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Database: UniProt
Entry: A0A401H0H6_9APHY
LinkDB: A0A401H0H6_9APHY
Original site: A0A401H0H6_9APHY 
ID   A0A401H0H6_9APHY        Unreviewed;       494 AA.
AC   A0A401H0H6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
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   ORFNames=SCP_1201140 {ECO:0000313|EMBL:GBE87889.1};
OS   Sparassis crispa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Sparassidaceae; Sparassis.
OX   NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE87889.1, ECO:0000313|Proteomes:UP000287166};
RN   [1] {ECO:0000313|EMBL:GBE87889.1, ECO:0000313|Proteomes:UP000287166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA   Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT   "Genome sequence of the cauliflower mushroom Sparassis crispa
RT   (Hanabiratake) and its association with beneficial usage.";
RL   Sci. Rep. 8:16053-16053(2018).
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:GBE87889.1}.
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DR   EMBL; BFAD01000012; GBE87889.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401H0H6; -.
DR   STRING; 139825.A0A401H0H6; -.
DR   InParanoid; A0A401H0H6; -.
DR   OrthoDB; 1027561at2759; -.
DR   Proteomes; UP000287166; Unassembled WGS sequence.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287166};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          292..319
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
SQ   SEQUENCE   494 AA;  53712 MW;  FACAE5E42C9B4D28 CRC64;
     MLGNSRQPPD PGFAGILLRS LSLIDKPWSS PPDATNADAS MMLSTFASFL APLLAAFIRD
     EHSVALTPPP SLQFELRHLH AVSPEGRVAV RDVHHTSLMA SGYTPHTVQT QITKSVRPSS
     FAAFSRARAR SIQYRESESI DWDEEEVLAP DVQSRLTLLE LAKMTNNAYL TEPGDSGWYN
     LSGAWNTSYP FGWEPDTDGF RGQIFATEDN STVVVSIKGT SAAFVGGGGT TTKKDKFNDN
     LLFSCCCARI DWTWTTVCDC YRGGWKCDQD CLETALIEDS LFYSAGINLY NNLTYLYPEA
     NVWAVGHSLG GALASLLGVT FGVPAVAFES PGEKMAARRL HLPSPPSVQP IVHVYHTADP
     IAMGICNGIL SSCALGGYAL ESRCHLGQSI VYDTVSNLSW SVDIRTHGIV NVIDNVLSKP
     WGPSVLAGRE VPELAPEEEC VECFSWEFGD FPPSARLQDM SQGVDLPGSD ELRVCNAVSA
     EAIMKSTRYH GDVS
//
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