Reviewed, UniProtKB/Swiss-Prot Q6CU02 (ATG15_KLULA)

Names and origin

Protein names

Recommended name:
    Putative lipase ATG15
    EC=3.1.1.3
Alternative name(s):
    Autophagy-related protein 15

Gene names

Name:	ATG15
Ordered Locus Names:	KLLA0C08679g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	May be involved in lysis of subvacuolar cytoplasm to vacuole targeted bodies, intravacuolar autophagic bodies and of intravacuolar multivesicular body (MVB) vesicles By similarity.
Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity. Golgi apparatus membrane; Single-pass type II membrane protein By similarity. Endosome › multivesicular body membrane; Single-pass type II membrane protein By similarity. Prevacuolar compartment membrane; Single-pass type II membrane protein By similarity. Note: From ER, targeted to vacuolar lumen at the MVB vesicles via the Golgi and the prevacuolar compartment (PVC) By similarity.
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family.

Ontologies

Keywords
Biological process	Autophagy Lipid degradation
Cellular component	Endoplasmic reticulum Endosome Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	autophagy Inferred from electronic annotation. Source: UniProtKB-KW lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW endosome Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	triglyceride lipase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 531	531	Putative lipase ATG15		PRO_0000090369
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 31	20	Signal-anchor for type II membrane protein Potential
	Topological domain	32 – 531	500	Lumenal Potential
Sites
	Active site	340	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Glycosylation	207	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6CU02-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 234A7D25A1E891E2	FASTA	531	58,819
	10 20 30 40 50 60 MKPGIKISKR YSARNASVIT VLLLLIYLIY INKETIQTKY QGSRINHDSG GDSTKDKTHT 70 80 90 100 110 120 FTIKEIHFRP LDEKTQSYGS LQVTPEFVNM AKSEFEQNVA VASGDNEDLY DKQLWSASIK 130 140 150 160 170 180 SNPWTHQFTL KQGSIKMKRM VNRDPDYVES FLDYAHENPE MARKVHLDWV DESVLAPNVT 190 200 210 220 230 240 DKETVISLAL MSSNAYVRLP YEGDWRNLSD WNNDLNPDLS VGIGWDSDGV RGHIFSNDDS 250 260 270 280 290 300 SVIVIALKGT SAQGLPGSGE DETTDNDKLN DNVLFSCCCA RVSYLWKTAC DCYVKSYTCD 310 320 330 340 350 360 EKCLEQELVR KDRYYQAVLD IYRSVVTAHP NSAIWITGHS LGGALASLLG RTFGAPAVAF 370 380 390 400 410 420 EAPGELLATK RLHLPMPPGL PAYQEGVWHI GHTADPIFMG TCNGASSSCS IAGYAMETSC 430 440 450 460 470 480 HSGKVCVYDV VTDKGWHVNM LNHRIHTVID GILTDYDTVA KCKTPDACHD CFNWNYVKGR 490 500 510 520 530 DVPKKHKSSS STASSTSAET STLTVGPSPP EKTTTSCIGR NWIGICTEYG I

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382123 Genomic DNA. Translation: CAH01438.1.
RefSeq	XP_452587.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6CU02.
Genome annotation databases
GeneID	2892241.
GenomeReviews	Gene locus KLLA0C08679g in contig CR382123_GR.
KEGG	kla:KLLA0C08679g.
Phylogenomic databases
HOGENOM	Q6CU02.
OMA	HIFHHGT.
Enzyme and pathway databases
BRENDA	3.1.1.3. 74088.
Family and domain databases
InterPro	IPR002921. Lipase_3. IPR008262. Lipase_Ser_AS. [Graphical view]
Pfam	PF01764. Lipase_3. 1 hit. [Graphical view]
PROSITE	PS00120. LIPASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATG15_KLULA

Accession

Primary (citable) accession number: Q6CU02

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	August 16, 2004
Last modified:	November 3, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)