ATG15_AJECN
ID ATG15_AJECN Reviewed; 585 AA.
AC A6REI4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; ORFNames=HCAG_08049;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN04383.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476664; EDN04383.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001536940.1; XM_001536890.1.
DR AlphaFoldDB; A6REI4; -.
DR STRING; 339724.A6REI4; -.
DR ESTHER; ajecn-atg15; Lipase_3.
DR EnsemblFungi; EDN04383; EDN04383; HCAG_08049.
DR GeneID; 5443371; -.
DR KEGG; aje:HCAG_08049; -.
DR HOGENOM; CLU_028295_0_0_1; -.
DR OrthoDB; 937562at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
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..585
FT /note="Putative lipase ATG15"
FT /id="PRO_0000317957"
FT TRANSMEM 1..21
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 22..585
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 500..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 291
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 585 AA; 63488 MW; 5EF38668984D7B6B CRC64;
MMGLDLLVSL LALSVSPCIA ATRSPLQIPV LDTQPIETGR EFTLRHMLHH GTYRDPLLHK
RLDIRPDTLL WAASENGEKR ESVPRFRVSS RPINIHRLSD RHVSVVEDYL SIARMTSSAV
TLSSDYWTLD EVDAPDVTDK ETVLSLAKMT SNAYIMIPGS GEWFDVVPPF NHSDSFGWDS
DGLRGHIYSD NTNSTIVVVL KGTSAAIFDG GGTTTNDKVN DNLFFSCCCA QGGHYFWRQV
CDCYSSTYTC NTACVRKALR QENRYYRAAL NLYSNITAMY PQSNIWVTGH SLGGAVSSLL
GMTYGLPVVT FEAVPEALPA SRLGLPPPPG TDPSSPQARN YTGAYHFGHT ADPIYMGTCN
GATSVCTLGG YAMESSCHTG QLCTYDTVED FGWRVGIGTH RIREVITDVI ERYDDVPTCA
PFTECVDCNN WKFFESNETT PTPTTTTTST STRTRTSTCK TPGWWGCLDP TTTPTTTATT
STTSTSTCKT PGWFGCKDPT TTSTVPTASP APTITPTSPP TTTASTTSTC ESPGWFGCND
PTSTTTFPVP STTSTSTPCS TPGWFWGCRD QTTTTSASPP ITSPP
