ID A0A0D1Z6U0_EXOME Unreviewed; 1178 AA.
AC A0A0D1Z6U0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=PV10_07819 {ECO:0000313|EMBL:KIV90522.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV90522.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV90522.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV90522.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847524; KIV90522.1; -; Genomic_DNA.
DR RefSeq; XP_016222096.1; XM_016372764.1.
DR AlphaFoldDB; A0A0D1Z6U0; -.
DR STRING; 212818.A0A0D1Z6U0; -.
DR GeneID; 27325664; -.
DR VEuPathDB; FungiDB:PV10_07819; -.
DR HOGENOM; CLU_001871_0_0_1; -.
DR OMA; SWKVHKG; -.
DR OrthoDB; 373802at2759; -.
DR Proteomes; UP000054302; 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:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G02710)-RELATED; 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:UP000054302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 832..1001
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1178 AA; 129149 MW; 277015C44D072FFA CRC64;
MFWTTPQESD KDDQDNQNDQ NDQNQLEYAP PNQHDIVLAR SPQGRTLLPA PAAALVSGIT
GLTSFYIRAG TKVGGWGLYA TREATLKTLS VSRSVLETVL IAAGRDVSYR SNGDLGRAEA
ENLLEKSISA LYTTISTASF IASASFFLTE ASLNSVSGLS IQGLSTLNAV LGQTESSRAV
AAIITLIRDE LNRPEAGNRG EVVSYLDLIT GTVGFVLLQR WGRRKTQLDF RNVGGEETIW
DAVIDDRGFR ADVVGTRRKG LINIHGASAG PTMTFGSPDG EDDFEAVERA TLHDVQALST
SPDSQTLLSE EEVRDLIEKQ LPPGARAVIT AETVTAKTIK VDIYDADTTH IEPPPGTVMV
AEKLNHEQEN KGLGRSHPRQ TVIFRTALKR SSSTDPPLGE LLRLTSEETI HDDTHEQPDP
EDILEMSPVP KRISIAENPI HIEPTTFSDS DHSTVIDAVQ PPIPPKIIPT GVNANEKRSR
RPILPDRKSS TTKISDHIPL MNKSQKKKHP HADKKEGGVL KKALKSLSPT QSSTAIKDIR
KPDLPQRSQP AFTQTNDLRK RASSVVRGDT TPRKGMASFN HGQSPTTSPS LYRTAHQESS
YFAIQNRRRD SSVSQTTETF SVHSVDSRPG SPTFTRTHTR VVSGLAQTKS ELALSMKEAD
TKVDIPNGST HHRRSRSFVP SLYSMATRDS HEAIILAPKF PLPRKSIYED QNILNALASE
GKVPGIFPDR HLVRTVRRFS RFASASYGSN FLRVMGLSSN EEQLRNSTEL LALNLHHEHD
SFSSHTGLPP HTILLSSFLD PQGVTGNTDW SPSAISPLIH FISIDDDSKA VVLTCRGTLG
FEDVLTDMTC DYDDLLWQGQ KYKVHKGIHA SARRLLGGNG SRIMATIRAT LEQYPDYGLV
LCGHSLGGAV AAVLAILISE PSQDESKTGF VTSSMPKLLP QRTTTNEFFE DAARPITLPA
GRPVHVYAYG TPACVSELLR KATRGLITTI VNNADIVPCL SLGILHDFRT VALHLKTDTS
DAFGSLKTRV WQRIKNAVMS SFFNNSNGPP PPENVAGDGL GEDTWAWSAL KTLRAAMIND
KLVPPGEVFV VETSRVFDRL DPDVAREAVF GPDDSKDDRT EKLYRALGRP ATRVQLKLIR
DVETRFGELR FGRDMFGDHS PGRYEAALAL LEKGVCED
//
