PA1B2_RAT
ID PA1B2_RAT Reviewed; 229 AA.
AC O35264;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha2 {ECO:0000305};
DE EC=3.1.1.47 {ECO:0000250|UniProtKB:P68401};
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;
DE AltName: Full=Platelet-activating factor acetylhydrolase alpha 2 subunit;
DE Short=PAF-AH alpha 2;
GN Name=Pafah1b2 {ECO:0000312|RGD:620332}; Synonyms=Pafahb;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 61-79 AND 134-142, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-64 AND THR-220, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:9660828). The activity and substrate specificity of PAF-AH (I)
CC are affected by its subunit composition. The alpha2/alpha2 homodimer
CC (PAFAH1B2/PAFAH1B2 homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-
CC glycero-3-phosphorylethanolamine (AAGPE) more efficiently than 1-O-
CC alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA). In contrast, the
CC alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes
CC AAGPA more efficiently than PAF, but has little hydrolytic activity
CC towards AAGPE (By similarity). May play a role in male germ cell
CC meiosis during the late pachytenestage and meiotic divisions as well as
CC early spermiogenesis (By similarity). {ECO:0000250|UniProtKB:P68401,
CC ECO:0000250|UniProtKB:Q61206, 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:P68401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705;
CC Evidence={ECO:0000250|UniProtKB:P68401};
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:0000250|UniProtKB:P68401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41709;
CC Evidence={ECO:0000250|UniProtKB:P68401};
CC -!- ACTIVITY REGULATION: Beta subunit (PAFAH1B1) stimulates the
CC acetylhydrolase activity of the alpha2/alpha2 catalytic homodimer.
CC {ECO:0000250|UniProtKB:P68401}.
CC -!- SUBUNIT: Forms a catalytic dimer which is either homodimer
CC (alpha2/alpha2 homodimer) or heterodimer with PAFAH1B3 (alpha2/alpha1
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 (PubMed:9660828). The catalytic
CC activity of the enzyme resides in the alpha1 (PAFAH1B3) and alpha2
CC (PAFAH1B2) subunits, whereas the beta subunit (PAFAH1B1) has regulatory
CC activity. Trimer formation is not essential for the catalytic activity
CC (By similarity). Interacts (homodimer form) with PAFAH1B1 (homodimer
CC form); PAFAH1B2 competes with NDEL1 for PAFAH1B1 binding (By
CC similarity). Interacts with VLDLR; this interaction may modulate the
CC Reelin pathway (By similarity). {ECO:0000250|UniProtKB:P68401,
CC ECO:0000250|UniProtKB:P68402, ECO:0000250|UniProtKB:Q61206,
CC ECO:0000269|PubMed:9660828}.
CC -!- INTERACTION:
CC O35264; P43033: PAFAH1B1; Xeno; NbExp=2; IntAct=EBI-915500, EBI-1007886;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver,
CC kidney and testis. Not expressed in skeletal muscle. Expressed in fetal
CC as heterodimer and adult brain as homodimer. In neural cells, expressed
CC in granule cells, astroglial cells, and oligodendrocytes
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. {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 (By similarity).
CC {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P68402,
CC ECO:0000250|UniProtKB:Q15102, ECO:0000250|UniProtKB:Q29460}.
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; AF016048; AAC27974.1; -; mRNA.
DR EMBL; BC081714; AAH81714.1; -; mRNA.
DR RefSeq; NP_071782.1; NM_022387.3.
DR RefSeq; XP_006243020.1; XM_006242958.3.
DR AlphaFoldDB; O35264; -.
DR SMR; O35264; -.
DR IntAct; O35264; 2.
DR STRING; 10116.ENSRNOP00000024828; -.
DR iPTMnet; O35264; -.
DR PhosphoSitePlus; O35264; -.
DR SwissPalm; O35264; -.
DR jPOST; O35264; -.
DR PaxDb; O35264; -.
DR PRIDE; O35264; -.
DR Ensembl; ENSRNOT00000111151; ENSRNOP00000091075; ENSRNOG00000057102.
DR GeneID; 64189; -.
DR KEGG; rno:64189; -.
DR UCSC; RGD:620332; rat.
DR CTD; 5049; -.
DR RGD; 620332; Pafah1b2.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00950000183199; -.
DR HOGENOM; CLU_051989_2_0_1; -.
DR InParanoid; O35264; -.
DR OMA; QQCEIWR; -.
DR OrthoDB; 1604899at2759; -.
DR PhylomeDB; O35264; -.
DR TreeFam; TF323955; -.
DR BRENDA; 3.1.1.47; 5301.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR PRO; PR:O35264; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000057102; Expressed in cerebellum and 19 other tissues.
DR Genevisible; O35264; 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: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:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; IDA: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:0016239; P:positive regulation of macroautophagy; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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; 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_0000058153"
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:0007744|PubMed:22673903"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 229 AA; 25581 MW; B4D24048621AB182 CRC64;
MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR
ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA
IVQLINTRQP QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDIDGGFV
HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTTIA
