PA1B3_MOUSE
ID PA1B3_MOUSE Reviewed; 232 AA.
AC Q61205;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha1 {ECO:0000305};
DE EC=3.1.1.47 {ECO:0000250|UniProtKB:Q29460};
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 {ECO:0000312|EMBL:AAC52996.1}; Synonyms=Pafahg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8954729; DOI=10.1006/dbio.1996.0330;
RA Albrecht U., Abu-Issa R., Raetz B., Hattori M., Aoki J., Arai H., Inoue K.,
RA Eichele G.;
RT "Platelet-activating factor acetylhydrolase expression and activity suggest
RT a link between neuronal migration and platelet-activating factor.";
RL Dev. Biol. 180:579-593(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=12775763; DOI=10.1073/pnas.1236145100;
RA Yan W., Assadi A.H., Wynshaw-Boris A., Eichele G., Matzuk M.M., Clark G.D.;
RT "Previously uncharacterized roles of platelet-activating factor
RT acetylhydrolase 1b complex in mouse spermatogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7189-7194(2003).
RN [4]
RP INTERACTION WITH VLDLR.
RX PubMed=17330141; DOI=10.1371/journal.pone.0000252;
RA Zhang G., Assadi A.H., McNeil R.S., Beffert U., Wynshaw-Boris A., Herz J.,
RA Clark G.D., D'Arcangelo G.;
RT "The Pafah1b complex interacts with the reelin receptor VLDLR.";
RL PLoS ONE 2:e252-e252(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Alpha1 catalytic subunit of the cytosolic type I platelet-
CC activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric
CC enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2
CC position of PAF and its analogs and modulates the action of PAF. The
CC activity and substrate specificity of PAF-AH (I) are affected by its
CC subunit composition. Both alpha1/alpha1 homodimer (PAFAH1B3/PAFAH1B3
CC homodimer) and alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B2 heterodimer)
CC hydrolyze 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA) more
CC efficiently than PAF, but they have little hydrolytic activity towards
CC 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE). Plays
CC an important role during the development of brain.
CC {ECO:0000250|UniProtKB:Q29460}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC Evidence={ECO:0000250|UniProtKB:Q29460};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000250|UniProtKB:Q29460};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000250|UniProtKB:Q29460};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000250|UniProtKB:Q29460};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + H2O = 1-O-
CC hexadecyl-sn-glycero-3-phosphate + acetate + H(+);
CC Xref=Rhea:RHEA:41704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:77580, ChEBI:CHEBI:78385;
CC Evidence={ECO:0000250|UniProtKB:Q29460};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705;
CC Evidence={ECO:0000250|UniProtKB:Q29460};
CC -!- ACTIVITY REGULATION: Beta subunit (PAFAH1B1) inhibits the
CC acetylhydrolase activity of the alpha1/alpha1 catalytic homodimer.
CC {ECO:0000250|UniProtKB:Q29460}.
CC -!- SUBUNIT: Forms a catalytic dimer which is either homodimer
CC (alpha1/alpha1 homodimer) or heterodimer with PAFAH1B2 (alpha1/alpha2
CC heterodimer). Component of the cytosolic (PAF-AH (I)) heterotetrameric
CC enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2 (alpha2) and
CC PAFAH1B3 (alpha1) subunits. The catalytic activity of the enzyme
CC resides in the alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits,
CC whereas the beta subunit (PAFAH1B1) has regulatory activity. Trimer
CC formation is not essential for the catalytic activity (By similarity).
CC Interacts with VLDLR; this interaction may modulate the Reelin pathway
CC (PubMed:17330141). {ECO:0000250|UniProtKB:Q29460,
CC ECO:0000269|PubMed:17330141}.
CC -!- INTERACTION:
CC Q61205; P63005: Pafah1b1; NbExp=2; IntAct=EBI-1007637, EBI-917499;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Expressed already by the time of neurulation. By
CC 10.5 dpc, expression is abundant in the developing central and
CC peripheral nervous systems. Major sites include the neuroepithelium of
CC the fore-, mid-, and hindbrain, the spinal cord, the dorsal root, and
CC cranial ganglia. In adult brain, expression is greatly diminished.
CC -!- DISRUPTION PHENOTYPE: Knockout mice which are homozygous for the
CC PAFAH1B2 gene appear developmentally normal, and are born at the
CC expected Mendelian rate. Mice have normal fertility and normal
CC spermatogenesis. Double mutant female mice which are homozygous for
CC PAFAH1B2 and PAFAH1B3 are grossly normal and fertile, whereas double-
CC mutant males are infertile. Double mutan mice manifest an earlier
CC disturbance of spermatogenesis with an onset at preleptotene or
CC leptotene stages of meiosis. {ECO:0000269|PubMed:12775763}.
CC -!- MISCELLANEOUS: Originally the subunits of the type I platelet-
CC activating factor (PAF) acetylhydrolase was named alpha (PAFAH1B1),
CC beta (PAFAH1B2) and gamma (PAFAH1B3) (By similarity). Now these
CC subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and
CC alpha1 (PAFAH1B3) respectively (By similarity).
CC {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P68402,
CC ECO:0000250|UniProtKB:Q15102, ECO:0000250|UniProtKB:Q29460}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. Platelet-
CC activating factor acetylhydrolase IB beta/gamma subunits subfamily.
CC {ECO:0000305}.
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DR EMBL; U57746; AAC52996.1; -; mRNA.
DR EMBL; BC067015; AAH67015.1; -; mRNA.
DR CCDS; CCDS20979.1; -.
DR RefSeq; NP_032802.1; NM_008776.2.
DR RefSeq; XP_017177515.1; XM_017322026.1.
DR RefSeq; XP_017177516.1; XM_017322027.1.
DR AlphaFoldDB; Q61205; -.
DR SMR; Q61205; -.
DR BioGRID; 202017; 8.
DR IntAct; Q61205; 1.
DR STRING; 10090.ENSMUSP00000005583; -.
DR ChEMBL; CHEMBL3259482; -.
DR iPTMnet; Q61205; -.
DR PhosphoSitePlus; Q61205; -.
DR SwissPalm; Q61205; -.
DR REPRODUCTION-2DPAGE; Q61205; -.
DR EPD; Q61205; -.
DR jPOST; Q61205; -.
DR MaxQB; Q61205; -.
DR PaxDb; Q61205; -.
DR PRIDE; Q61205; -.
DR ProteomicsDB; 295448; -.
DR Antibodypedia; 30926; 286 antibodies from 26 providers.
DR DNASU; 18476; -.
DR Ensembl; ENSMUST00000005583; ENSMUSP00000005583; ENSMUSG00000005447.
DR GeneID; 18476; -.
DR KEGG; mmu:18476; -.
DR UCSC; uc009fsf.1; mouse.
DR CTD; 5050; -.
DR MGI; MGI:108414; Pafah1b3.
DR VEuPathDB; HostDB:ENSMUSG00000005447; -.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00950000183199; -.
DR HOGENOM; CLU_051989_2_0_1; -.
DR InParanoid; Q61205; -.
DR OMA; HHRFIAD; -.
DR OrthoDB; 1604899at2759; -.
DR PhylomeDB; Q61205; -.
DR TreeFam; TF323955; -.
DR BRENDA; 3.1.1.47; 3474.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 18476; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Pafah1b3; mouse.
DR PRO; PR:Q61205; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61205; protein.
DR Bgee; ENSMUSG00000005447; Expressed in cortical plate and 268 other tissues.
DR ExpressionAtlas; Q61205; baseline and differential.
DR Genevisible; Q61205; MM.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15102"
FT CHAIN 2..232
FT /note="Platelet-activating factor acetylhydrolase IB
FT subunit alpha1"
FT /id="PRO_0000058156"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 48
FT /evidence="ECO:0000250|UniProtKB:Q29460"
FT ACT_SITE 193
FT /evidence="ECO:0000250|UniProtKB:Q29460"
FT ACT_SITE 196
FT /evidence="ECO:0000250|UniProtKB:Q29460"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q15102"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15102"
SQ SEQUENCE 232 AA; 25853 MW; 5D3C63E2A611670B CRC64;
MSGEGENPAS KPTPVQDVQG DGRWMSLHHR FVADSKDKEP EVVFIGDSLV QLMHQCEIWR
ELFSPLHALN FGIGGDSTQH VLWRLENGEL EHIRPKIVVV WVGTNNHSHT AEQVTGGIKA
IVQLVNKLQP QARVVVLGLL PRGQHPNPLR EKNRQVNELV RAALAGYPRA HFLDADPGFV
HSDGTISHHD MYDYLHLSRL GYTPVCRALH SLLLRLLAQD QGQGIPLPET AS
