PA1B3_RAT
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 03-AUG-2022, entry version 146.
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}.
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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 jPOST; O35263; -.
DR PaxDb; O35263; -.
DR PRIDE; O35263; -.
DR Ensembl; ENSRNOT00000027774; ENSRNOP00000027774; ENSRNOG00000020481.
DR GeneID; 114113; -.
DR KEGG; rno:114113; -.
DR UCSC; RGD:620333; rat.
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; 1604899at2759; -.
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 tissues.
DR Genevisible; O35263; RN.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA: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:0007420; P:brain development; IEP:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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 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
