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Database: UniProt
Entry: A0A1C7M6X7_GRIFR
LinkDB: A0A1C7M6X7_GRIFR
Original site: A0A1C7M6X7_GRIFR 
ID   A0A1C7M6X7_GRIFR        Unreviewed;       734 AA.
AC   A0A1C7M6X7;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Autophagy-related protein 15 {ECO:0000256|ARBA:ARBA00029828};
DE            EC=3.1.1.117 {ECO:0000256|ARBA:ARBA00026105};
DE            EC=3.1.1.3 {ECO:0000256|ARBA:ARBA00013279};
GN   Name=ATG15_1 {ECO:0000313|EMBL:OBZ72129.1};
GN   ORFNames=A0H81_08058 {ECO:0000313|EMBL:OBZ72129.1};
OS   Grifola frondosa (Maitake) (Polyporus frondosus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Grifolaceae; Grifola.
OX   NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ72129.1, ECO:0000313|Proteomes:UP000092993};
RN   [1] {ECO:0000313|EMBL:OBZ72129.1, ECO:0000313|Proteomes:UP000092993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9006-11 {ECO:0000313|EMBL:OBZ72129.1,
RC   ECO:0000313|Proteomes:UP000092993};
RA   Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT   "Whole genome sequencing of Grifola frondosa 9006-11.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-
CC         O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+);
CC         Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668;
CC         EC=3.1.1.117; Evidence={ECO:0000256|ARBA:ARBA00024511};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC         Evidence={ECO:0000256|ARBA:ARBA00024511};
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   -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC       {ECO:0000256|ARBA:ARBA00010092}.
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:OBZ72129.1}.
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DR   EMBL; LUGG01000009; OBZ72129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C7M6X7; -.
DR   STRING; 5627.A0A1C7M6X7; -.
DR   OrthoDB; 1420757at2759; -.
DR   Proteomes; UP000092993; Unassembled WGS sequence.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092993};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..734
FT                   /note="Autophagy-related protein 15"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008888963"
FT   DOMAIN          234..261
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
FT   COILED          411..448
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   734 AA;  80155 MW;  97EA4952A8DE2485 CRC64;
     MLLALTNLLI PLLSIFSREQ TPISVPEVSS APELHFELRH LHAATPSGQI LFHDVHPADS
     FIADSQVSYT LRTRHIKSHK PSSFAAFSRA RARSIEFGES EALHWDIEEM IGPDSEDRDT
     LLQIAKMTNN AYLEPGEPGW YDLEGKWNVS YPFGWEAEDD SLRGHIFATS DNSTVVLAIK
     GTSAAFVGGG GPTSKKDKVN DNLLGGWKCD QNCLEDALIE ENLFYPIGTN LYNNLTYLYP
     DSNVWVVGHS LGGALASLLG VTFGIPVVAI ESPGEKMAAA RLHLPSPPSV QHITHLYHTA
     DPIAMGTCNG VLSSCALGGY AMESKCHLGS SIIYDTVSNL SWAVDIRTHT IVNVIEKLLA
     LPWPPSVEVG REVPEAKPEE DCVECFSWEF GDFPASGRVD VVSGEQYRYA LTNFRIAHEK
     VEEQRMQLQE QERQVALLRA RIALLEGTNQ DGQAGAFAME GSNSVDDFSI KNAASNLGRL
     MNRWAADIVR APPVPLDQIR DAAVKDLLDG DIPEPNPFTS NTTGMQVQGL LRHAMSQTIS
     EGIINCLVIT NCPDANIQLT RIHEHIFSRD ATVAAVWRRQ TFSAAVESCS NEMSRFLLTE
     HMAALTATLN IENGKPPASE ALDVLQAAYG FSRMLHGSPS SSGGTVDAFY RAFVPELRGT
     LDPQQIELVK RCVKTEHGQS DRVGATVFPG LVKVSRSAAG PSGQENTQTV VKRAQVVCEC
     ALGVNTDAQC SEWY
//
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