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 27-MAR-2024, entry version 130. 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}. 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; 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; 9913-ENSBTAP00000007398; -. DR PeptideAtlas; P68401; -. DR Ensembl; ENSBTAT00000007398.4; ENSBTAP00000007398.3; ENSBTAG00000005627.4. 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; EAWNQYF; -. DR OrthoDB; 4162633at2759; -. DR TreeFam; TF323955; -. DR BRENDA; 3.1.1.47; 908. DR Reactome; R-BTA-6798695; Neutrophil degranulation. DR Reactome; R-BTA-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR EvolutionaryTrace; P68401; -. DR Proteomes; UP000009136; Chromosome 15. DR Bgee; ENSBTAG00000005627; Expressed in occipital lobe and 107 other cell types or 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: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 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:SF1; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT ALPHA2; 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: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 //