PA1B2_PONAB
ID PA1B2_PONAB Reviewed; 229 AA.
AC Q5R4G2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha2 {ECO:0000250|UniProtKB:P68401};
DE EC=3.1.1.47 {ECO:0000250|UniProtKB:P68401};
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 {ECO:0000250|UniProtKB:P68402}; Synonyms=PAFAHB;
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: Alpha2 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. The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2
CC homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3-
CC phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2-
CC acetyl-sn-glycero-3-phosphoric acid (AAGPA). In contrast, the
CC alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes
CC AAGPA more efficiently than PAF, but has little hydrolytic activity
CC towards AAGPE (By similarity). May play a role in male germ cell
CC meiosis during the late pachytenestage and meiotic divisions as well as
CC early spermiogenesis (By similarity). {ECO:0000250|UniProtKB:P68401,
CC ECO:0000250|UniProtKB:Q61206}.
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:P68401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000250|UniProtKB:P68401};
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:P68401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000250|UniProtKB:P68401};
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:P68401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705;
CC Evidence={ECO:0000250|UniProtKB:P68401};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphoethanolamine + H2O
CC = 1-O-hexadecyl-sn-glycero-3-phosphoethanolamine + acetate + H(+);
CC Xref=Rhea:RHEA:41708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:78387, ChEBI:CHEBI:78390;
CC Evidence={ECO:0000250|UniProtKB:P68401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41709;
CC Evidence={ECO:0000250|UniProtKB:P68401};
CC -!- ACTIVITY REGULATION: Beta subunit (PAFAH1B1) stimulates the
CC acetylhydrolase activity of the alpha2/alpha2 catalytic homodimer.
CC {ECO:0000250|UniProtKB:P68401}.
CC -!- SUBUNIT: Forms a catalytic dimer which is either homodimer
CC (alpha2/alpha2 homodimer) or heterodimer with PAFAH1B3 (alpha2/alpha1
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 (homodimer form) with PAFAH1B1 (homodimer form); PAFAH1B2
CC competes with NDEL1 for PAFAH1B1 binding (By similarity). Interacts
CC with VLDLR; this interaction may modulate the Reelin pathway (By
CC similarity). {ECO:0000250|UniProtKB:P68401,
CC ECO:0000250|UniProtKB:P68402, ECO:0000250|UniProtKB:Q61206}.
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; CR861287; CAH93354.1; -; mRNA.
DR RefSeq; NP_001126974.1; NM_001133502.1.
DR AlphaFoldDB; Q5R4G2; -.
DR SMR; Q5R4G2; -.
DR STRING; 9601.ENSPPYP00000023693; -.
DR Ensembl; ENSPPYT00000004652; ENSPPYP00000004476; ENSPPYG00000003907.
DR GeneID; 100173993; -.
DR KEGG; pon:100173993; -.
DR CTD; 5049; -.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00950000183199; -.
DR HOGENOM; CLU_051989_2_0_1; -.
DR InParanoid; Q5R4G2; -.
DR OrthoDB; 1604899at2759; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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 GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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:P68402"
FT CHAIN 2..229
FT /note="Platelet-activating factor acetylhydrolase IB
FT subunit alpha2"
FT /id="PRO_0000252683"
FT ACT_SITE 48
FT /evidence="ECO:0000250"
FT ACT_SITE 193
FT /evidence="ECO:0000250"
FT ACT_SITE 196
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P68402"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68402"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68402"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61206"
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
