beta and gamma subunits, whereas the
CC alpha subunit has regulatory activity. Trimer formation is not
CC essential for the catalytic activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P68402-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P68402-2; Sequence=VSP_042896;
CC Name=3;
CC IsoId=P68402-3; Sequence=VSP_043217;
CC Name=4;
CC IsoId=P68402-4; Sequence=VSP_044680;
CC Note=Ref.2 (ABI58227/ABI58228) sequences are in conflict in
CC position: 151:V->M;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC Platelet-activating factor acetylhydrolase IB beta/gamma subunits
CC subfamily.
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DR EMBL; D63390; BAA19917.1; -; mRNA.
DR EMBL; DQ836738; ABI58225.1; -; mRNA.
DR EMBL; DQ836739; ABI58226.1; -; mRNA.
DR EMBL; DQ836740; ABI58227.1; -; mRNA.
DR EMBL; DQ836741; ABI58228.1; -; mRNA.
DR EMBL; DQ836742; ABI58229.1; -; mRNA.
DR EMBL; DQ836743; ABI58230.1; -; mRNA.
DR EMBL; AK292973; BAF85662.1; -; mRNA.
DR EMBL; CR456736; CAG33017.1; -; mRNA.
DR EMBL; EF445007; ACA06040.1; -; Genomic_DNA.
DR EMBL; AP005018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67281.1; -; Genomic_DNA.
DR EMBL; BC000398; AAH00398.1; -; mRNA.
DR EMBL; BC019301; AAH19301.1; -; mRNA.
DR PIR; JC5409; JC5409.
DR RefSeq; NP_001171675.1; NM_001184746.1.
DR RefSeq; NP_001171676.1; NM_001184747.1.
DR RefSeq; NP_001171677.1; NM_001184748.1.
DR RefSeq; NP_002563.1; NM_002572.3.
DR UniGene; Hs.728488; -.
DR PDB; 1VYH; X-ray; 3.40 A; A/B/E/F/I/J/M/N/Q/R=1-229.
DR PDBsum; 1VYH; -.
DR ProteinModelPortal; P68402; -.
DR SMR; P68402; 6-217.
DR IntAct; P68402; 15.
DR MINT; MINT-5002700; -.
DR STRING; 9606.ENSP00000304006; -.
DR ChEMBL; CHEMBL4463; -.
DR PhosphoSite; P68402; -.
DR DMDM; 55977294; -.
DR REPRODUCTION-2DPAGE; IPI00026546; -.
DR PaxDb; P68402; -.
DR PeptideAtlas; P68402; -.
DR PRIDE; P68402; -.
DR Ensembl; ENST00000419197; ENSP00000388742; ENSG00000168092.
DR Ensembl; ENST00000527958; ENSP00000435289; ENSG00000168092.
DR Ensembl; ENST00000529887; ENSP00000434951; ENSG00000168092.
DR Ensembl; ENST00000530272; ENSP00000431365; ENSG00000168092.
DR GeneID; 5049; -.
DR KEGG; hsa:5049; -.
DR UCSC; uc009yzl.2; human.
DR CTD; 5049; -.
DR GeneCards; GC11P117014; -.
DR H-InvDB; HIX0022939; -.
DR HGNC; HGNC:8575; PAFAH1B2.
DR HPA; HPA051836; -.
DR MIM; 602508; gene.
DR neXtProt; NX_P68402; -.
DR PharmGKB; PA32906; -.
DR eggNOG; NOG69837; -.
DR HOGENOM; HOG000232143; -.
DR HOVERGEN; HBG053477; -.
DR InParanoid; P68402; -.
DR KO; K16795; -.
DR OMA; NIRPKVV; -.
DR OrthoDB; EOG7HB5BS; -.
DR PhylomeDB; P68402; -.
DR ChiTaRS; PAFAH1B2; human.
DR EvolutionaryTrace; P68402; -.
DR GeneWiki; PAFAH1B2; -.
DR GenomeRNAi; 5049; -.
DR NextBio; 19456; -.
DR PRO; PR:P68402; -.
DR ArrayExpress; P68402; -.
DR Bgee; P68402; -.
DR CleanEx; HS_PAFAH1B2; -.
DR Genevestigator; P68402; -.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR013831; SGNH_hydro-type_esterase_dom.
DR PROSITE; PS01098; LIPASE_GDSL_SER; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Lipid degradation;
KW Lipid metabolism; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 229 Platelet-activating factor
FT acetylhydrolase IB subunit beta.
FT /FTId=PRO_0000058151.
FT ACT_SITE 48 48 By similarity.
FT ACT_SITE 193 193 By similarity.
FT ACT_SITE 196 196 By similarity.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT VAR_SEQ 133 229 Missing (in isoform 3).
FT /FTId=VSP_043217.
FT VAR_SEQ 138 229 GLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGG
FT FVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEE
FT TPEEKQTTIA -> IIYWQDEQDYHERKVQMD (in
FT isoform 2).
FT /FTId=VSP_042896.
FT VAR_SEQ 139 229 LLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGF
FT VHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEET
FT PEEKQTTIA -> KAAASKYSISEIVRLEQGSVNWSIGTYP
FT DDTPATTRPAILQLFTGKMSRITMKEKSRWTEEILH (in
FT isoform 4).
FT /FTId=VSP_044680.
FT HELIX 8 10
FT STRAND 19 21
FT HELIX 23 37
FT STRAND 41 47
FT HELIX 48 53
FT HELIX 57 62
FT HELIX 64 66
FT STRAND 68 72
FT HELIX 78 86
FT TURN 87 90
FT STRAND 96 101
FT HELIX 111 128
FT STRAND 133 137
FT STRAND 143 145
FT HELIX 148 163
FT STRAND 164 167
FT STRAND 170 173
FT TURN 188 190
FT STRAND 194 197
FT HELIX 199 219
SQ SEQUENCE 229 AA; 25569 MW; 14CF5D48621AA504 CRC64;
MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR
ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA
IVQLINTRQP QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDTDGGFV
HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTTIA
//
ID PA1B2_HUMAN Reviewed; 229 AA.
AC P68402; A8DPS5; A8DPS6; A8DPS7; E9PEJ5; E9PLP3; O00687; Q29459;
read moreAC Q6IBR6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit beta;
DE EC=3.1.1.47;
DE AltName: Full=PAF acetylhydrolase 30 kDa subunit;
DE Short=PAF-AH 30 kDa subunit;
DE AltName: Full=PAF-AH subunit beta;
DE Short=PAFAH subunit beta;
GN Name=PAFAH1B2; Synonyms=PAFAHB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal liver;
RX PubMed=9144386; DOI=10.1006/bbrc.1997.6383;
RA Adachi H., Tsujimoto M., Hattori M., Arai H., Inoue K.;
RT "Differential tissue distribution of the beta- and gamma-subunits of
RT human cytosolic platelet-activating factor acetylhydrolase (isoform
RT I).";
RL Biochem. Biophys. Res. Commun. 233:10-13(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Testis;
RX PubMed=18155631; DOI=10.1016/j.prostaglandins.2007.10.005;
RA Scott B.T., Olson N., Long G.L., Bovill E.G.;
RT "Novel isoforms of intracellular platelet activating factor
RT acetylhydrolase (PAFAH1b2) in human testis; encoded by alternatively
RT spliced mRNAs.";
RL Prostaglandins Other Lipid Mediat. 85:69-80(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G;);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 61-79, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Inactivates PAF by removing the acetyl group at the sn-2
CC position. This is a catalytic subunit.
CC -!- CATALYTIC ACTIVITY: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine +
CC H(2)O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.
CC -!- SUBUNIT: Cytosolic PAF-AH IB is formed of three subunits of 45 kDa
CC (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity
CC of the enzyme resides in the beta and gamma subunits, whereas the
CC alpha subunit has regulatory activity. Trimer formation is not
CC essential for the catalytic activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P68402-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P68402-2; Sequence=VSP_042896;
CC Name=3;
CC IsoId=P68402-3; Sequence=VSP_043217;
CC Name=4;
CC IsoId=P68402-4; Sequence=VSP_044680;
CC Note=Ref.2 (ABI58227/ABI58228) sequences are in conflict in
CC position: 151:V->M;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC Platelet-activating factor acetylhydrolase IB beta/gamma subunits
CC subfamily.
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DR EMBL; D63390; BAA19917.1; -; mRNA.
DR EMBL; DQ836738; ABI58225.1; -; mRNA.
DR EMBL; DQ836739; ABI58226.1; -; mRNA.
DR EMBL; DQ836740; ABI58227.1; -; mRNA.
DR EMBL; DQ836741; ABI58228.1; -; mRNA.
DR EMBL; DQ836742; ABI58229.1; -; mRNA.
DR EMBL; DQ836743; ABI58230.1; -; mRNA.
DR EMBL; AK292973; BAF85662.1; -; mRNA.
DR EMBL; CR456736; CAG33017.1; -; mRNA.
DR EMBL; EF445007; ACA06040.1; -; Genomic_DNA.
DR EMBL; AP005018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67281.1; -; Genomic_DNA.
DR EMBL; BC000398; AAH00398.1; -; mRNA.
DR EMBL; BC019301; AAH19301.1; -; mRNA.
DR PIR; JC5409; JC5409.
DR RefSeq; NP_001171675.1; NM_001184746.1.
DR RefSeq; NP_001171676.1; NM_001184747.1.
DR RefSeq; NP_001171677.1; NM_001184748.1.
DR RefSeq; NP_002563.1; NM_002572.3.
DR UniGene; Hs.728488; -.
DR PDB; 1VYH; X-ray; 3.40 A; A/B/E/F/I/J/M/N/Q/R=1-229.
DR PDBsum; 1VYH; -.
DR ProteinModelPortal; P68402; -.
DR SMR; P68402; 6-217.
DR IntAct; P68402; 15.
DR MINT; MINT-5002700; -.
DR STRING; 9606.ENSP00000304006; -.
DR ChEMBL; CHEMBL4463; -.
DR PhosphoSite; P68402; -.
DR DMDM; 55977294; -.
DR REPRODUCTION-2DPAGE; IPI00026546; -.
DR PaxDb; P68402; -.
DR PeptideAtlas; P68402; -.
DR PRIDE; P68402; -.
DR Ensembl; ENST00000419197; ENSP00000388742; ENSG00000168092.
DR Ensembl; ENST00000527958; ENSP00000435289; ENSG00000168092.
DR Ensembl; ENST00000529887; ENSP00000434951; ENSG00000168092.
DR Ensembl; ENST00000530272; ENSP00000431365; ENSG00000168092.
DR GeneID; 5049; -.
DR KEGG; hsa:5049; -.
DR UCSC; uc009yzl.2; human.
DR CTD; 5049; -.
DR GeneCards; GC11P117014; -.
DR H-InvDB; HIX0022939; -.
DR HGNC; HGNC:8575; PAFAH1B2.
DR HPA; HPA051836; -.
DR MIM; 602508; gene.
DR neXtProt; NX_P68402; -.
DR PharmGKB; PA32906; -.
DR eggNOG; NOG69837; -.
DR HOGENOM; HOG000232143; -.
DR HOVERGEN; HBG053477; -.
DR InParanoid; P68402; -.
DR KO; K16795; -.
DR OMA; NIRPKVV; -.
DR OrthoDB; EOG7HB5BS; -.
DR PhylomeDB; P68402; -.
DR ChiTaRS; PAFAH1B2; human.
DR EvolutionaryTrace; P68402; -.
DR GeneWiki; PAFAH1B2; -.
DR GenomeRNAi; 5049; -.
DR NextBio; 19456; -.
DR PRO; PR:P68402; -.
DR ArrayExpress; P68402; -.
DR Bgee; P68402; -.
DR CleanEx; HS_PAFAH1B2; -.
DR Genevestigator; P68402; -.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR013831; SGNH_hydro-type_esterase_dom.
DR PROSITE; PS01098; LIPASE_GDSL_SER; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Lipid degradation;
KW Lipid metabolism; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 229 Platelet-activating factor
FT acetylhydrolase IB subunit beta.
FT /FTId=PRO_0000058151.
FT ACT_SITE 48 48 By similarity.
FT ACT_SITE 193 193 By similarity.
FT ACT_SITE 196 196 By similarity.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT VAR_SEQ 133 229 Missing (in isoform 3).
FT /FTId=VSP_043217.
FT VAR_SEQ 138 229 GLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGG
FT FVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEE
FT TPEEKQTTIA -> IIYWQDEQDYHERKVQMD (in
FT isoform 2).
FT /FTId=VSP_042896.
FT VAR_SEQ 139 229 LLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGF
FT VHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEET
FT PEEKQTTIA -> KAAASKYSISEIVRLEQGSVNWSIGTYP
FT DDTPATTRPAILQLFTGKMSRITMKEKSRWTEEILH (in
FT isoform 4).
FT /FTId=VSP_044680.
FT HELIX 8 10
FT STRAND 19 21
FT HELIX 23 37
FT STRAND 41 47
FT HELIX 48 53
FT HELIX 57 62
FT HELIX 64 66
FT STRAND 68 72
FT HELIX 78 86
FT TURN 87 90
FT STRAND 96 101
FT HELIX 111 128
FT STRAND 133 137
FT STRAND 143 145
FT HELIX 148 163
FT STRAND 164 167
FT STRAND 170 173
FT TURN 188 190
FT STRAND 194 197
FT HELIX 199 219
SQ SEQUENCE 229 AA; 25569 MW; 14CF5D48621AA504 CRC64;
MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR
ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA
IVQLINTRQP QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDTDGGFV
HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTTIA
//
MIM
602508
*RECORD*
*FIELD* NO
602508
*FIELD* TI
*602508 PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE, ISOFORM 1B, BETA SUBUNIT;
PAFAH1B2
read more*FIELD* TX
DESCRIPTION
Platelet-activating factor (PAF) is a biologically active phospholipid
with diverse biologic effects. PAF is degraded to inactive products by
hydrolysis of the acetyl group at the sn-2 position to produce the
biologically inactive products LYSO-PAF and acetate. This reaction is
catalyzed by PAF acetylhydrolase (PAFAH). The various monomeric and
multimeric forms of the enzyme are composed of alpha (601545), beta, and
gamma (603074) PAFAH subunits.
CLONING
By screening a human fetal liver library with 2
oligodeoxyribonucleotides derived from the cDNA sequence of the bovine
PAFAH beta subunit, Adachi et al. (1997) cloned the cDNA encoding the
human PAFAH beta subunit. The PAFAH1B2 gene encodes a 229-amino acid
polypeptide with a molecular mass of 30 kD. The human PAFAH1B2 amino
acid sequence is 62.4% identical to that of the human gamma subunit.
Northern blot analysis revealed that the gene was expressed as a 4.0-kb
mRNA in all human adult and fetal tissues tested.
MAPPING
By radiation hybrid mapping, screening of a YAC library, and
fluorescence in situ hybridization, Moro et al. (1998) localized the
PAFAH1B2 gene to 11q23.
GENE FUNCTION
By analysis of crystalline structures of mouse proteins, Tarricone et
al. (2004) determined that a Lis1 (601545) homodimer binds with a
homodimer of either Pafah1b2 or Ndel1 (607538) to form a tetramer. Ndel1
competes with the Pafah1b2 homodimer for Lis1, but the interaction is
complex and requires both the N- and C-terminal domains of Lis1. The
data suggested that the Lis1 molecule undergoes major conformational
changes when switching from a complex with the acetylhydrolase to that
with Ndel1.
By studying human erythrocytes, Zhou et al. (2011) determined that
aspirin (acetylsalicylic acid) is hydrolyzed and rendered biologically
inactive by type I PAF, and that the reaction occurs intracellularly
within erythrocytes. Overexpression of the catalytic PAFAH1B2 or
PAFAH1B3 (603074) subunits in HEK293 cells showed that each could
hydrolyze aspirin. Inhibition of recombinant PAFAH1B2 reduced aspirin
hydrolysis. In contrast, plasma PAF (PLA2G7; 601690) was devoid of
aspirin hydrolase activity. Exposing platelets to aspirin and
erythrocytes decreased the ability of aspirin to inhibit thromboxane A2
synthesis and platelet aggregation, and aspirin preincubated with
erythrocytes was almost completely ineffective as a platelet inhibitor.
Analysis of 10 different healthy blood donors revealed that aspirin
hydrolysis varied more than 2-fold, and this variation corresponded to
the erythrocyte protein content of PAFAH1B2, as determined by
immunoblot, but did not correspond to levels of PAFAH1B3. Zhou et al.
(2011) concluded that intracellular type I PAF acetylhydrolase is the
major aspirin hydrolase in human blood (erythrocytes), and that
variation in this hydrolase activity may underlie the variation in
therapeutic response among humans (see 608233).
*FIELD* RF
1. Adachi, H.; Tsujimoto, M.; Hattori, M.; Arai, H.; Inoue, K.: Differential
tissue distribution of the beta- and gamma-subunits of human cytosolic
platelet-activating factor acetylhydrolase (isoform 1). Biochem.
Biophys. Res. Commun. 233: 10-13, 1997.
2. Moro, F.; Arrigo, G.; Fogli, A.; Bernard, L.; Carrozzo, R.: The
beta and gamma subunits of the human platelet-activating factor acetyl
hydrolase isoform Ib (PAFAH1B2 and PAFAH1B3) map to chromosome 11q23
and 19q13.1, respectively. Genomics 51: 157-159, 1998.
3. Tarricone, C.; Perrina, F.; Monzani, S.; Massimiliano, L.; Kim,
M.-H.; Derewenda, Z. S.; Knapp, S.; Tsai, L.-H.; Musacchio, A.: Coupling
PAF signaling to dynein regulation: structure of LIS1 in complex with
PAF-acetylhydrolase. Neuron 44: 809-821, 2004.
4. Zhou, G.; Marathe, G. K.; Willard, B.; McIntyre, T. M.: Intracellular
erythrocyte platelet-activating factor acetylhydrolase I inactivates
aspirin in blood. J. Biol. Chem. 286: 34820-34829, 2011.
*FIELD* CN
Cassandra L. Kniffin - updated: 10/5/2011
Cassandra L. Kniffin - updated: 4/5/2005
Patti M. Sherman - updated: 10/1/1998
*FIELD* CD
Jennifer P. Macke: 4/10/1998
*FIELD* ED
carol: 10/06/2011
ckniffin: 10/5/2011
alopez: 2/4/2009
wwang: 4/19/2005
ckniffin: 4/5/2005
psherman: 10/1/1998
alopez: 7/29/1998
alopez: 7/27/1998
dholmes: 4/16/1998
*RECORD*
*FIELD* NO
602508
*FIELD* TI
*602508 PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE, ISOFORM 1B, BETA SUBUNIT;
PAFAH1B2
read more*FIELD* TX
DESCRIPTION
Platelet-activating factor (PAF) is a biologically active phospholipid
with diverse biologic effects. PAF is degraded to inactive products by
hydrolysis of the acetyl group at the sn-2 position to produce the
biologically inactive products LYSO-PAF and acetate. This reaction is
catalyzed by PAF acetylhydrolase (PAFAH). The various monomeric and
multimeric forms of the enzyme are composed of alpha (601545), beta, and
gamma (603074) PAFAH subunits.
CLONING
By screening a human fetal liver library with 2
oligodeoxyribonucleotides derived from the cDNA sequence of the bovine
PAFAH beta subunit, Adachi et al. (1997) cloned the cDNA encoding the
human PAFAH beta subunit. The PAFAH1B2 gene encodes a 229-amino acid
polypeptide with a molecular mass of 30 kD. The human PAFAH1B2 amino
acid sequence is 62.4% identical to that of the human gamma subunit.
Northern blot analysis revealed that the gene was expressed as a 4.0-kb
mRNA in all human adult and fetal tissues tested.
MAPPING
By radiation hybrid mapping, screening of a YAC library, and
fluorescence in situ hybridization, Moro et al. (1998) localized the
PAFAH1B2 gene to 11q23.
GENE FUNCTION
By analysis of crystalline structures of mouse proteins, Tarricone et
al. (2004) determined that a Lis1 (601545) homodimer binds with a
homodimer of either Pafah1b2 or Ndel1 (607538) to form a tetramer. Ndel1
competes with the Pafah1b2 homodimer for Lis1, but the interaction is
complex and requires both the N- and C-terminal domains of Lis1. The
data suggested that the Lis1 molecule undergoes major conformational
changes when switching from a complex with the acetylhydrolase to that
with Ndel1.
By studying human erythrocytes, Zhou et al. (2011) determined that
aspirin (acetylsalicylic acid) is hydrolyzed and rendered biologically
inactive by type I PAF, and that the reaction occurs intracellularly
within erythrocytes. Overexpression of the catalytic PAFAH1B2 or
PAFAH1B3 (603074) subunits in HEK293 cells showed that each could
hydrolyze aspirin. Inhibition of recombinant PAFAH1B2 reduced aspirin
hydrolysis. In contrast, plasma PAF (PLA2G7; 601690) was devoid of
aspirin hydrolase activity. Exposing platelets to aspirin and
erythrocytes decreased the ability of aspirin to inhibit thromboxane A2
synthesis and platelet aggregation, and aspirin preincubated with
erythrocytes was almost completely ineffective as a platelet inhibitor.
Analysis of 10 different healthy blood donors revealed that aspirin
hydrolysis varied more than 2-fold, and this variation corresponded to
the erythrocyte protein content of PAFAH1B2, as determined by
immunoblot, but did not correspond to levels of PAFAH1B3. Zhou et al.
(2011) concluded that intracellular type I PAF acetylhydrolase is the
major aspirin hydrolase in human blood (erythrocytes), and that
variation in this hydrolase activity may underlie the variation in
therapeutic response among humans (see 608233).
*FIELD* RF
1. Adachi, H.; Tsujimoto, M.; Hattori, M.; Arai, H.; Inoue, K.: Differential
tissue distribution of the beta- and gamma-subunits of human cytosolic
platelet-activating factor acetylhydrolase (isoform 1). Biochem.
Biophys. Res. Commun. 233: 10-13, 1997.
2. Moro, F.; Arrigo, G.; Fogli, A.; Bernard, L.; Carrozzo, R.: The
beta and gamma subunits of the human platelet-activating factor acetyl
hydrolase isoform Ib (PAFAH1B2 and PAFAH1B3) map to chromosome 11q23
and 19q13.1, respectively. Genomics 51: 157-159, 1998.
3. Tarricone, C.; Perrina, F.; Monzani, S.; Massimiliano, L.; Kim,
M.-H.; Derewenda, Z. S.; Knapp, S.; Tsai, L.-H.; Musacchio, A.: Coupling
PAF signaling to dynein regulation: structure of LIS1 in complex with
PAF-acetylhydrolase. Neuron 44: 809-821, 2004.
4. Zhou, G.; Marathe, G. K.; Willard, B.; McIntyre, T. M.: Intracellular
erythrocyte platelet-activating factor acetylhydrolase I inactivates
aspirin in blood. J. Biol. Chem. 286: 34820-34829, 2011.
*FIELD* CN
Cassandra L. Kniffin - updated: 10/5/2011
Cassandra L. Kniffin - updated: 4/5/2005
Patti M. Sherman - updated: 10/1/1998
*FIELD* CD
Jennifer P. Macke: 4/10/1998
*FIELD* ED
carol: 10/06/2011
ckniffin: 10/5/2011
alopez: 2/4/2009
wwang: 4/19/2005
ckniffin: 4/5/2005
psherman: 10/1/1998
alopez: 7/29/1998
alopez: 7/27/1998
dholmes: 4/16/1998