ID G7DWA2_MIXOS Unreviewed; 1100 AA.
AC G7DWA2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN Name=Mo01444 {ECO:0000313|EMBL:GAA94790.1};
GN ORFNames=E5Q_01444 {ECO:0000313|EMBL:GAA94790.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA94790.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(2011).
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:GAA94790.1}.
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DR EMBL; BABT02000047; GAA94790.1; -; Genomic_DNA.
DR AlphaFoldDB; G7DWA2; -.
DR eggNOG; KOG2088; Eukaryota.
DR HOGENOM; CLU_256442_0_0_1; -.
DR InParanoid; G7DWA2; -.
DR Proteomes; UP000009131; 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 Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009131};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 763..926
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 122096 MW; 70F6FB7AA0AF0F11 CRC64;
MAASSSGRRS TGDSAAHAGL FRPLLGPADS NPARSGSGTA RMISTVLLGA PPFTSSTKSS
NKRRNPSRQR AASTDRTLPS KPNGREIKDD FERRIFDDAA ARPSLRRQNA VPSHRVARDS
DDTELEEPPS PSLLPGGYTW SVGRSQEQNG KQSEQYHAAL RLPPPLLDDA STPESFEGLL
GIRRDRETQR SLARQQRLQA RDRPPPKNFS ESLLGAASKL YYTLAPPTLP PARPVARRAP
SSHFVASPTA LDDDIPLLDE EEQEASNRNL VKMDRRRERS ELSLKGYEAT GKLATRVATR
LRREASSRRS KAVAESKGLH LSLDRADSLV VSESTRTDQR TLPPRTLTPS ALFAPHTRSQ
SETKPTDVES EMPLSVPRAP RLVALESDIL PSPFPFEPSI PAPNKLQRPA QENDYFATSH
KQTHQSHLSL LHALRSMIEY IRSKSDALTW LLIGDFQEGA QVEEVGGLIG AIYLLAGFVY
FVLVHLVALL YSTAQVLRTA SLFVYWIFVN LTGKTDLSRV VMRYYRSCRA EWDSVASQDH
ETLSLWAVIL GLAEMAAVHA VTRDRYLLEG PGQLERLSPA SLSGPSNATA HSSPRMSRRQ
KRKSVSAEGE QLIVTKDENN ILEGTLFSPR ADTTQEERFA YLGGILQSPA LEPMKPRKSL
DAKQDSDDFM RRLKRHCRFS TASYGLHSYI LHPPTPLFTP SGATLPHTIF SSLSKISDKA
SVLHVAIQKE YSGAWGADEG SDTESEWEPS FYLIRDHDNR EIIVTFRGTQ SLHDIVTDLT
ADDETLMLDN LEGDGQTSYR IHSGILKAAR RLIDADRSPL YATLKTALQD NPDYALALTG
HSLGGAVASA VAILLAQYEP SAQDAGSGRW RLSAKCDLPG PRDVYAYCYA HPTTLDAALC
DYCAAGTQPL VYSVCLAADI IPRIGPSQMR ETRRILGRLA RLRRGVMPKT KHALFETEES
QQHASWSILR LWWRWRRLGG GVVLAEGQEL PEEAAQLAEH AWSIRNGLDM ALDDSTTRDE
PAMMRPPGKV YHVDRLPVAE EARARLEARS TASPNDEEEE ERWTIYRVTK PSSFFAYPWL
ELDAVRAHLP QVYLDSIEAL
//
