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Q6CU02 · ATG15_KLULA

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.

153150100150200250300350400450500
TypeIDPosition(s)Description
Active site340Charge relay system

GO annotations

AspectTerm
Cellular Componentmultivesicular body membrane
Molecular Functionphospholipase activity
Molecular Functiontriacylglycerol lipase activity
Biological Processmultivesicular body membrane disassembly
Biological Processneutral lipid 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
    • Ordered locus names
      KLLA0C08679g

Organism names

Accessions

  • Primary accession
    Q6CU02

Proteomes

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.

Type
IDPosition(s)Description
Topological domain1-11Cytoplasmic
Transmembrane12-31Helical; Signal-anchor for type II membrane protein
Topological domain32-531Lumenal

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation.

Type
IDPosition(s)Description
ChainPRO_00000903691-531Putative lipase ATG15
Glycosylation178N-linked (GlcNAc...) asparagine
Glycosylation207N-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

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region482-513Disordered
Compositional bias488-513Polar residues

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    531
  • Mass (Da)
    58,819
  • Last updated
    2004-08-16 v1
  • MD5 Checksum
    42A351863F1630EA8E53F8C0C7D7F34B
MKPGIKISKRYSARNASVITVLLLLIYLIYINKETIQTKYQGSRINHDSGGDSTKDKTHTFTIKEIHFRPLDEKTQSYGSLQVTPEFVNMAKSEFEQNVAVASGDNEDLYDKQLWSASIKSNPWTHQFTLKQGSIKMKRMVNRDPDYVESFLDYAHENPEMARKVHLDWVDESVLAPNVTDKETVISLALMSSNAYVRLPYEGDWRNLSDWNNDLNPDLSVGIGWDSDGVRGHIFSNDDSSVIVIALKGTSAQGLPGSGEDETTDNDKLNDNVLFSCCCARVSYLWKTACDCYVKSYTCDEKCLEQELVRKDRYYQAVLDIYRSVVTAHPNSAIWITGHSLGGALASLLGRTFGAPAVAFEAPGELLATKRLHLPMPPGLPAYQEGVWHIGHTADPIFMGTCNGASSSCSIAGYAMETSCHSGKVCVYDVVTDKGWHVNMLNHRIHTVIDGILTDYDTVAKCKTPDACHDCFNWNYVKGRDVPKKHKSSSSTASSTSAETSTLTVGPSPPEKTTTSCIGRNWIGICTEYGI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias488-513Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CR382123
EMBL· GenBank· DDBJ
CAH01438.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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