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 15-JUL-1999 (Rel. 38, Last annotation update) DE PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB BETA SUBUNIT DE (EC 3.1.1.47) (PAF ACETYLHYDROLASE 30 KD SUBUNIT) (PAF-AH 30 KD DE SUBUNIT) (PAF-AH BETA SUBUNIT). GN PAFAH1B2 OR PAFAHB. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; OC Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BALB/C; RX MEDLINE; 97115706. 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 KD CC (ALPHA), 30 KD (BETA) AND 29 KD (GAMMA). THE CATALYTIC ACTIVITY OF CC 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 -!- SIMILARITY: BELONGS TO THE PLATELET-ACTIVATING FACTOR CC ACETYLHYDROLASE IB BETA/GAMMA SUBUNITS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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. 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; A105A550 CRC32; MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA IVQLINTRHA QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDIDGGFV HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PGEKQTTIA //