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Database: UniProt
Entry: A0A2J7Q253_9NEOP
LinkDB: A0A2J7Q253_9NEOP
Original site: A0A2J7Q253_9NEOP 
ID   A0A2J7Q253_9NEOP        Unreviewed;       199 AA.
AC   A0A2J7Q253;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE            EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN   ORFNames=B7P43_G07100 {ECO:0000313|EMBL:PNF22657.1};
OS   Cryptotermes secundus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX   NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF22657.1, ECO:0000313|Proteomes:UP000235965};
RN   [1] {ECO:0000313|EMBL:PNF22657.1, ECO:0000313|Proteomes:UP000235965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole body {ECO:0000313|EMBL:PNF22657.1};
RA   Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA   Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA   Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA   Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA   Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA   Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA   Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA   Bornberg-Bauer E.;
RT   "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL   Submitted (DEC-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNF22657.1}.
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DR   EMBL; NEVH01019373; PNF22657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J7Q253; -.
DR   Proteomes; UP000235965; 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:SF8; DIACYLGLYCEROL LIPASE-ALPHA; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235965};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          26..98
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
SQ   SEQUENCE   199 AA;  21692 MW;  18DBBAA6E681032E CRC64;
     MVQAAEYIRD KLEEEAILAR AFSHSEERGT QDYGLVLVGH SLGAGTASIL AILLRQDYPT
     LQCFAYSPPG GSLSMPAVEY TKSFITSVVV GKDVVPRIGL HQLESLRADL INTIKRSKDP
     KWKTIVCSVV CCGCASLPTS AAELKSEDSQ MAEYLKAKEV AREVAVHPSD SSIALTLHQP
     LYPPGRIIHI VRHHPTKGE
//
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