ID PA1B_MOUSE STANDARD; PRT; 229 AA. AC Q61206; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Platelet-activating factor acetylhydrolase IB beta subunit DE (EC 3.1.1.47) (PAF acetylhydrolase 30 kDa subunit) (PAF-AH 30 kDa DE subunit) (PAF-AH beta subunit) (PAFAH beta subunit). GN PAFAH1B2 OR PAFAHB. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BALB/c; RX MEDLINE=97115706; PubMed=8954729; 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). CC -!- FUNCTION: INACTIVATES PAF BY REMOVING THE ACETYL GROUP AT THE SN-2 CC POSITION. THIS IS A CATALYTIC SUBUNIT. CC -!- CATALYTIC ACTIVITY: 2-acetyl-1-alkyl-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 -!- SUBCELLULAR LOCATION: Cytoplasmic. 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 PLATELET-ACTIVATING FACTOR CC ACETYLHYDROLASE IB BETA/GAMMA SUBUNITS FAMILY. 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; -. DR HSSP; Q29460; 1WAB. DR MGD; MGI:108415; Pafah1b2. DR InterPro; IPR001087; Lipase_GDSL. DR Pfam; PF00657; Lipase_GDSL; 1. KW Hydrolase; Lipid degradation. FT ACT_SITE 48 48 BY SIMILARITY. FT ACT_SITE 193 193 BY SIMILARITY. FT ACT_SITE 196 196 BY SIMILARITY. SQ SEQUENCE 229 AA; 25492 MW; 5370D4BE75E58D72 CRC64; MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA IVQLINTRHA QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDIDGGFV HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PGEKQTTIA //