ID A0A182QAQ8_9DIPT Unreviewed; 308 AA.
AC A0A182QAQ8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=sn-1-specific diacylglycerol lipase ABHD11 {ECO:0000256|ARBA:ARBA00044064};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 11 {ECO:0000256|ARBA:ARBA00042703};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF006426-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF006426-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF006426-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoylglycerol + H2O = decanoate + decanoylglycerol +
CC H(+); Xref=Rhea:RHEA:48596, ChEBI:CHEBI:11152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:90605;
CC Evidence={ECO:0000256|ARBA:ARBA00043771};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycerol + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-glycerol +
CC H(+) + octadecanoate; Xref=Rhea:RHEA:77107, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:77129,
CC ChEBI:CHEBI:186738; Evidence={ECO:0000256|ARBA:ARBA00043706};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + H2O = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:38507, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:52392,
CC ChEBI:CHEBI:75728; Evidence={ECO:0000256|ARBA:ARBA00043768};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H2O = 2-(9Z-
CC octadecenoyl)-glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:77103,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:73990, ChEBI:CHEBI:75468;
CC Evidence={ECO:0000256|ARBA:ARBA00043740};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty
CC acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:28868; EC=3.1.1.116;
CC Evidence={ECO:0000256|ARBA:ARBA00043667};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,3-diacyl-sn-glycerol + H2O = a 1-acyl-sn-glycerol + a
CC fatty acid + H(+); Xref=Rhea:RHEA:38503, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64683,
CC ChEBI:CHEBI:77272; Evidence={ECO:0000256|ARBA:ARBA00043742};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00008645}.
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DR EMBL; AXCN02000790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182QAQ8; -.
DR STRING; 69004.A0A182QAQ8; -.
DR ESTHER; anoga-Q7PVF9; ABHD11-Acetyl_transferase.
DR EnsemblMetazoa; AFAF006426-RA; AFAF006426-PA; AFAF006426.
DR VEuPathDB; VectorBase:AFAF006426; -.
DR OrthoDB; 1123232at2759; -.
DR Proteomes; UP000075886; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR PANTHER; PTHR46118; PROTEIN ABHD11; 1.
DR PANTHER; PTHR46118:SF4; PROTEIN ABHD11; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 50..294
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 308 AA; 34293 MW; 19FBA99FD83C7B59 CRC64;
MYPSTINPAS MILYSSIRTL HLGATCNARS VPVPLSFTRY ENNVSSSNAP PVLVLHGLFG
SKSNWNSLAK AFHKNTKPVR KIYAIDARNH GDSPHTDEHS YDHMVEDLVE LYKTLGIQQA
SIIGHSMGGR AMMLLALKYP ELVEKAIIVD ISPSPGLGTS NTNIPLFLQS MKMIRISPDA
TIHQARKIAD EQLARIVSEK PLRDFLITNL VKGEKMGGEF RWRINLQSLE RNFNTGVAQF
PTLTGVKFDG PTLFIAGGRS DYVQSKDVPL IKTLFPNSEI TYVKDAGHWV HSEKSTEFSK
LVLNFLNE
//
