ID A0A0L7QW72_9HYME Unreviewed; 718 AA.
AC A0A0L7QW72;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=WH47_02512 {ECO:0000313|EMBL:KOC62809.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC62809.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC62809.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC62809.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:ARBA00024531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33276;
CC Evidence={ECO:0000256|ARBA:ARBA00024531};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KQ414716; KOC62809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7QW72; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR45792; DIACYLGLYCEROL LIPASE HOMOLOG-RELATED; 1.
DR PANTHER; PTHR45792:SF2; DIACYLGLYCEROL LIPASE-BETA; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 417..549
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 718 AA; 81977 MW; 1ECC22D4CB2A9594 CRC64;
MPAIKLFGRK WLAATDDLVY PGLFEIFIRA VWLILITTAC IRYYAYTWRC QLGGELVRVY
LIGELVFLVT SILFILIIAR QSAKGTIMEA RDRKYVEPLL TIKILLLLPE IAWNVLGCLW
MFGPNVECGY EHYTVTVVQA LVFFDWILIG LTIFGLALIF DPLGSLGDKQ LESTAEHGKI
SSIWFRRFRF LWWMRKDESA NEIFQHAAGL LSALFRGTDL VPSDVMAGCI LLRIRQKRET
HELRLLNLLI RPVYTPSLLS ALFRGTDLVP SDVMAGCILL RIRQKRETHE LRLLNLLIRP
VYTPNASIIF KDTPSWMSLE NAVHYMKLSI ACYGWLFVLY QHMCTGCCHI MQNLTCCACF
RRKRISISGD NCCYCYLAGV KYLSDISTDN ILFASFKNHL CEIPFCVIND QETNNIVIVI
RGSLSLRDLL TDIAADSEVF PCDDLPPGSQ AHRGMITAAK SILKQLDDNQ ILERAFSTYT
QHNLVITGHS LGAGIGILLA LLLRPRYPNL KVYAFATPGG LLSREAAKVT EEFVLTIGVG
DDLVMRLSVD STENLRTSLL LTLRACRLPK YRVVLNGLGY ILFGIPERDL SKTWTNCNVI
TTATGESPLL NERDINRIEE NKIYEQDITK RRFSRVKLYV GGKILHIVKC KPERSEEKSN
KKQNVKEKKY EMRWAQPEEF TELMVVPRML LDHLPENIEK ALSTLLEQQN KIPYHFDP
//
