ID PA1B3_RAT Reviewed; 232 AA. AC O35263; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 153. DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha1 {ECO:0000305}; DE EC=3.1.1.47 {ECO:0000269|PubMed:9660828}; 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; DE AltName: Full=Platelet-activating factor acetylhydrolase alpha 1 subunit; DE Short=PAF-AH alpha 1; GN Name=Pafah1b3 {ECO:0000312|RGD:620333}; Synonyms=Pafahg; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Brain; RX PubMed=9459487; DOI=10.1016/s0167-4889(97)00128-6; RA Watanabe M., Aoki J., Manya H., Arai H., Inoue K.; RT "Molecular cloning of cDNAs encoding alpha1, alpha2, and beta subunits of RT rat brain platelet-activating factor acetylhydrolase."; RL Biochim. Biophys. Acta 1401:73-79(1998). RN [2] RP TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND RP DEVELOPMENTAL STAGE. RX PubMed=9660828; DOI=10.1074/jbc.273.29.18567; RA Manya H., Aoki J., Watanabe M., Adachi T., Asou H., Inoue Y., Arai H., RA Inoue K.; RT "Switching of platelet-activating factor acetylhydrolase catalytic subunits RT in developing rat brain."; RL J. Biol. Chem. 273:18567-18572(1998). 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:9660828). The activity and substrate specificity of PAF-AH (I) CC are affected by its subunit composition. Both alpha1/alpha1 homodimer CC (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). Plays an important role CC during the development of brain (By similarity). CC {ECO:0000250|UniProtKB:Q29460, ECO:0000269|PubMed:9660828}. 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:9660828}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; CC Evidence={ECO:0000305|PubMed:9660828}; 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:9660828}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; CC Evidence={ECO:0000305|PubMed:9660828}; 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:Q29460}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705; CC Evidence={ECO:0000250|UniProtKB:Q29460}; CC -!- ACTIVITY REGULATION: Beta subunit (PAFAH1B1) inhibits the CC acetylhydrolase activity of the alpha1/alpha1 catalytic homodimer. CC {ECO:0000250|UniProtKB:Q29460}. CC -!- SUBUNIT: Forms a catalytic dimer which is either homodimer CC (alpha1/alpha1 homodimer) or heterodimer with PAFAH1B2 (alpha1/alpha2 CC heterodimer) (PubMed:9660828). Component of the cytosolic (PAF-AH (I)) CC heterotetrameric enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2 CC (alpha2) and PAFAH1B3 (alpha1) subunits. The catalytic activity of the CC enzyme 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 with VLDLR; this interaction may modulate the Reelin pathway CC (By similarity). {ECO:0000250|UniProtKB:Q29460, CC ECO:0000250|UniProtKB:Q61205, ECO:0000269|PubMed:9660828}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in brain, spleen, lung, liver, kidney and CC testis. Not expressed in heart and skeletal muscle. Expressed in fetal CC brain as heterodimer (PubMed:9660828). Not expressed in adult tissues CC (PubMed:9660828). Expressed exclusively in granule cells CC (PubMed:9660828). {ECO:0000269|PubMed:9660828}. CC -!- DEVELOPMENTAL STAGE: During the embryonic stages, high expressed in the CC brain, spinal cord, sensory ganglia (dorsal root and trigeminal CC ganglia), and thymus. In brain found throughout the ventricular and CC marginal zones. Expressed mainly in neural tissues. CC {ECO:0000269|PubMed:9660828}. 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:9459487). CC {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P68402, CC ECO:0000250|UniProtKB:Q15102, ECO:0000303|PubMed:9459487}. 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; AF016047; AAC27973.1; -; mRNA. DR RefSeq; NP_446106.1; NM_053654.2. DR RefSeq; XP_006228427.1; XM_006228365.3. DR RefSeq; XP_017444141.1; XM_017588652.1. DR AlphaFoldDB; O35263; -. DR SMR; O35263; -. DR IntAct; O35263; 1. DR STRING; 10116.ENSRNOP00000027774; -. DR PhosphoSitePlus; O35263; -. DR jPOST; O35263; -. DR PaxDb; 10116-ENSRNOP00000027774; -. DR Ensembl; ENSRNOT00000027774.5; ENSRNOP00000027774.2; ENSRNOG00000020481.5. DR Ensembl; ENSRNOT00055057956; ENSRNOP00055047796; ENSRNOG00055033531. DR Ensembl; ENSRNOT00060053458; ENSRNOP00060044412; ENSRNOG00060030747. DR Ensembl; ENSRNOT00065002034; ENSRNOP00065001435; ENSRNOG00065001520. DR Ensembl; ENSRNOT00065055510; ENSRNOP00065045676; ENSRNOG00065032241. DR GeneID; 114113; -. DR KEGG; rno:114113; -. DR UCSC; RGD:620333; rat. DR AGR; RGD:620333; -. DR CTD; 5050; -. DR RGD; 620333; Pafah1b3. DR eggNOG; KOG1388; Eukaryota. DR GeneTree; ENSGT00950000183199; -. DR HOGENOM; CLU_051989_2_0_1; -. DR InParanoid; O35263; -. DR OMA; HHRFIAD; -. DR OrthoDB; 4162633at2759; -. DR PhylomeDB; O35263; -. DR TreeFam; TF323955; -. DR BRENDA; 3.1.1.47; 5301. DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR PRO; PR:O35263; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000020481; Expressed in jejunum and 19 other cell types or tissues. DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; TAS:RGD. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0007283; P:spermatogenesis; ISO:RGD. 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. DR Genevisible; O35263; RN. PE 1: Evidence at protein 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:Q15102" FT CHAIN 2..232 FT /note="Platelet-activating factor acetylhydrolase IB FT subunit alpha1" FT /id="PRO_0000058157" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 48 FT /evidence="ECO:0000250|UniProtKB:Q29460" FT ACT_SITE 193 FT /evidence="ECO:0000250|UniProtKB:Q29460" FT ACT_SITE 196 FT /evidence="ECO:0000250|UniProtKB:Q29460" 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" SQ SEQUENCE 232 AA; 25863 MW; 5FEC63E2A611670B CRC64; MSGEGENPAS KPTPVQDVQG DGRWMSLHHR FVADSKDKEP EVVFIGDSLV QLMHQCEIWR ELFSPLHALN FGIGGDSTQH VLWRLENGEL EHIRPKIVVV WVGTNNHSHT AEQVTGGIKA IVQLVNKLQP QARVVVLGLL PRGQHPNPLR EKNRQVNELV RAALAGYPRA HFLDADPGFV HSDGTISHHD MYDYLHLSRL GYTPVCRALH SLLLRLLAQD QGQGIPLPET AP //