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 28-MAR-2018, entry version 142. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Inoue K., Eichele G.; RT "Platelet-activating factor acetylhydrolase expression and activity RT suggest a link between neuronal migration and platelet-activating RT 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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, RC Pancreas, 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 RT 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: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + CC H(2)O = 1-alkyl-sn-glycero-3-phosphocholine + acetate. 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 CC of the enzyme resides in the beta and gamma subunits, whereas the CC alpha subunit has regulatory activity. Trimer formation is not CC essential for the catalytic activity. CC -!- INTERACTION: CC O35685:Nudc; NbExp=2; IntAct=EBI-7445518, EBI-911192; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DEVELOPMENTAL STAGE: Expressed already by the time of neurulation. CC By E10.5, expression is abundant in the developing central and CC peripheral nervous systems. Major sites include the CC neuroepithelium of the fore-, mid-, and hindbrain, the spinal CC cord, the dorsal root, and cranial ganglia. CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. CC Platelet-activating factor acetylhydrolase IB beta/gamma subunits CC subfamily. {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 UniGene; Mm.200859; -. DR ProteinModelPortal; Q61206; -. 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 REPRODUCTION-2DPAGE; IPI00118821; -. DR REPRODUCTION-2DPAGE; Q61206; -. DR UCD-2DPAGE; Q61206; -. DR EPD; Q61206; -. DR MaxQB; Q61206; -. DR PaxDb; Q61206; -. DR PeptideAtlas; Q61206; -. DR PRIDE; Q61206; -. DR Ensembl; ENSMUST00000172450; ENSMUSP00000127851; ENSMUSG00000003131. DR Ensembl; ENSMUST00000214179; ENSMUSP00000149819; ENSMUSG00000003131. DR GeneID; 18475; -. DR UCSC; uc009pgx.1; mouse. DR CTD; 5049; -. DR MGI; MGI:108415; Pafah1b2. DR eggNOG; ENOG410IMK6; Eukaryota. DR eggNOG; ENOG410XPWQ; LUCA. DR GeneTree; ENSGT00390000016520; -. DR HOGENOM; HOG000232143; -. DR HOVERGEN; HBG053477; -. DR InParanoid; Q61206; -. DR OMA; RGQQPNK; -. DR OrthoDB; EOG091G0OII; -. 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 PRO; PR:Q61206; -. DR Proteomes; UP000000589; Chromosome 9. DR Bgee; ENSMUSG00000003131; -. 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:0047179; F:platelet-activating factor acetyltransferase activity; IBA:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl. 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; Complete proteome; Cytoplasm; Direct protein sequencing; KW Hydrolase; Lipid degradation; Lipid metabolism; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P68402}. FT CHAIN 2 229 Platelet-activating factor FT acetylhydrolase IB subunit beta. FT /FTId=PRO_0000058152. FT ACT_SITE 48 48 {ECO:0000250}. FT ACT_SITE 193 193 {ECO:0000250}. FT ACT_SITE 196 196 {ECO:0000250}. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000250|UniProtKB:P68402}. FT MOD_RES 2 2 Phosphoserine. FT {ECO:0000250|UniProtKB:P68402}. FT MOD_RES 64 64 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 220 220 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT CONFLICT 129 130 QP -> HA (in Ref. 1; AAC52997). FT {ECO:0000305}. FT CONFLICT 188 188 C -> W (in Ref. 3; AAH56211). FT {ECO:0000305}. FT CONFLICT 222 222 E -> G (in Ref. 1; AAC52997). FT {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 //