O13934 · ATG15_SCHPO

Function

function

Lipase which is essential for lysis of subvacuolar cytoplasm to vacuole targeted bodies and intravacuolar autophagic bodies. Involved in the lysis of intravacuolar multivesicular body (MVB) vesicles. The intravacuolar membrane disintegration by atg15 is critical to life span extension (By similarity).

Catalytic activity

Features

Showing features for active site.

142450100150200250300350400
TypeIDPosition(s)Description
Active site283Charge relay system

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentfungal-type vacuole lumen
Cellular Componentmembrane
Cellular Componentmultivesicular body membrane
Cellular Componentvacuolar lumen
Molecular Functionlysophospholipase activity
Molecular Functionphospholipase activity
Molecular Functiontriglyceride lipase activity
Biological Processmacroautophagy
Biological Processmultivesicular body membrane disassembly
Biological Processneutral lipid catabolic process
Biological Processphosphatidylserine catabolic process
Biological Processpiecemeal microautophagy of the nucleus

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Putative lipase atg15
  • EC number
  • Alternative names
    • Autophagy-related protein 15

Gene names

    • Name
      atg15
    • ORF names
      SPAC23C4.16c

Organism names

Accessions

  • Primary accession
    O13934

Proteomes

Organism-specific databases

Subcellular Location

Endosome, multivesicular body membrane
; Single-pass type II membrane protein
Prevacuolar compartment membrane
; Single-pass type II membrane protein
Note: From ER, targeted to vacuolar lumen at the MVB vesicles via the Golgi and the prevacuolar compartment (PVC).

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-9Cytoplasmic
Transmembrane10-30Helical; Signal-anchor for type II membrane protein
Topological domain31-424Lumenal

Keywords

Phenotypes & Variants

Disruption phenotype

Impairs atg8-processing.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00000903701-424Putative lipase atg15
Glycosylation187N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Binds to both phosphatidylinositol (PI) and phosphatidylinositol 3,5-bisphosphate (PIP2).

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    424
  • Mass (Da)
    47,938
  • Last updated
    1998-01-01 v1
  • Checksum
    8B8BA13645C5097E
MSQLLFLRRFFFLFCFIIRISCTGVFESVIKSSENVPDKVNVKLQHVFHYGLNEDSISYYRLDVAKKSVYAESESKLPLKMKKGYSVHLKDQSRDALTDYRYKSMKGIYSEANSPADLWEQEAIVIPDITDKETIYSLGKMSYNAYQKIPFDGDWLDLGPDWNITPPEGFGWEEDGLRGHVFSNDDNSTIIIAMKGTSIFGIGRGTSQKDRVNDNLLFSCCCARVSWAWSTVCGCYKNTYTCSQTCLEDEVQDDSRYYSASLDIFYSVKELYPDAQIWLTGHSLGGATAALMGLSFGIPTVTFEAPGDRMAARRLHLPMPPGLPDEESLVWHFGHNADPIYLGKCTGPTSLCWAGGYAMESTCHTGQECLYDVVKDKGWHLSITHHRMQTVLNDVIDAYEKLPDCSHTPNCVDCYLWEFPDDDS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU329670
EMBL· GenBank· DDBJ
CAB16887.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp