ATG15_COCIM
ID ATG15_COCIM Reviewed; 634 AA.
AC Q1DZE0; J3KDM8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Putative lipase ATG15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=ATG15; ORFNames=CIMG_04323;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
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).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704914; EAS33299.3; -; Genomic_DNA.
DR RefSeq; XP_001244882.2; XM_001244881.2.
DR AlphaFoldDB; Q1DZE0; -.
DR STRING; 246410.Q1DZE0; -.
DR ESTHER; cocim-atg15; Lipase_3.
DR EnsemblFungi; EAS33299; EAS33299; CIMG_04323.
DR GeneID; 4565174; -.
DR KEGG; cim:CIMG_04323; -.
DR VEuPathDB; FungiDB:CIMG_04323; -.
DR InParanoid; Q1DZE0; -.
DR OMA; WFGCKDE; -.
DR OrthoDB; 937562at2759; -.
DR Proteomes; UP000001261; 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.
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..634
FT /note="Putative lipase ATG15"
FT /id="PRO_0000317962"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 37..634
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT REGION 526..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 317
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 634 AA; 68882 MW; 1FAD8CA59F94B2F3 CRC64;
MMTPSQWKDD ICTSQLAMVA CAIFLLLPIF SPVVFATGLE SHRNLQVPFV QPEDLGFLPQ
RSPQGHEFAL RHIFHHGTYQ YPLLHKRLDV NPETKIWVAS EDGAKLEFSP HFRVSSQPSQ
IQRLTDRRVQ VMEARLSAAR TPEVFSTLSP PVWTIDELPG PNISDKTTVL NLAKMTANAY
IMEPGAERWE DVSGPFNQSL SFGWEKDGLR GHIYADQTNS TIIIALKGTS AALFDGDETT
TNDKINDNLF FSCCCGQGGQ YFWRQVCDCY SSAYTCNSTC LVSALVTENR YYRASLDLYA
NVTDIYPNST VWLAGHSLGG AVSSLLGLTY GLPVVTFEGV PEALPASRLG LPVPPGTDPN
TPQAREYTGA YHFGHTADPV YMGTCNGATS FCTLAGYAME SACHTGQRCV YDTVGDLGWR
VGIGTHRILN VISDVIERYE DVPTCVPDTE CRDCALWKFF ESNGSHPIPP SSSTTSPTRT
RTSTCETPGW WGCLDKTTTT GTTTNVITTS TSTCKTPGWF GCKDPTTTSS VPSATPSPTP
IITSISMPTP TSTTCETPGW FGGCNDPPTT ATSKPNSSSP STSTTCTRPG FFWGCWDPTS
SSETPTAAFS STATHTSCAS KTWFGRSCTT PAPR
