ATG15_DEBHA
ID ATG15_DEBHA Reviewed; 615 AA.
AC Q6BLM0; B5RUF1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; OrderedLocusNames=DEHA2F12364g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Binds to both phosphatidylinositol (PI) and
CC phosphatidylinositol 3,5-bisphosphate (PIP2). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:P25641}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P25641}. Prevacuolar compartment membrane
CC {ECO:0000250|UniProtKB:P25641}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P25641}. Note=From ER, targeted to vacuolar
CC lumen at the MVB vesicles via the Golgi and the prevacuolar compartment
CC (PVC). {ECO:0000250|UniProtKB:P25641}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; CR382138; CAR66329.1; -; Genomic_DNA.
DR RefSeq; XP_002770804.1; XM_002770758.1.
DR AlphaFoldDB; Q6BLM0; -.
DR STRING; 4959.XP_002770804.1; -.
DR ESTHER; debha-atg15; Lipase_3.
DR EnsemblFungi; CAR66329; CAR66329; DEHA2F12364g.
DR GeneID; 8998954; -.
DR KEGG; dha:DEHA2F12364g; -.
DR VEuPathDB; FungiDB:DEHA2F12364g; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_0_2_1; -.
DR InParanoid; Q6BLM0; -.
DR OMA; CYEKTYT; -.
DR OrthoDB; 937562at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 3: Inferred from homology;
KW Autophagy; Endosome; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..615
FT /note="Putative lipase ATG15"
FT /id="PRO_0000090367"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..615
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 520..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 378
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 615 AA; 69083 MW; 81F12D95ECBF55D9 CRC64;
MKQLGEEHPL ISTKRPRAKK RRSIAICAAV LTLIAFGFIR FVPKDILAGG WYEGEKDGLS
ALDNEEVRDM QTDGTTFELK HIFHRGTGSH NYMVHRRLDV TKEYLEAHSE ELEELTTMQT
SEVDESNLQD VYDAYDWPQA HTGKNPWTIK LQIRQSPTNG VVKRLKERHT PNFLDSYLAY
ALSVKGNPAL LNKIELEWED EHEIPIPDVK DRDTVVSLAT ISSNAYVKFP KDDKEKKRSD
WIDVGDPWVP DENHTDINFG WADDGLRGHV FVSTDNKTVV IGIKGTSGAG LIGTGPEETT
ANDKLNDNLL FSCCCARVGY MWTTVCDCYQ KAYTCDQDCL EKELMRQDRY YQATLDLYRN
VSQLYDPSTT NIWVTGHSLG GALASLVGRT YGLPAVAFEA PGEMLATRRL HLPQPPGLPK
HLENIWHFGN TADPIYMGVC NGVSSSCNVA GYAMETACHT AHQCVYDVVT DMGWRVNLLN
HRIHTVIDDI ILAYNDTPPC VQQPPCRDCF NWRFTSSDDN KNDEPPLPNP LHPKPPSTVR
SSNMPHEQSP NASRSLSSLC TEPSCTSSFQ SVSPSFSSQL PSHPSQNPQR CLRRTWYGRC
SKWGHNSAAH HVSSI
