PA1B3_PONAB
ID PA1B3_PONAB Reviewed; 231 AA.
AC Q5R6X1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha1 {ECO:0000250|UniProtKB:Q15102};
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:0000250|UniProtKB:Q15102}; Synonyms=PAFAHG;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:Q29460,
CC ECO:0000250|UniProtKB:Q61205}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; CR860358; CAH92489.1; -; mRNA.
DR RefSeq; NP_001126468.1; NM_001132996.1.
DR RefSeq; XP_009230936.1; XM_009232661.1.
DR AlphaFoldDB; Q5R6X1; -.
DR SMR; Q5R6X1; -.
DR STRING; 9601.ENSPPYP00000011239; -.
DR GeneID; 100173455; -.
DR KEGG; pon:100173455; -.
DR CTD; 5050; -.
DR eggNOG; KOG1388; Eukaryota.
DR InParanoid; Q5R6X1; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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..231
FT /note="Platelet-activating factor acetylhydrolase IB
FT subunit alpha1"
FT /id="PRO_0000252685"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:Q29460"
FT ACT_SITE 192
FT /evidence="ECO:0000250|UniProtKB:Q29460"
FT ACT_SITE 195
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 231 AA; 25748 MW; E5A47630AFB13356 CRC64;
MSGEENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ LMHQCEIWRE
LFSPLHALNF GIGGDGTQHV LWRLENGELE HIRPKIVVVW VGTNNHGHTA EQVTGGIKAI
VQLVNERQPQ ARVVVLDLLP RGQHPNPLRE KNQRVNELVR AALAGHPRAH FLDADPGFVH
SDGTISHHDM YDYLHLSRLG YAPVCRALHS LLLRLLAQDQ GQGAPLLDPA P
