ID L5KRR3_PTEAL Unreviewed; 1165 AA.
AC L5KRR3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=PAL_GLEAN10011503 {ECO:0000313|EMBL:ELK13468.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13468.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701}.
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DR EMBL; KB030625; ELK13468.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KRR3; -.
DR STRING; 9402.L5KRR3; -.
DR eggNOG; KOG2088; Eukaryota.
DR InParanoid; L5KRR3; -.
DR Proteomes; UP000010552; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 505..607
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 972..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1165 AA; 127621 MW; 605500145D80C2F5 CRC64;
MPGIVVFRRR WSVGSDDLVL PAIFLFLLHT TCSQQAVPET YKPLGDSHVE PRDLTWPPPD
LSPALGKAAA AVSPLLAAGL PALASCPWPS VSSEALSARF VILSVVLFGL VYNPHEACSL
NLVDHGRGYL GILLSCMIAE MAIIWLSMRG GILYTEPRES MQYVLYVRLA ILVIEFIYAI
VGIVWLTQYY TSCNDLTAKN VTLGMVVCNW VVILSVCITV LCVFDPTGRT FVKLRATKRR
QRNLRTYNLR HRLEEGQATS WSRRLKVFLC CTRTKDSQSD AYSEIAYLFA EFFRDLDIVP
SDIIAGLVLL RQRQRAKRNA VLDEANNDIL AFLSGMPVTR NTKYLDLKNS QEMLRYKEVC
YYMLFALAAY GWPMYLMRKP ACGLCQLARS CSCCLCPTRP RFAPGVTIEE DNCCGCNAIA
IRRHFLDENM TAVDIVYTSC HDAVYETPFY VAVDHDKKKV VISIRGTLSP KPRPSPVPSP
HKDALTDLTG DAERLPVEGH HGTWLGHKGM VLSAEYIKKK LEQEMVLSQA FGRDLGRGTK
HYGLIVVGHS LGAGTAAILS FLLRPQYPTL KCFAYSPPGG LLSEDAMEYS KEFVTAVVLG
KDLVPRQVSV APSLHCPSLG WSSLLRASPG LYVALTQTPT HPKDPRAPLC ALRIGLSQLE
GFRRQLLDVL QRSTKPKWRI IVGATKCIPK SELPEEVEVA ALASTRLWTH PSDLTIALSA
STPLYPPGRI IHVVHNHPAE QCCCCEQEEP TYFAIWGDNK AFNEVIISPA MLHEHLPYVV
MEGLNKVLEN YNKGKTALLS AAKVMVSPTE VDLTPELIFQ QQPLPTGPSM PAGLALELPT
ADHRNSSVRS KSQSEMSLEG FSEGQLLSPV AAAAAARQDP VELLLLSTQE RLAAELQARR
APLATMESLS DTESLYSFDS RRSSGFRSIR GSPSLHAVLE RDEGHLFYID PAIPEENPSL
SSRTELLAAD SLSKHSQDTQ PLEAALGSGG ATPERPPSAA ATDQEEEGGG GVAPRGELAL
HNGRLGDSPS PQVLEFAEFI DSLFNLDSKS SSLQDLYCMV VPESPTSDYA EGPKSPSQQE
ILLRAQFEPN LVPKPPRRFA GSADPSSGIS LSPSFPLSSS GELMDLTPTG LSSQECLAVD
KIRTSTPTGH GASPTKQDDL VISAR
//
