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 17-JUN-2020, entry version 155. DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit beta; DE EC=3.1.1.47; 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; 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 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: Inactivates PAF by removing the acetyl group at the sn-2 CC position. This is a catalytic subunit. 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 -!- SUBUNIT: Cytosolic PAF-AH IB is formed of three subunits of 45 kDa CC (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity of CC the enzyme resides in the beta and gamma subunits, whereas the alpha CC subunit has regulatory activity. Trimer formation is not essential for CC the catalytic activity. 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 -!- 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 SMR; Q61206; -. DR BioGRID; 202016; 3. DR IntAct; Q61206; 4. 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 Antibodypedia; 32310; 236 antibodies. 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 eggNOG; ENOG410IMK6; Eukaryota. DR eggNOG; ENOG410XPWQ; LUCA. DR GeneTree; ENSGT00950000183199; -. DR HOGENOM; CLU_051989_2_0_1; -. DR InParanoid; Q61206; -. DR KO; K16795; -. 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; 2 hits in 12 CRISPR screens. DR ChiTaRS; Pafah1b2; mouse. DR PRO; PR:Q61206; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q61206; protein. DR Bgee; ENSMUSG00000003131; Expressed in embryo and 330 other tissues. DR ExpressionAtlas; Q61206; baseline and differential. DR Genevisible; Q61206; MM. 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; IEA:UniProtKB-EC. 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: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:MGI. 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 beta" 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:0000244|PubMed:21183079" FT MOD_RES 220 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|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 //