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Database: UniProt
Entry: A0A091EE65_FUKDA
LinkDB: A0A091EE65_FUKDA
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ID   A0A091EE65_FUKDA        Unreviewed;       231 AA.
AC   A0A091EE65;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha1 {ECO:0000256|ARBA:ARBA00044095};
DE            EC=3.1.1.47 {ECO:0000256|ARBA:ARBA00013201};
DE   AltName: Full=PAF acetylhydrolase 29 kDa subunit {ECO:0000256|ARBA:ARBA00044307};
DE   AltName: Full=PAF-AH subunit gamma {ECO:0000256|ARBA:ARBA00044294};
GN   ORFNames=H920_04987 {ECO:0000313|EMBL:KFO33641.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO33641.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO33641.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO33641.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) 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=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}.
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DR   EMBL; KN122065; KFO33641.1; -; Genomic_DNA.
DR   RefSeq; XP_010621619.1; XM_010623317.2.
DR   RefSeq; XP_010621620.1; XM_010623318.2.
DR   AlphaFoldDB; A0A091EE65; -.
DR   STRING; 885580.ENSFDAP00000021156; -.
DR   Ensembl; ENSFDAT00000011242; ENSFDAP00000021156; ENSFDAG00000007905.
DR   GeneID; 104861733; -.
DR   CTD; 5050; -.
DR   eggNOG; KOG1388; Eukaryota.
DR   OMA; HHRFIAD; -.
DR   OrthoDB; 4162633at2759; -.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
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:SF2; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT ALPHA1; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Hydrolase {ECO:0000313|EMBL:KFO33641.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT   DOMAIN          43..201
FT                   /note="SGNH hydrolase-type esterase"
FT                   /evidence="ECO:0000259|Pfam:PF13472"
SQ   SEQUENCE   231 AA;  25829 MW;  5FD5EB28E754ECCA CRC64;
     MSEGDNPASK PTSVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ LMHQCEIWRE
     LFSPLHALNF GIGGDSTQHV LWRLENGELE HIRPKIVVVW VGTNNHGHTA EQVTGGIKAI
     VELVNQRQPQ ARVVVMGLLP RGQHPNPLRE KNRLVNELVR AALAGHPRAH FLDADPGFVH
     SDGTISHHDM YDYLHLTRLG YTPVCRALHS LLLRLLAQDQ GQSVPLPEPT P
//
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