ID B3RF71_SORAR Unreviewed; 229 AA.
AC B3RF71;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha2 {ECO:0000256|ARBA:ARBA00044096};
DE EC=3.1.1.47 {ECO:0000256|ARBA:ARBA00013201};
DE AltName: Full=PAF acetylhydrolase 30 kDa subunit {ECO:0000256|ARBA:ARBA00044363};
DE AltName: Full=PAF-AH subunit beta {ECO:0000256|ARBA:ARBA00044225};
GN Name=PAFAH1B2 {ECO:0000313|EMBL:ACE77697.1};
OS Sorex araneus (Eurasian common shrew) (European shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Sorex.
OX NCBI_TaxID=42254 {ECO:0000313|EMBL:ACE77697.1};
RN [1] {ECO:0000313|EMBL:ACE77697.1}
RP NUCLEOTIDE SEQUENCE.
RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA Tsipouri V., Young A., Green E.D.;
RT "NISC Comparative Sequencing Initiative.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + H2O = 1-O-
CC hexadecyl-sn-glycero-3-phosphate + acetate + H(+);
CC Xref=Rhea:RHEA:41704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:77580, ChEBI:CHEBI:78385;
CC Evidence={ECO:0000256|ARBA:ARBA00035804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705;
CC Evidence={ECO:0000256|ARBA:ARBA00035804};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000256|ARBA:ARBA00023721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000256|ARBA:ARBA00023721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphoethanolamine + H2O
CC = 1-O-hexadecyl-sn-glycero-3-phosphoethanolamine + acetate + H(+);
CC Xref=Rhea:RHEA:41708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:78387, ChEBI:CHEBI:78390;
CC Evidence={ECO:0000256|ARBA:ARBA00043786};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41709;
CC Evidence={ECO:0000256|ARBA:ARBA00043786};
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 Evidence={ECO:0000256|ARBA:ARBA00023737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000256|ARBA:ARBA00023737};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. Platelet-
CC activating factor acetylhydrolase IB beta/gamma subunits subfamily.
CC {ECO:0000256|ARBA:ARBA00038184}.
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; DP000785; ACE77697.1; -; Genomic_DNA.
DR RefSeq; XP_004604768.1; XM_004604711.1.
DR AlphaFoldDB; B3RF71; -.
DR KEGG; sara:101543285; -.
DR HOGENOM; CLU_051989_2_0_1; -.
DR OrthoDB; 4162633at2759; -.
DR TreeFam; TF323955; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd01820; PAF_acetylesterase_like; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR11852; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR PANTHER; PTHR11852:SF1; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT ALPHA2; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|EMBL:ACE77697.1}.
FT DOMAIN 44..203
FT /note="SGNH hydrolase-type esterase"
FT /evidence="ECO:0000259|Pfam:PF13472"
SQ SEQUENCE 229 AA; 25623 MW; 4C698CA01CA1BD7B CRC64;
MSQGDTNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR
ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA
IVQLINTRQP QAKIIVLGLL PRGEKPNPLR QKNARVNQLL KVSLPKLANV QLLDTDGGFV
HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTIIA
//
