Full text data of PAFAH1B3
PAFAH1B3
(PAFAHG)
[Confidence: low (only semi-automatic identification from reviews)]
Platelet-activating factor acetylhydrolase IB subunit gamma; 3.1.1.47 (PAF acetylhydrolase 29 kDa subunit; PAF-AH 29 kDa subunit; PAF-AH subunit gamma; PAFAH subunit gamma)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Platelet-activating factor acetylhydrolase IB subunit gamma; 3.1.1.47 (PAF acetylhydrolase 29 kDa subunit; PAF-AH 29 kDa subunit; PAF-AH subunit gamma; PAFAH subunit gamma)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15102
ID PA1B3_HUMAN Reviewed; 231 AA.
AC Q15102; Q53X88;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit gamma;
DE EC=3.1.1.47;
DE AltName: Full=PAF acetylhydrolase 29 kDa subunit;
DE Short=PAF-AH 29 kDa subunit;
DE AltName: Full=PAF-AH subunit gamma;
DE Short=PAFAH subunit gamma;
GN Name=PAFAH1B3; Synonyms=PAFAHG;
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].
RC TISSUE=Fetal liver;
RX PubMed=7669037; DOI=10.1006/bbrc.1995.2272;
RA Adachi H., Tsujimoto M., Hattori M., Arai H., Inoue K.;
RT "cDNA cloning of human cytosolic platelet-activating factor
RT acetylhydrolase gamma-subunit and its mRNA expression in human
RT tissues.";
RL Biochem. Biophys. Res. Commun. 214:180-187(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Uterus;
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 [6]
RP PROTEIN SEQUENCE OF 84-127; 133-141 AND 199-231, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
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 [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Inactivates paf by removing the acetyl group at the sn-2
CC position. This is a catalytic subunit. Plays an important role
CC during the development of brain.
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 -!- INTERACTION:
CC Q8TBB1:LNX1; NbExp=2; IntAct=EBI-711522, EBI-739832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: In the adult, expressed in brain, skeletal
CC muscle, kidney, thymus, spleen, colon, testis, ovary and
CC peripheral blood leukocytes. In the fetus, highest expression
CC occurs in brain.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC Platelet-activating factor acetylhydrolase IB beta/gamma subunits
CC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D63391; BAA09706.1; -; mRNA.
DR EMBL; CR407626; CAG28554.1; -; mRNA.
DR EMBL; AC006486; AAD11989.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57122.1; -; Genomic_DNA.
DR EMBL; BC003016; AAH03016.1; -; mRNA.
DR EMBL; BC007863; AAH07863.1; -; mRNA.
DR PIR; JC4246; JC4246.
DR RefSeq; NP_001139411.1; NM_001145939.1.
DR RefSeq; NP_001139412.1; NM_001145940.1.
DR RefSeq; NP_002564.1; NM_002573.3.
DR UniGene; Hs.466831; -.
DR ProteinModelPortal; Q15102; -.
DR SMR; Q15102; 5-207.
DR IntAct; Q15102; 32.
DR MINT; MINT-1368260; -.
DR STRING; 9606.ENSP00000262890; -.
DR ChEMBL; CHEMBL5108; -.
DR PhosphoSite; Q15102; -.
DR DMDM; 3024344; -.
DR REPRODUCTION-2DPAGE; IPI00014808; -.
DR PaxDb; Q15102; -.
DR PeptideAtlas; Q15102; -.
DR PRIDE; Q15102; -.
DR Ensembl; ENST00000262890; ENSP00000262890; ENSG00000079462.
DR Ensembl; ENST00000538771; ENSP00000444935; ENSG00000079462.
DR GeneID; 5050; -.
DR KEGG; hsa:5050; -.
DR UCSC; uc002otg.2; human.
DR CTD; 5050; -.
DR GeneCards; GC19M042801; -.
DR HGNC; HGNC:8576; PAFAH1B3.
DR HPA; HPA035639; -.
DR MIM; 603074; gene.
DR neXtProt; NX_Q15102; -.
DR PharmGKB; PA32907; -.
DR eggNOG; NOG69837; -.
DR HOGENOM; HOG000232143; -.
DR HOVERGEN; HBG053477; -.
DR InParanoid; Q15102; -.
DR KO; K16795; -.
DR OMA; FAPLHCL; -.
DR OrthoDB; EOG7HB5BS; -.
DR PhylomeDB; Q15102; -.
DR GeneWiki; PAFAH1B3; -.
DR GenomeRNAi; 5050; -.
DR NextBio; 19460; -.
DR PRO; PR:Q15102; -.
DR ArrayExpress; Q15102; -.
DR Bgee; Q15102; -.
DR CleanEx; HS_PAFAH1B3; -.
DR Genevestigator; Q15102; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0007399; P:nervous system development; TAS:ProtInc.
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 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Lipid degradation; Lipid metabolism; Polymorphism;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 231 Platelet-activating factor
FT acetylhydrolase IB subunit gamma.
FT /FTId=PRO_0000058155.
FT ACT_SITE 47 47 By similarity.
FT ACT_SITE 192 192 By similarity.
FT ACT_SITE 195 195 By similarity.
FT MOD_RES 2 2 N-acetylserine.
FT VARIANT 214 214 R -> G (in dbSNP:rs1043818).
FT /FTId=VAR_051261.
SQ SEQUENCE 231 AA; 25734 MW; 58A4CB8E7076AE23 CRC64;
MSGEENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ LMHQCEIWRE
LFSPLHALNF GIGGDGTQHV LWRLENGELE HIRPKIVVVW VGTNNHGHTA EQVTGGIKAI
VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE KNRQVNELVR AALAGHPRAH FLDADPGFVH
SDGTISHHDM YDYLHLSRLG YTPVCRALHS LLLRLLAQDQ GQGAPLLEPA P
//
ID PA1B3_HUMAN Reviewed; 231 AA.
AC Q15102; Q53X88;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit gamma;
DE EC=3.1.1.47;
DE AltName: Full=PAF acetylhydrolase 29 kDa subunit;
DE Short=PAF-AH 29 kDa subunit;
DE AltName: Full=PAF-AH subunit gamma;
DE Short=PAFAH subunit gamma;
GN Name=PAFAH1B3; Synonyms=PAFAHG;
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].
RC TISSUE=Fetal liver;
RX PubMed=7669037; DOI=10.1006/bbrc.1995.2272;
RA Adachi H., Tsujimoto M., Hattori M., Arai H., Inoue K.;
RT "cDNA cloning of human cytosolic platelet-activating factor
RT acetylhydrolase gamma-subunit and its mRNA expression in human
RT tissues.";
RL Biochem. Biophys. Res. Commun. 214:180-187(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Uterus;
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 [6]
RP PROTEIN SEQUENCE OF 84-127; 133-141 AND 199-231, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
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 [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Inactivates paf by removing the acetyl group at the sn-2
CC position. This is a catalytic subunit. Plays an important role
CC during the development of brain.
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 -!- INTERACTION:
CC Q8TBB1:LNX1; NbExp=2; IntAct=EBI-711522, EBI-739832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: In the adult, expressed in brain, skeletal
CC muscle, kidney, thymus, spleen, colon, testis, ovary and
CC peripheral blood leukocytes. In the fetus, highest expression
CC occurs in brain.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC Platelet-activating factor acetylhydrolase IB beta/gamma subunits
CC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D63391; BAA09706.1; -; mRNA.
DR EMBL; CR407626; CAG28554.1; -; mRNA.
DR EMBL; AC006486; AAD11989.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57122.1; -; Genomic_DNA.
DR EMBL; BC003016; AAH03016.1; -; mRNA.
DR EMBL; BC007863; AAH07863.1; -; mRNA.
DR PIR; JC4246; JC4246.
DR RefSeq; NP_001139411.1; NM_001145939.1.
DR RefSeq; NP_001139412.1; NM_001145940.1.
DR RefSeq; NP_002564.1; NM_002573.3.
DR UniGene; Hs.466831; -.
DR ProteinModelPortal; Q15102; -.
DR SMR; Q15102; 5-207.
DR IntAct; Q15102; 32.
DR MINT; MINT-1368260; -.
DR STRING; 9606.ENSP00000262890; -.
DR ChEMBL; CHEMBL5108; -.
DR PhosphoSite; Q15102; -.
DR DMDM; 3024344; -.
DR REPRODUCTION-2DPAGE; IPI00014808; -.
DR PaxDb; Q15102; -.
DR PeptideAtlas; Q15102; -.
DR PRIDE; Q15102; -.
DR Ensembl; ENST00000262890; ENSP00000262890; ENSG00000079462.
DR Ensembl; ENST00000538771; ENSP00000444935; ENSG00000079462.
DR GeneID; 5050; -.
DR KEGG; hsa:5050; -.
DR UCSC; uc002otg.2; human.
DR CTD; 5050; -.
DR GeneCards; GC19M042801; -.
DR HGNC; HGNC:8576; PAFAH1B3.
DR HPA; HPA035639; -.
DR MIM; 603074; gene.
DR neXtProt; NX_Q15102; -.
DR PharmGKB; PA32907; -.
DR eggNOG; NOG69837; -.
DR HOGENOM; HOG000232143; -.
DR HOVERGEN; HBG053477; -.
DR InParanoid; Q15102; -.
DR KO; K16795; -.
DR OMA; FAPLHCL; -.
DR OrthoDB; EOG7HB5BS; -.
DR PhylomeDB; Q15102; -.
DR GeneWiki; PAFAH1B3; -.
DR GenomeRNAi; 5050; -.
DR NextBio; 19460; -.
DR PRO; PR:Q15102; -.
DR ArrayExpress; Q15102; -.
DR Bgee; Q15102; -.
DR CleanEx; HS_PAFAH1B3; -.
DR Genevestigator; Q15102; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0007399; P:nervous system development; TAS:ProtInc.
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 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Lipid degradation; Lipid metabolism; Polymorphism;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 231 Platelet-activating factor
FT acetylhydrolase IB subunit gamma.
FT /FTId=PRO_0000058155.
FT ACT_SITE 47 47 By similarity.
FT ACT_SITE 192 192 By similarity.
FT ACT_SITE 195 195 By similarity.
FT MOD_RES 2 2 N-acetylserine.
FT VARIANT 214 214 R -> G (in dbSNP:rs1043818).
FT /FTId=VAR_051261.
SQ SEQUENCE 231 AA; 25734 MW; 58A4CB8E7076AE23 CRC64;
MSGEENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ LMHQCEIWRE
LFSPLHALNF GIGGDGTQHV LWRLENGELE HIRPKIVVVW VGTNNHGHTA EQVTGGIKAI
VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE KNRQVNELVR AALAGHPRAH FLDADPGFVH
SDGTISHHDM YDYLHLSRLG YTPVCRALHS LLLRLLAQDQ GQGAPLLEPA P
//
MIM
603074
*RECORD*
*FIELD* NO
603074
*FIELD* TI
*603074 PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE, ISOFORM 1B, GAMMA SUBUNIT;
PAFAH1B3
read more*FIELD* TX
DESCRIPTION
Platelet-activating factor acetylhydrolase (PAFAH) catalyzes the removal
of the acetyl group at the sn-2 position of the glycerol backbone of
platelet-activating factor (PAF), producing biologically inactive
lyso-PAF. Isoform 1B of PAFAH consists of 3 subunits: alpha (PAFAH1B1;
601545), beta (PAFAH1B2; 602508), and gamma. The catalytic activity of
the enzyme resides in the beta and gamma subunits, whereas the alpha
subunit has regulatory activity (summary by Adachi et al., 1995).
CLONING
By screening a human fetal liver cDNA library with oligonucleotides
based on the cDNA sequence of the bovine PAFAH-gamma subunit, Adachi et
al. (1995) cloned a cDNA encoding PAFAH1B3. The deduced 231-amino acid
human protein has 97.8% identity with the bovine PAFAH-gamma subunit.
Southern blot analysis showed that PAFAH1B3 is a single-copy gene in the
human genome. Northern blot analysis detected a 1.0-kb PAFAH1B3
transcript in several human adult and fetal tissues, with the highest
expression in fetal brain. Adachi et al. (1995) expressed the PAFAH1B3
cDNA in E. coli and found that the resulting protein was catalytically
active, demonstrating that trimer formation is not essential for
PAFAH1B3 activity.
GENE STRUCTURE
Adachi et al. (1995) determined that the PAFAH1B3 gene spans
approximately 5.6 kb and contains 5 exons.
MAPPING
By radiation hybrid mapping and fluorescence in situ hybridization, Moro
et al. (1998) localized the PAFAH1B3 gene to chromosome 19q13.1.
GENE FUNCTION
Zhou et al. (2011) determined that aspirin (acetylsalicylic acid) is
hydrolyzed and rendered biologically inactive by type I
platelet-activating factor, and that the reaction occurs intracellularly
within erythrocytes. Hydrolase activity could be mediated by either of
the 2 catalytic subunits, PAFAH1B2 (602508) or PAFAH1B3, but not by
plasma PAF (PLA2G7; 601690). In vitro studies showed that 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.
CYTOGENETICS
Nothwang et al. (2001) reported a translocation t(1;19)(q21.3;q13.2) in
a female with mental retardation, ataxia, and atrophy of the brain.
Sequence analysis of the breakpoints revealed an Alu repeat-mediated
mechanism of recombination that led to truncation of PAFAH1B3 and the
kinase CLK2 (602989). One expressed fusion gene encoded the first 136
amino acids of PAFAH1B3, followed by the complete CLK2 protein.
Truncated PAFAH1B3 protein lost its potential to interact with LIS1
(601545), whereas CLK2 activity was conserved within the fusion protein.
These data emphasized the importance of PAFAH1B in brain development and
function.
*FIELD* RF
1. Adachi, H.; Tsujimoto, M.; Hattori, M.; Arai, H.; Inoue, K.: cDNA
cloning of human cytosolic platelet-activating factor acetylhydrolase
gamma-subunit and its mRNA expression in human tissues. Biochem.
Biophys. Res. Commun. 214: 180-187, 1995.
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. Nothwang, H. G.; Kim, H. G.; Aoki, J.; Geisterfer, M.; Kubart,
S.; Wegner, R. D.; van Moers, A.; Ashworth, L. K.; Haaf, T.; Bell,
J.; Arai, H.; Tommerup, N.; Ropers, H. H.; Wirth, J.: Functional
hemizygosity of PAFAH1B3 due to a PAFAH1B3-CLK2 fusion gene in a female
with mental retardation, ataxia and atrophy of the brain. Hum. Molec.
Genet. 10: 797-806, 2001.
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
George E. Tiller - updated: 7/20/2001
*FIELD* CD
Sheryl A. Jankowski: 9/29/1998
*FIELD* ED
carol: 10/06/2011
ckniffin: 10/5/2011
wwang: 2/17/2011
cwells: 7/27/2001
cwells: 7/20/2001
psherman: 10/1/1998
*RECORD*
*FIELD* NO
603074
*FIELD* TI
*603074 PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE, ISOFORM 1B, GAMMA SUBUNIT;
PAFAH1B3
read more*FIELD* TX
DESCRIPTION
Platelet-activating factor acetylhydrolase (PAFAH) catalyzes the removal
of the acetyl group at the sn-2 position of the glycerol backbone of
platelet-activating factor (PAF), producing biologically inactive
lyso-PAF. Isoform 1B of PAFAH consists of 3 subunits: alpha (PAFAH1B1;
601545), beta (PAFAH1B2; 602508), and gamma. The catalytic activity of
the enzyme resides in the beta and gamma subunits, whereas the alpha
subunit has regulatory activity (summary by Adachi et al., 1995).
CLONING
By screening a human fetal liver cDNA library with oligonucleotides
based on the cDNA sequence of the bovine PAFAH-gamma subunit, Adachi et
al. (1995) cloned a cDNA encoding PAFAH1B3. The deduced 231-amino acid
human protein has 97.8% identity with the bovine PAFAH-gamma subunit.
Southern blot analysis showed that PAFAH1B3 is a single-copy gene in the
human genome. Northern blot analysis detected a 1.0-kb PAFAH1B3
transcript in several human adult and fetal tissues, with the highest
expression in fetal brain. Adachi et al. (1995) expressed the PAFAH1B3
cDNA in E. coli and found that the resulting protein was catalytically
active, demonstrating that trimer formation is not essential for
PAFAH1B3 activity.
GENE STRUCTURE
Adachi et al. (1995) determined that the PAFAH1B3 gene spans
approximately 5.6 kb and contains 5 exons.
MAPPING
By radiation hybrid mapping and fluorescence in situ hybridization, Moro
et al. (1998) localized the PAFAH1B3 gene to chromosome 19q13.1.
GENE FUNCTION
Zhou et al. (2011) determined that aspirin (acetylsalicylic acid) is
hydrolyzed and rendered biologically inactive by type I
platelet-activating factor, and that the reaction occurs intracellularly
within erythrocytes. Hydrolase activity could be mediated by either of
the 2 catalytic subunits, PAFAH1B2 (602508) or PAFAH1B3, but not by
plasma PAF (PLA2G7; 601690). In vitro studies showed that 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.
CYTOGENETICS
Nothwang et al. (2001) reported a translocation t(1;19)(q21.3;q13.2) in
a female with mental retardation, ataxia, and atrophy of the brain.
Sequence analysis of the breakpoints revealed an Alu repeat-mediated
mechanism of recombination that led to truncation of PAFAH1B3 and the
kinase CLK2 (602989). One expressed fusion gene encoded the first 136
amino acids of PAFAH1B3, followed by the complete CLK2 protein.
Truncated PAFAH1B3 protein lost its potential to interact with LIS1
(601545), whereas CLK2 activity was conserved within the fusion protein.
These data emphasized the importance of PAFAH1B in brain development and
function.
*FIELD* RF
1. Adachi, H.; Tsujimoto, M.; Hattori, M.; Arai, H.; Inoue, K.: cDNA
cloning of human cytosolic platelet-activating factor acetylhydrolase
gamma-subunit and its mRNA expression in human tissues. Biochem.
Biophys. Res. Commun. 214: 180-187, 1995.
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. Nothwang, H. G.; Kim, H. G.; Aoki, J.; Geisterfer, M.; Kubart,
S.; Wegner, R. D.; van Moers, A.; Ashworth, L. K.; Haaf, T.; Bell,
J.; Arai, H.; Tommerup, N.; Ropers, H. H.; Wirth, J.: Functional
hemizygosity of PAFAH1B3 due to a PAFAH1B3-CLK2 fusion gene in a female
with mental retardation, ataxia and atrophy of the brain. Hum. Molec.
Genet. 10: 797-806, 2001.
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
George E. Tiller - updated: 7/20/2001
*FIELD* CD
Sheryl A. Jankowski: 9/29/1998
*FIELD* ED
carol: 10/06/2011
ckniffin: 10/5/2011
wwang: 2/17/2011
cwells: 7/27/2001
cwells: 7/20/2001
psherman: 10/1/1998