ID ATG15_SCHPO Reviewed; 424 AA.
AC O13934;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Putative lipase atg15;
DE EC=3.1.1.3;
DE AltName: Full=Autophagy-related protein 15;
GN Name=atg15; ORFNames=SPAC23C4.16c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA Du L.L.;
RT "Global analysis of fission yeast mating genes reveals new autophagy
RT factors.";
RL PLoS Genet. 9:E1003715-E1003715(2013).
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 -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC {ECO:0000269|PubMed:23950735}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {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; CU329670; CAB16887.1; -; Genomic_DNA.
DR PIR; T38271; T38271.
DR RefSeq; NP_593188.1; NM_001018584.2.
DR AlphaFoldDB; O13934; -.
DR STRING; 284812.O13934; -.
DR ESTHER; schpo-C23C4.16C; Lipase_3.
DR GlyCosmos; O13934; 1 site, No reported glycans.
DR iPTMnet; O13934; -.
DR MaxQB; O13934; -.
DR PaxDb; 4896-SPAC23C4-16c-1; -.
DR EnsemblFungi; SPAC23C4.16c.1; SPAC23C4.16c.1:pep; SPAC23C4.16c.
DR GeneID; 2541924; -.
DR KEGG; spo:SPAC23C4.16c; -.
DR PomBase; SPAC23C4.16c; atg15.
DR VEuPathDB; FungiDB:SPAC23C4.16c; -.
DR eggNOG; KOG4540; Eukaryota.
DR HOGENOM; CLU_028295_1_1_1; -.
DR InParanoid; O13934; -.
DR OMA; KEVITHV; -.
DR PhylomeDB; O13934; -.
DR PRO; PR:O13934; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000328; C:fungal-type vacuole lumen; ISO:PomBase.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004622; F:lysophospholipase activity; ISO:PomBase.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR GO; GO:0034496; P:multivesicular body membrane disassembly; IBA:GO_Central.
DR GO; GO:0046461; P:neutral lipid catabolic process; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
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.
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..424
FT /note="Putative lipase atg15"
FT /id="PRO_0000090370"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..424
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 424 AA; 47938 MW; 8B8BA13645C5097E CRC64;
MSQLLFLRRF FFLFCFIIRI SCTGVFESVI KSSENVPDKV NVKLQHVFHY GLNEDSISYY
RLDVAKKSVY AESESKLPLK MKKGYSVHLK DQSRDALTDY RYKSMKGIYS EANSPADLWE
QEAIVIPDIT DKETIYSLGK MSYNAYQKIP FDGDWLDLGP DWNITPPEGF GWEEDGLRGH
VFSNDDNSTI IIAMKGTSIF GIGRGTSQKD RVNDNLLFSC CCARVSWAWS TVCGCYKNTY
TCSQTCLEDE VQDDSRYYSA SLDIFYSVKE LYPDAQIWLT GHSLGGATAA LMGLSFGIPT
VTFEAPGDRM AARRLHLPMP PGLPDEESLV WHFGHNADPI YLGKCTGPTS LCWAGGYAME
STCHTGQECL YDVVKDKGWH LSITHHRMQT VLNDVIDAYE KLPDCSHTPN CVDCYLWEFP
DDDS
//
