ID A0A068S4G8_9FUNG Unreviewed; 1035 AA.
AC A0A068S4G8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=LCOR_07201.1 {ECO:0000313|EMBL:CDH56116.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH56116.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH56116.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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:CDH56116.1}.
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DR EMBL; CBTN010000035; CDH56116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S4G8; -.
DR VEuPathDB; FungiDB:LCOR_07201.1; -.
DR OrthoDB; 1341793at2759; -.
DR Proteomes; UP000027586; 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; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR45792; DIACYLGLYCEROL LIPASE HOMOLOG-RELATED; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR PROSITE; PS50004; C2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 71..180
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 115994 MW; EE4CDAAEF2F40A72 CRC64;
MVATSLATPP PARSSTTVAH DHHHHHHHHV TNPSSPRPVP QHAPDSKSHS TLPSRRLSLP
DMRELRTEWA RREALQINAL PPGKLQIDLL NVRSDVKVKR PFVRLRMGPQ RYFSSCSKAS
HGDWNEGFLF TISFHNQLFD TIELDLFDRR NGWRSKTRHI GKAKLRLLQL NNRDDVFLTF
IPMYEYHTRR YLPAHIQLPH NFLKSHIPRF RTQEQASYRE QHPSHRKHSM TPLIGSVQVR
VRYSYQKPPD MHDTLSPVYK DADTHSIVSS FMDRSTLASS QSGKSRNSGN SMVTLSSVGT
HNTTMSSSGE TTTSAGRVHG SSSSSSSSSS RGSNSSDDDQ HDNDTTEKSS SEMEDFHDAV
EPNLVLVDDP SAIPSSRSLA PPPNKPSIGT IGRQSSIDLV FRKQLYNKLA RRTESTRRLD
TSSTTTGADG GYGFSRSDME NRRRRSVKRK NSESSIRSHN FGDKNFAFRW INESFEEVAL
AHPSLDRMIG FVVSPQTRIL VRAVVKIFTG FGQGFRITGI QLLSCLSLLQ NFYADIPRPP
PAEKVSDLRF LDKANYFLGH AIIAYGWRGL SYLGDYAKYL KDVMKTRSNK EAIVRYLKIP
QEDLLGYEYG LRKGAVFQPS YFVSIDRGYE AIVLGIRGTW SLYDCITDLV CEYRPWKGGL
VHAGMLASAQ WFFTRIIPQI FHYIHENCKS ETRPISSFII TGHSLGAGTA ALITMMVADH
IDELRRLSNN PNFQVHCYSY APVASVSLDL SEKYSEYIDS FVCQDDLVAR LSYGTASCSK
ELIMDTMISV DGLGGSSKIN SDTKARKACF DIIETRRQEI FYSNEPRYPL LYIPGQVYQF
HRQPTEGSKK RRASTTDDAV PKRSPSSARE ESSKASSSRR TFSLLDDMPV CHSEPALSTS
KANGNGRPRN NSIDDTNDNT NLFTLHKGSP QLSKEMLISK TCLEDHMLVT YLNAFQAVRQ
DCMRELRQQQ RKQNGTATAT AVLASRQSST SSSCRSESPV PSIQIEDPEG KVEVANTTIA
AAAIASPSSS SSSSS
//
