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-DEC-1998 (REL. 37, 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; VERTEBRATA; MAMMALIA; EUTHERIA; OC 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 IS FORMED OF THREE SUBUNITS OF 45 KD CC (ALPHA), 30 KD (BETA) AND 29 KD (GAMMA). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: TO THE GAMMA SUBUNIT. 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; G1373363; -. DR MGD; MGI:108415; PAFAH1B2. DR HSSP; Q29460; 1WAB. 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 //