Reviewed, UniProtKB/Swiss-Prot A5DC90 (ATG15_PICGU)

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
ORF Names:	PGUG_00895

Organism

Pichia guilliermondii (Yeast) (Candida guilliermondii) [Complete proteome]

Taxonomic identifier

4929 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
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 – 566	566	Putative lipase ATG15		PRO_0000317970
Regions
	Topological domain	1 – 17	17	Cytoplasmic By similarity
	Transmembrane	18 – 38	21	Signal-anchor for type II membrane protein
	Topological domain	39 – 566	528	Lumenal By similarity
Sites
	Active site	366	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	264	1	N-linked (GlcNAc...) Potential
	Glycosylation	348	1	N-linked (GlcNAc...) Potential
	Glycosylation	483	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	A5DC90-1 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: 4E888F2055B87459	FASTA	566	64,076
	10 20 30 40 50 60 MGSKHKKNAS KSLRAFSFII LSASIALVYI FNPVKLIFPS SIIRFHHGLP PQSQEIVTEQ 70 80 90 100 110 120 PKSHSKFQLK HIYHHGSGKN YKIHRRLDIT PEYLAKHDAY FQHFNQLQSG TEQVSLDNLD 130 140 150 160 170 180 SVVAQYDWPK HHQGKNPWTI ELPMKIAKRP AVRLKQRHDH NYIDSYLQYA LSVKSNPQHI 190 200 210 220 230 240 NNVQLEWISE DISVPDVKDR DTVVSLATIS SNAYVRFPKD DDEKKNSDWI DVGEPWVPDD 250 260 270 280 290 300 RNNNIEFGWG DDGLRGHIFV SEDNKTVVIG VKGTSGAGLP GSGSEETQAN DKTNDNLLFS 310 320 330 340 350 360 CCCARISYMW TTVCDCYEKT YTCNQDCLEK ELVRKDRYYQ AVLDLYRNVT EIYPSESHDI 370 380 390 400 410 420 WVTGHSLGGA LASLLGRTYG LPVVAYEAPG EMLATQRLHL PQPPGLPKHA ENIWHFGNTA 430 440 450 460 470 480 DPIFMGVCNG ASSSCNLAGY ALETACHTGR QCVYDVVTDK GWHVNLLNHR IHTVIDDIIM 490 500 510 520 530 540 TYNDTAPCAD QPPCRDCFNW RFTSRDDSLD DEPPLPNPLR PGKPSTTSSS QHHTSTTTTT 550 560 ETSRPQKCLK RTWYGWCVEW GDEEDA

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH408155 Genomic DNA. Translation: EDK36797.2.
3D structure databases
ModBase	Search...
Phylogenomic databases
OrthoDB	EOG973R85.
PhylomeDB	A5DC90.
Enzyme and pathway databases
BRENDA	3.1.1.3. 3704.
Family and domain databases
InterPro	IPR002921. Lipase_3. [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_PICGU

Accession

Primary (citable) accession number: A5DC90

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 10, 2009
Last modified:	January 19, 2010
This is version 19 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)