ID A0A026WU22_OOCBI Unreviewed; 911 AA.
AC A0A026WU22;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=X777_00326 {ECO:0000313|EMBL:EZA59483.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA59483.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA59483.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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; KK107105; EZA59483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026WU22; -.
DR EnsemblMetazoa; XM_026973887.1; XP_026829688.1; LOC105275272.
DR OMA; YCMVAPE; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd00519; Lipase_3; 1.
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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 407..543
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 694..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 101701 MW; 52ADBA0136A51EEA CRC64;
MPSLIAFGRR WRVGSDDLLL PGVVLFWTHL FELTVLGVLL GILEWNRSVT CILLLWEYVI
GYEGLFVACM AVEFSICFLA TRGSILDTTA RAPMQYILYI RLFLVLVEIG WLCAGVTWLA
RYYQTCPVDQ AKDVMLGLVI SNWCLLAFLM ATIWCTYDAA GRSWVKMKKY QRSMREAESR
AARLHYKRSG SRNRNWRQRK VIRAYQDSWD NRCRLLFCCL GNSDRNRNSF ADLARLLSDF
FRDLDVVPSD VVAGLVLLRK FQKIERELIV KQRKNDTYEF LSGVPVTPRT KFLSMTEDGD
LGHFQLAIHY MHFALAAYGW PMFLVSSSTE LCQLCTRLQC CCCCFPCGGH REDETTIVED
NCCRCNYAAL SRMLDLGEIE VVYATFHVDV GETPFFVALD YTKRKVVVSI RGTLSMKDVL
TDLNAEGEVL PLSPPREDWL GHKGMVQAAE YIRKKLQEED IIARALAKDP SRGTHQFGLT
LVGHSLGAGT AAILAILLKQ DYPDLICFSF GPPGGLLSMP AQQYSQEFIT SVVVGKDVVP
RIGLRQMESL RADLINAIKR SVDPKWKTIA CSVMCCGCGW TPTSAANLEA GGCIGEYQRD
KDRARAQTIV PSDSSIALTL HRPLYPPGRI IHVVRHHPNK GEQMLSKREP VYQALWAGPC
DFDEVLISPV MIQDHMPDNM LRALNKVVTT LGPAKPQRLT SGHASSTEAS SETAREHHMI
EVQELEIQEQ EMRALLSPSS PSRYQLGNLA GTPPHRLCLE TSFTSLQSPT DIPQAGRELS
VDSRGIPWEY VSLASELLHT PRPEDSKPPS RWDDPTRTAP LATPETLSEA STSSSPPSPV
PAPRPMRRTP KIPGNLSTAA DDLKNNLHYA MLSAKNYFLR TKGEHATGSN NGSSSGNSEA
SYESAKSLAT A
//
