ID PA1B2_MOUSE Reviewed; 229 AA. AC Q61206; Q6PKE6; Q7TNP3; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 25-MAY-2022, entry version 163. 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; GN Name=Pafah1b2 {ECO:0000312|MGI:MGI:108415}; Synonyms=Pafahb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; RX PubMed=8954729; DOI=10.1006/dbio.1996.0330; RA Albrecht U., Abu-Issa R., Raetz B., Hattori M., Aoki J., Arai H., Inoue K., RA Eichele G.; RT "Platelet-activating factor acetylhydrolase expression and activity suggest RT a link between neuronal migration and platelet-activating factor."; RL Dev. Biol. 180:579-593(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryo, and Mammary tumor; 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 [4] RP PROTEIN SEQUENCE OF 61-79 AND 134-142, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. RN [5] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=12775763; DOI=10.1073/pnas.1236145100; RA Yan W., Assadi A.H., Wynshaw-Boris A., Eichele G., Matzuk M.M., Clark G.D.; RT "Previously uncharacterized roles of platelet-activating factor RT acetylhydrolase 1b complex in mouse spermatogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7189-7194(2003). RN [6] RP INTERACTION WITH VLDLR. RX PubMed=17330141; DOI=10.1371/journal.pone.0000252; RA Zhang G., Assadi A.H., McNeil R.S., Beffert U., Wynshaw-Boris A., Herz J., RA Clark G.D., D'Arcangelo G.; RT "The Pafah1b complex interacts with the reelin receptor VLDLR."; RL PLoS ONE 2:e252-e252(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND THR-220, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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. The CC activity and substrate specificity of PAF-AH (I) are affected by its CC subunit composition. The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 CC homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3- CC phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2- CC 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 (PubMed:12775763). {ECO:0000250|UniProtKB:P68401, CC ECO:0000269|PubMed:12775763}. 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:0000250|UniProtKB:P68401}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; CC Evidence={ECO:0000250|UniProtKB:P68401}; 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:0000250|UniProtKB:P68401}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; CC Evidence={ECO:0000250|UniProtKB:P68401}; 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). Component of the cytosolic (PAF-AH (I)) heterotetrameric CC enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2 (alpha2) and CC PAFAH1B3 (alpha1) subunits. The catalytic activity of the enzyme CC 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 (homodimer form) with PAFAH1B1 (homodimer form); PAFAH1B2 CC competes with NDEL1 for PAFAH1B1 binding (By similarity). Interacts CC with VLDLR; this interaction may modulate the Reelin pathway CC (PubMed:17330141). {ECO:0000250|UniProtKB:P68401, CC ECO:0000250|UniProtKB:P68402, ECO:0000269|PubMed:17330141}. CC -!- INTERACTION: CC Q61206; O35685: Nudc; NbExp=2; IntAct=EBI-7445518, EBI-911192; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DEVELOPMENTAL STAGE: Expressed already by the time of neurulation. By CC 10.5 dpc, expression is abundant in the developing central and CC peripheral nervous systems. Major sites include the neuroepithelium of CC the fore-, mid-, and hindbrain, the spinal cord, the dorsal root, and CC cranial ganglia. CC -!- DISRUPTION PHENOTYPE: Knockout mice which are homozygous for the CC PAFAH1B2 gene appear developmentally normal, and are born at the CC expected Mendelian rate (PubMed:12775763). Females bred normally, CC whereas male are infertile, and spermatogenesis is disrupted at mid- or CC late pachytene stages of meiosis or early spermiogenesis CC (PubMed:12775763). Double mutant female mice which are homozygous for CC PAFAH1B2 and PAFAH1B3 are grossly normal and fertile, whereas double- CC mutant males are infertile. Double mutan mice manifest an earlier CC disturbance of spermatogenesis with an onset at preleptotene or CC leptotene stages of meiosis (PubMed:12775763). CC {ECO:0000269|PubMed:12775763}. 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}. 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; U57747; AAC52997.1; -; mRNA. DR EMBL; AK153424; BAE31983.1; -; mRNA. DR EMBL; BC002037; AAH02037.1; -; mRNA. DR EMBL; BC056211; AAH56211.1; -; mRNA. DR CCDS; CCDS23139.1; -. DR RefSeq; NP_032801.2; NM_008775.3. DR RefSeq; XP_006510147.1; XM_006510084.3. DR RefSeq; XP_006510148.1; XM_006510085.1. DR RefSeq; XP_017168698.1; XM_017313209.1. DR AlphaFoldDB; Q61206; -. DR SMR; Q61206; -. DR BioGRID; 202016; 4. DR IntAct; Q61206; 3. DR MINT; Q61206; -. DR STRING; 10090.ENSMUSP00000127851; -. DR BindingDB; Q61206; -. DR ChEMBL; CHEMBL3259481; -. DR iPTMnet; Q61206; -. DR PhosphoSitePlus; Q61206; -. DR SwissPalm; Q61206; -. DR REPRODUCTION-2DPAGE; IPI00118821; -. DR REPRODUCTION-2DPAGE; Q61206; -. DR UCD-2DPAGE; Q61206; -. DR EPD; Q61206; -. DR jPOST; Q61206; -. DR MaxQB; Q61206; -. DR PaxDb; Q61206; -. DR PeptideAtlas; Q61206; -. DR PRIDE; Q61206; -. DR ProteomicsDB; 294315; -. DR Antibodypedia; 32310; 248 antibodies from 27 providers. DR DNASU; 18475; -. DR Ensembl; ENSMUST00000172450; ENSMUSP00000127851; ENSMUSG00000003131. DR Ensembl; ENSMUST00000214179; ENSMUSP00000149819; ENSMUSG00000003131. DR GeneID; 18475; -. DR KEGG; mmu:18475; -. DR UCSC; uc009pgx.1; mouse. DR CTD; 5049; -. DR MGI; MGI:108415; Pafah1b2. DR VEuPathDB; HostDB:ENSMUSG00000003131; -. DR eggNOG; KOG1388; Eukaryota. DR GeneTree; ENSGT00950000183199; -. DR HOGENOM; CLU_051989_2_0_1; -. DR InParanoid; Q61206; -. DR OMA; QQCEIWR; -. DR OrthoDB; 1604899at2759; -. DR PhylomeDB; Q61206; -. DR TreeFam; TF323955; -. DR BRENDA; 3.1.1.47; 3474. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR BioGRID-ORCS; 18475; 4 hits in 75 CRISPR screens. DR ChiTaRS; Pafah1b2; mouse. DR PRO; PR:Q61206; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q61206; protein. DR Bgee; ENSMUSG00000003131; Expressed in midbrain and 350 other tissues. DR ExpressionAtlas; Q61206; baseline and differential. DR Genevisible; Q61206; MM. DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; ISO:MGI. 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; ISO:MGI. DR GO; GO:0007420; P:brain development; IBA:GO_Central. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI. DR GO; GO:0007283; P:spermatogenesis; IMP: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_0000058152" 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:0007744|PubMed:21183079" FT MOD_RES 220 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT CONFLICT 129..130 FT /note="QP -> HA (in Ref. 1; AAC52997)" FT /evidence="ECO:0000305" FT CONFLICT 188 FT /note="C -> W (in Ref. 3; AAH56211)" FT /evidence="ECO:0000305" FT CONFLICT 222 FT /note="E -> G (in Ref. 1; AAC52997)" FT /evidence="ECO:0000305" 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 //