ID A0A2V1AVE6_9ASCO Unreviewed; 568 AA.
AC A0A2V1AVE6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Putative lipase ATG15 {ECO:0000256|ARBA:ARBA00018542};
DE EC=3.1.1.3 {ECO:0000256|ARBA:ARBA00013279};
DE AltName: Full=Autophagy-related protein 15 {ECO:0000256|ARBA:ARBA00029828};
DE AltName: Full=Putative lipase atg15 {ECO:0000256|ARBA:ARBA00019241};
GN ORFNames=CXQ85_000743 {ECO:0000313|EMBL:PVH21752.1};
OS [Candida] haemuloni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH21752.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH21752.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH21752.1,
RC ECO:0000313|Proteomes:UP000244309};
RA Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA Litvintseva A.P.;
RT "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT Patient with Chronic Leg Ulcers in Israel.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipase which is essential for lysis of subvacuolar cytoplasm
CC to vacuole targeted bodies and intravacuolar autophagic bodies.
CC Involved in the lysis of intravacuolar multivesicular body (MVB)
CC vesicles. The intravacuolar membrane disintegration by ATG15 is
CC critical to life span extension. {ECO:0000256|ARBA:ARBA00024663}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001024};
CC -!- SUBUNIT: Binds to both phosphatidylinositol (PI) and
CC phosphatidylinositol 3,5-bisphosphate (PIP2).
CC {ECO:0000256|ARBA:ARBA00011137}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000256|ARBA:ARBA00004343}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004343}. Prevacuolar compartment membrane
CC {ECO:0000256|ARBA:ARBA00004270}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004270}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701}.
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:PVH21752.1}.
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DR EMBL; PKFO01000005; PVH21752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1AVE6; -.
DR STRING; 45357.A0A2V1AVE6; -.
DR EnsemblFungi; CXQ85_000743-t46_1; CXQ85_000743-t46_1-p1; CXQ85_000743.
DR VEuPathDB; FungiDB:CXQ85_000743; -.
DR OrthoDB; 1027561at2759; -.
DR Proteomes; UP000244309; Unassembled WGS sequence.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; PTHR47175; LIPASE ATG15-RELATED; 1.
DR PANTHER; PTHR47175:SF2; LIPASE ATG15-RELATED; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
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:UP000244309};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 358..377
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 511..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 64048 MW; C4BB9E4C10444E6F CRC64;
MLSEKQPLRQ RRRSSFSILS IIAHVALSVA LFISIYTFWP SRHSPEPDQL HQLEEAPSLE
RSTSFQLKHV FHHGTGKYNR VHKRLDVTPE FLERHENTLA ELTESLYAEN EPVDPNNADS
VLRSEGWSRA LGDKDPWTMD LTIRPSSKPA RLRRLKERHT PHFLDSYLQY AMEVKGDPKK
LDRIGLEWEP EQDVLLPDIQ DKDSVVALAL ISSNAYVKLP LDDDEKKKSD WIDVGDPWDV
DEENPDVNFG WLDDGLRGHV FVSNDSKTVV IGIKGTSGAG LPGGGSDETS GNDKTNDNLL
FSCCCARVGY MWTTVCDCYE KTYTCNQDCL EKELLRQDRY YQAALDLYRN VTKIYDPETT
DIWVTGHSLG GALASLLGRT YGLPVVAFEA PGEMLATKRL HLPQAPGIPK HMEHIWHFGN
TADPIFMGVC NGASSSCSVG GYAMETACHT GKLCVYDVVT DHGWHVSLLN HRIHTVIDEI
ILKYNTTATC VDQPPCRDCF NWRFVSKDDL EPDEPKLPHP LKPKPKPTET SSSASTSTSS
SLPSESDKPK KCLERTWYGW CKKWEGEE
//
