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   27-MAR-2024, entry version 155.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.ENSBTAP00000066532; -.
DR   SwissLipids; SLP:000000693; -.
DR   iPTMnet; Q29460; -.
DR   PaxDb; 9913-ENSBTAP00000026366; -.
DR   PeptideAtlas; Q29460; -.
DR   Ensembl; ENSBTAT00000026366.4; ENSBTAP00000026366.3; ENSBTAG00000019787.4.
DR   Ensembl; ENSBTAT00000067093.1; ENSBTAP00000066532.1; ENSBTAG00000019787.4.
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; 4162633at2759; -.
DR   TreeFam; TF323955; -.
DR   BRENDA; 3.1.1.47; 908.
DR   Reactome; R-BTA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   EvolutionaryTrace; Q29460; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000019787; Expressed in pons and 106 other cell types or 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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; ISS:AgBase.
DR   CDD; cd01820; PAF_acetylesterase_like; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR11852; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR   PANTHER; PTHR11852:SF2; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT ALPHA1; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 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
//