PA1B2_BOVIN
ID PA1B2_BOVIN Reviewed; 229 AA.
AC P68401; O00687; Q29459; Q3ZBB8;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha2 {ECO:0000305};
DE EC=3.1.1.47 {ECO:0000269|PubMed:10542206};
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=PAFAH1B2P68402; Synonyms=PAFAHB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 37-53; 134-152 AND
RP 167-196.
RC TISSUE=Brain;
RX PubMed=8537406; DOI=10.1074/jbc.270.52.31345;
RA Hattori M., Adachi H., Aoki J., Tsujimoto M., Arai H., Inoue K.;
RT "Cloning and expression of a cDNA encoding the beta-subunit (30-kDa
RT subunit) of bovine brain platelet-activating factor acetylhydrolase.";
RL J. Biol. Chem. 270:31345-31352(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, AND INTERACTION
RP WITH PAFAH1B1.
RX PubMed=10542206; DOI=10.1074/jbc.274.45.31827;
RA Manya H., Aoki J., Kato H., Ishii J., Hino S., Arai H., Inoue K.;
RT "Biochemical characterization of various catalytic complexes of the brain
RT platelet-activating factor acetylhydrolase.";
RL J. Biol. Chem. 274:31827-31832(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RC TISSUE=Brain;
RX PubMed=11522926; DOI=10.1093/protein/14.7.513;
RA Sheffield P.J., McMullen T.W., Li J., Ho Y.S., Garrard S.M., Derewenda U.,
RA Derewenda Z.S.;
RT "Preparation and crystal structure of the recombinant alpha(1)/alpha(2)
RT catalytic heterodimer of bovine brain platelet-activating factor
RT acetylhydrolase Ib.";
RL Protein Eng. 14:513-519(2001).
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
CC (PubMed:10542206). The activity and substrate specificity of PAF-AH (I)
CC are affected by its subunit composition (PubMed:10542206). The
CC alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 homodimer) hydrolyzes PAF
CC and 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE) more
CC efficiently than 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid
CC (AAGPA) (PubMed:10542206). In contrast, the alpha1/alpha2
CC heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes AAGPA more
CC efficiently than PAF, but has little hydrolytic activity towards AAGPE
CC (PubMed:10542206). May play a role in male germ cell meiosis during the
CC late pachytenestage and meiotic divisions as well as early
CC spermiogenesis (By similarity). {ECO:0000250|UniProtKB:Q61206,
CC ECO:0000269|PubMed:10542206}.
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:0000269|PubMed:10542206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000305|PubMed:10542206};
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:0000269|PubMed:10542206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000305|PubMed:10542206};
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:0000269|PubMed:10542206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705;
CC Evidence={ECO:0000305|PubMed:10542206};
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:0000269|PubMed:10542206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41709;
CC Evidence={ECO:0000305|PubMed:10542206};
CC -!- ACTIVITY REGULATION: Beta subunit (PAFAH1B1) stimulates the
CC acetylhydrolase activity of the alpha2/alpha2 catalytic homodimer.
CC {ECO:0000269|PubMed:10542206}.
CC -!- SUBUNIT: Forms a catalytic dimer which is either homodimer
CC (alpha2/alpha2 homodimer) or heterodimer with PAFAH1B3 (alpha2/alpha1
CC heterodimer) (PubMed:10542206). Component of the cytosolic (PAF-AH (I))
CC heterotetrameric enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2
CC (alpha2) and PAFAH1B3 (alpha1) subunits (PubMed:10542206). The
CC catalytic activity of the enzyme resides in the alpha1 (PAFAH1B3) and
CC alpha2 (PAFAH1B2) subunits, whereas the beta subunit (PAFAH1B1) has
CC regulatory activity (PubMed:10542206). Trimer formation is not
CC essential for the catalytic activity (PubMed:10542206). Interacts
CC (homodimer form) with PAFAH1B1 (homodimer form); PAFAH1B2 competes with
CC NDEL1 for PAFAH1B1 binding (By similarity). Interacts with VLDLR; this
CC interaction may modulate the Reelin pathway (By similarity).
CC {ECO:0000250|UniProtKB:P68402, ECO:0000250|UniProtKB:Q61206,
CC ECO:0000269|PubMed:10542206}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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) (PubMed:8537406).
CC Now these subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2)
CC and alpha1 (PAFAH1B3) respectively (By similarity).
CC {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:Q15102,
CC ECO:0000250|UniProtKB:Q29460, ECO:0000303|PubMed:8537406}.
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; D49678; BAA08534.1; -; mRNA.
DR EMBL; BC103452; AAI03453.1; -; mRNA.
DR RefSeq; NP_777089.1; NM_174664.2.
DR PDB; 1FXW; X-ray; 2.10 A; F=1-229.
DR PDBsum; 1FXW; -.
DR AlphaFoldDB; P68401; -.
DR SMR; P68401; -.
DR CORUM; P68401; -.
DR IntAct; P68401; 1.
DR MINT; P68401; -.
DR STRING; 9913.ENSBTAP00000007398; -.
DR SwissLipids; SLP:000000692; -.
DR PaxDb; P68401; -.
DR PeptideAtlas; P68401; -.
DR PRIDE; P68401; -.
DR Ensembl; ENSBTAT00000007398; ENSBTAP00000007398; ENSBTAG00000005627.
DR GeneID; 282514; -.
DR KEGG; bta:282514; -.
DR CTD; 5049; -.
DR VEuPathDB; HostDB:ENSBTAG00000005627; -.
DR VGNC; VGNC:32550; PAFAH1B2.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00950000183199; -.
DR HOGENOM; CLU_051989_2_0_1; -.
DR InParanoid; P68401; -.
DR OMA; QQCEIWR; -.
DR OrthoDB; 1604899at2759; -.
DR TreeFam; TF323955; -.
DR BRENDA; 3.1.1.47; 908.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; P68401; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000005627; Expressed in occipital lobe and 107 other tissues.
DR ExpressionAtlas; P68401; baseline and differential.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Lipid degradation; Lipid metabolism; 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_0000058149"
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"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1FXW"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:1FXW"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:1FXW"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:1FXW"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1FXW"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1FXW"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1FXW"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1FXW"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1FXW"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:1FXW"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:1FXW"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1FXW"
FT HELIX 111..128
FT /evidence="ECO:0007829|PDB:1FXW"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1FXW"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1FXW"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:1FXW"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:1FXW"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1FXW"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:1FXW"
FT HELIX 199..216
FT /evidence="ECO:0007829|PDB:1FXW"
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
