PA1B3_BOVIN
ID PA1B3_BOVIN Reviewed; 232 AA.
AC Q29460; Q0VCF0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha1 {ECO:0000305};
DE EC=3.1.1.47 {ECO:0000269|PubMed:10542206};
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 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 38-85; 96-111 AND
RP 119-151.
RC TISSUE=Brain;
RX PubMed=8083218; DOI=10.1016/s0021-9258(17)31632-0;
RA Hattori M., Adachi H., Tsujimoto M., Arai H., Inoue K.;
RT "The catalytic subunit of bovine brain platelet-activating factor
RT acetylhydrolase is a novel type of serine esterase.";
RL J. Biol. Chem. 269:23150-23155(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal brain;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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 (1.7 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=8985254; DOI=10.1038/385089a0;
RA Ho Y.S., Swenson L., Derewenda U., Serre L., Wei Y., Dauter Z., Hattori M.,
RA Adachi T., Aoki J., Arai H., Inoue K., Derewenda Z.S.;
RT "Brain acetylhydrolase that inactivates platelet-activating factor is a G-
RT protein-like trimer.";
RL Nature 385:89-93(1997).
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
CC (PubMed:10542206). The activity and substrate specificity of PAF-AH (I)
CC are affected by its subunit composition (PubMed:10542206). Both
CC alpha1/alpha1 homodimer (PAFAH1B3/PAFAH1B3 homodimer) and alpha1/alpha2
CC heterodimer(PAFAH1B3/PAFAH1B2 heterodimer) hydrolyze 1-O-alkyl-2-
CC acetyl-sn-glycero-3-phosphoric acid (AAGPA) more efficiently than PAF,
CC but they have little hydrolytic activity towards 1-O-alkyl-2-acetyl-sn-
CC glycero-3-phosphorylethanolamine (AAGPE) (PubMed:10542206). Plays an
CC important role during the development of brain.
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 -!- ACTIVITY REGULATION: Beta subunit (PAFAH1B1) inhibits the
CC acetylhydrolase activity of the alpha1/alpha1 catalytic homodimer.
CC {ECO:0000269|PubMed:10542206}.
CC -!- SUBUNIT: Forms a catalytic dimer which is either homodimer
CC (alpha1/alpha1 homodimer) or heterodimer with PAFAH1B2 (alpha1/alpha2
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 with
CC VLDLR; this interaction may modulate the Reelin pathway (By
CC similarity). {ECO:0000250|UniProtKB:Q61205,
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). Now these
CC subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and
CC alpha1 (PAFAH1B3) respectively (PubMed:8985254).
CC {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P68402,
CC ECO:0000250|UniProtKB:Q15102, ECO:0000269|PubMed:8985254}.
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; D30789; BAA06455.1; -; mRNA.
DR EMBL; BC120202; AAI20203.1; -; mRNA.
DR PIR; A54754; A54754.
DR RefSeq; NP_777090.1; NM_174665.2.
DR PDB; 1BWP; X-ray; 2.10 A; A=1-232.
DR PDB; 1BWQ; X-ray; 2.30 A; A=1-232.
DR PDB; 1BWR; X-ray; 2.40 A; A=1-232.
DR PDB; 1ES9; X-ray; 1.30 A; A=1-232.
DR PDB; 1FXW; X-ray; 2.10 A; A=1-232.
DR PDB; 1WAB; X-ray; 1.70 A; A=1-232.
DR PDB; 3DT6; X-ray; 2.10 A; A=1-232.
DR PDB; 3DT8; X-ray; 1.85 A; A=1-232.
DR PDB; 3DT9; X-ray; 1.85 A; A=1-232.
DR PDBsum; 1BWP; -.
DR PDBsum; 1BWQ; -.
DR PDBsum; 1BWR; -.
DR PDBsum; 1ES9; -.
DR PDBsum; 1FXW; -.
DR PDBsum; 1WAB; -.
DR PDBsum; 3DT6; -.
DR PDBsum; 3DT8; -.
DR PDBsum; 3DT9; -.
DR AlphaFoldDB; Q29460; -.
DR SMR; Q29460; -.
DR CORUM; Q29460; -.
DR IntAct; Q29460; 1.
DR MINT; Q29460; -.
DR STRING; 9913.ENSBTAP00000026366; -.
DR SwissLipids; SLP:000000693; -.
DR iPTMnet; Q29460; -.
DR PaxDb; Q29460; -.
DR PeptideAtlas; Q29460; -.
DR PRIDE; Q29460; -.
DR Ensembl; ENSBTAT00000026366; ENSBTAP00000026366; ENSBTAG00000019787.
DR Ensembl; ENSBTAT00000067093; ENSBTAP00000066532; ENSBTAG00000019787.
DR GeneID; 282515; -.
DR KEGG; bta:282515; -.
DR CTD; 5050; -.
DR VEuPathDB; HostDB:ENSBTAG00000019787; -.
DR VGNC; VGNC:32551; PAFAH1B3.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00950000183199; -.
DR HOGENOM; CLU_051989_2_0_1; -.
DR InParanoid; Q29460; -.
DR OMA; HHRFIAD; -.
DR OrthoDB; 1604899at2759; -.
DR TreeFam; TF323955; -.
DR BRENDA; 3.1.1.47; 908.
DR EvolutionaryTrace; Q29460; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000019787; Expressed in pons and 106 other tissues.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
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; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS: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:0007283; P:spermatogenesis; ISS:AgBase.
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:Q15102"
FT CHAIN 2..232
FT /note="Platelet-activating factor acetylhydrolase IB
FT subunit alpha1"
FT /id="PRO_0000058154"
FT ACT_SITE 47
FT /evidence="ECO:0000269|PubMed:8985254,
FT ECO:0007744|PDB:1BWP"
FT ACT_SITE 192
FT /evidence="ECO:0000269|PubMed:8985254,
FT ECO:0007744|PDB:1BWP"
FT ACT_SITE 195
FT /evidence="ECO:0000269|PubMed:8985254,
FT ECO:0007744|PDB:1BWP"
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"
FT CONFLICT 79
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="E -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1ES9"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1ES9"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:1ES9"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1ES9"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1ES9"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1ES9"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:1ES9"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1ES9"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1ES9"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:1ES9"
FT TURN 86..91
FT /evidence="ECO:0007829|PDB:1ES9"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1ES9"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:1ES9"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1ES9"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1ES9"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:1ES9"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1ES9"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:1ES9"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1ES9"
FT HELIX 198..215
FT /evidence="ECO:0007829|PDB:1ES9"
SQ SEQUENCE 232 AA; 25865 MW; 81C2CECA8E2204ED CRC64;
MSGDENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ LMHQCEIWRE
LFSPLHALNF GIGGDSTQHV LWRLENGELE HIRPKIVVVW VGTNNHGHTA EQVTGGIKAI
VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE KNRRVNELVR AALAGHPRAH FLDADPGFVH
SDGTISHHDM YDYLHLSRLG YTPVCRALHS LLLRLLTQDQ GQGGAPLPEP SP
