PA1B2_CHICK
ID PA1B2_CHICK Reviewed; 229 AA.
AC Q5ZMS2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha2 {ECO:0000250|UniProtKB:P68401};
DE EC=3.1.1.47 {ECO:0000250|UniProtKB:P68401};
DE AltName: Full=PAF acetylhydrolase 30 kDa subunit;
DE Short=PAF-AH 30 kDa subunit;
DE AltName: Full=PAF-AH subunit beta;
DE AltName: Full=PAFAH subunit beta;
GN Name=PAFAH1B2; Synonyms=PAFAHB; ORFNames=RCJMB04_1f10;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Alpha2 catalytic subunit of the cytosolic type I platelet-
CC activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric
CC enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2
CC position of PAF and its analogs and modulates the action of PAF.
CC {ECO:0000250|UniProtKB:P68401}.
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:0000250|UniProtKB:P68401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000250|UniProtKB:P68401};
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:0000250|UniProtKB:P68401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000250|UniProtKB:P68401};
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:0000250|UniProtKB:P68401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705;
CC Evidence={ECO:0000250|UniProtKB:P68401};
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:0000250|UniProtKB:P68401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41709;
CC Evidence={ECO:0000250|UniProtKB:P68401};
CC -!- SUBUNIT: Forms a catalytic dimer which is either homodimer
CC (alpha2/alpha2 homodimer) or heterodimer with PAFAH1B3 (alpha2/alpha1
CC heterodimer). Component of the cytosolic (PAF-AH (I)) heterotetrameric
CC enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2 (alpha2) and
CC PAFAH1B3 (alpha1) subunits. The catalytic activity of the enzyme
CC resides in the alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits,
CC whereas the beta subunit (PAFAH1B1) has regulatory activity. Trimer
CC formation is not essential for the catalytic activity.
CC {ECO:0000250|UniProtKB:P68401}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Originally the subunits of the type I platelet-
CC activating factor (PAF) acetylhydrolase was named alpha (PAFAH1B1),
CC beta (PAFAH1B2) and gamma (PAFAH1B3) (By similarity). Now these
CC subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and
CC alpha1 (PAFAH1B3) respectively (By similarity).
CC {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P68402,
CC ECO:0000250|UniProtKB:Q15102, ECO:0000250|UniProtKB:Q29460}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. Platelet-
CC activating factor acetylhydrolase IB beta/gamma subunits subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ719312; CAG30971.1; -; mRNA.
DR AlphaFoldDB; Q5ZMS2; -.
DR SMR; Q5ZMS2; -.
DR STRING; 9031.ENSGALP00000042949; -.
DR PaxDb; Q5ZMS2; -.
DR VEuPathDB; HostDB:geneid_419765; -.
DR eggNOG; KOG1388; Eukaryota.
DR InParanoid; Q5ZMS2; -.
DR PhylomeDB; Q5ZMS2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..229
FT /note="Platelet-activating factor acetylhydrolase IB
FT subunit alpha2"
FT /id="PRO_0000252684"
FT ACT_SITE 48
FT /evidence="ECO:0000250"
FT ACT_SITE 193
FT /evidence="ECO:0000250"
FT ACT_SITE 196
FT /evidence="ECO:0000250"
SQ SEQUENCE 229 AA; 25567 MW; 27AEDEAA33C4B130 CRC64;
MSHGDSNPAA VPHAADDIQG DDRWMSQHNR FVSDCKDKEP DVLFVGDSMV QLLQQYEIWR
ELFSPLHALN FWIGGDTTGH VLWRLKNGEL ENIKPKVIVV WVGTNNYGNT AEEVAGGIEA
IVRLINTQQP QAKVIVLGLL PRGEKPNPLR QKNAKVNHLL KASLPKLPNV QLLDVDAGFV
HSDGTISYHD MFDFLHLTGG AYAKICKPLH ELIMQLLEET PEEKRAALA
