ID H3D2L7_TETNG Unreviewed; 230 AA.
AC H3D2L7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=1-alkyl-2-acetylglycerophosphocholine esterase {ECO:0000256|ARBA:ARBA00013201};
DE EC=3.1.1.47 {ECO:0000256|ARBA:ARBA00013201};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000014755.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000014755.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- 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 AlphaFoldDB; H3D2L7; -.
DR STRING; 99883.ENSTNIP00000014755; -.
DR Ensembl; ENSTNIT00000014955.1; ENSTNIP00000014755.1; ENSTNIG00000011800.1.
DR GeneTree; ENSGT00950000183199; -.
DR HOGENOM; CLU_051989_2_0_1; -.
DR InParanoid; H3D2L7; -.
DR OMA; EAWNQYF; -.
DR TreeFam; TF323955; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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:SF0; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT BETA HOMOLOG; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007303}.
FT DOMAIN 44..204
FT /note="SGNH hydrolase-type esterase"
FT /evidence="ECO:0000259|Pfam:PF13472"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 230 AA; 25686 MW; 2ACAF4DBDE4C861F CRC64;
MSGDEGNPAA VPQPVEETQG DGRWISQHTR FVQECKDAEP DVLFVGDSMV QLMQQFEVWR
ELFSPLHALS FGIGGDTTCN VLWRLQNGEL ENIRPKVVVL WVGTNNYQHT AEQVAGGILA
IAELLRSRLP KAKIIVLSLL PRGERPNPLR EKNAAVNGLV RSWLPRLGQQ AQFLDVSKGF
VHSDGTIVPQ DMFDFLHLTS LGYRSIAKPL SDLLLQILEE TPEERRASLV
//
