Reviewed, UniProtKB/Swiss-Prot Q5A4N0 (ATG15_CANAL)

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:	Ca20C1.17, CaO19.3412, CaO19.10915

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	597 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
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 – 597	597	Putative lipase ATG15		PRO_0000090365
Regions
	Topological domain	1 – 15	15	Cytoplasmic Potential
	Transmembrane	16 – 36	21	Signal-anchor for type II membrane protein Potential
	Topological domain	37 – 597	561	Lumenal Potential
	Compositional bias	519 – 560	42	Ser-rich
Sites
	Active site	364	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	195	1	N-linked (GlcNAc...) Potential
	Glycosylation	262	1	N-linked (GlcNAc...) Potential
	Glycosylation	346	1	N-linked (GlcNAc...) Potential
	Glycosylation	481	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	106	1	E → K in CAA21938. Ref.1
	Sequence conflict	585	1	D → Y in CAA21938. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q5A4N0-1 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 3B8130FA04964AB4	FASTA	597	67,469
	10 20 30 40 50 60 MTLEKNRHAN KGTSWTWMIY KFVVGVITVA ILVLFITQKS VSQAQDKLRV EQQAIFSDQD 70 80 90 100 110 120 TLQLKHIFHH GTGPKNYRLH RRLDITSEYL AKHQPYFTTL TQQLSEPVLE EHIASDNLDK 130 140 150 160 170 180 IYQQSDWPEI HKGKNPFSIE LPFKKADSEA TRLKERNTLN FIESYLNYAR DIKGDAQILN 190 200 210 220 230 240 RINLDWIHDE IKVPNVTDRD TVVTLATISS NAYVRYPKDD DEKRKSDWID LGDWDPNRED 250 260 270 280 290 300 DDVNFGWDDI GLRGHVFVSK DNKTVVIGIK GTSGAGLPGG GSDETGGNDK TNDNLLFSCC 310 320 330 340 350 360 CARISYMWTT VCDCYEKTYT CNQDCLEKEL RKEDKYYQAV LELYRNVTDI YPPESTDIWV 370 380 390 400 410 420 TGHSLGGALA SLLGRTFGLP AVAFEAPGEM LATRRLHLPS PPGLPQHMEN IWHFGNTADP 430 440 450 460 470 480 IYMGVCNGAS STCNLAGYAM ETTCHTGLQC VYDVVTDKGW SVNLLNHRIH TVIDDIILTY 490 500 510 520 530 540 NETAPCAPSP PCRDCFNWRF VAHDDNEKDE PKLPNPLRSS SKSTLSTKTT SLKSSSTYSG 550 560 570 580 590 STSSSTVTKT TQTSPISSAS PTDQDPPKKC LKRTWYGWCT KWGYDDDDDD EDTFERK

References

[1]	"Candida albicans strain 1161 genome pilot sequencing project." Oliver K., Harris D., Barrell B.G., Rajandream M.A. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1161.
[2]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL033391 Genomic DNA. Translation: CAA21938.1. AACQ01000064 Genomic DNA. Translation: EAK97731.1. AACQ01000065 Genomic DNA. Translation: EAK97667.1.
RefSeq	XP_716661.1. XP_716721.1.
3D structure databases
SMR	Q5A4N0. Positions 196-374.
ModBase	Search...
Genome annotation databases
GeneID	3641641. 3641666.
KEGG	cal:CaO19.10915. cal:CaO19.3412.
Organism-specific databases
CGD	CAL0004893. ATG15.
Phylogenomic databases
OrthoDB	EOG973R85.
PhylomeDB	Q5A4N0.
Enzyme and pathway databases
BRENDA	3.1.1.3. 1124.
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_CANAL

Accession

Primary (citable) accession number: Q5A4N0
Secondary accession number(s): O94004

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	April 26, 2005
Last modified:	January 19, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)