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Reviewed, UniProtKB/Swiss-Prot O13934 (ATG15_SCHPO)

Last modified January 19, 2010. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative lipase atg15
    EC=3.1.1.3
Alternative name(s):
    Autophagy-related protein 15
Gene names
Name: atg15
ORF Names: SPAC23C4.16c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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. Endosomemultivesicular 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 processAutophagy
Lipid degradation
   Cellular componentEndoplasmic reticulum
Endosome
Golgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processautophagy

Inferred from electronic annotation. Source: UniProtKB-KW

triglyceride catabolic process

Inferred by curator. Source: GeneDB_SPombe

   Cellular componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum

Inferred from direct assay. Source: GeneDB_SPombe

endosome

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontriglyceride lipase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Putative lipase atg15
PRO_0000090370

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Signal-anchor for type II membrane protein Potential
Topological domain31 – 424394Lumenal Potential

Sites

Active site2831Charge relay system By similarity

Amino acid modifications

Glycosylation1871N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O13934-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 8B8BA13645C5097E

FASTA42447,938
        10         20         30         40         50         60 
MSQLLFLRRF FFLFCFIIRI SCTGVFESVI KSSENVPDKV NVKLQHVFHY GLNEDSISYY 

        70         80         90        100        110        120 
RLDVAKKSVY AESESKLPLK MKKGYSVHLK DQSRDALTDY RYKSMKGIYS EANSPADLWE 

       130        140        150        160        170        180 
QEAIVIPDIT DKETIYSLGK MSYNAYQKIP FDGDWLDLGP DWNITPPEGF GWEEDGLRGH 

       190        200        210        220        230        240 
VFSNDDNSTI IIAMKGTSIF GIGRGTSQKD RVNDNLLFSC CCARVSWAWS TVCGCYKNTY 

       250        260        270        280        290        300 
TCSQTCLEDE VQDDSRYYSA SLDIFYSVKE LYPDAQIWLT GHSLGGATAA LMGLSFGIPT 

       310        320        330        340        350        360 
VTFEAPGDRM AARRLHLPMP PGLPDEESLV WHFGHNADPI YLGKCTGPTS LCWAGGYAME 

       370        380        390        400        410        420 
STCHTGQECL YDVVKDKGWH LSITHHRMQT VLNDVIDAYE KLPDCSHTPN CVDCYLWEFP 


DDDS 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB16887.1.
PIRT38271.
RefSeqNP_593188.1.

3D structure databases

SMRO13934. Positions 129-314, 135-341.
ModBaseSearch...

Genome annotation databases

GeneID2541924.
GenomeReviewsGene locus atg15 in contig CU329670_GR.
KEGGspo:SPAC23C4.16c.
NMPDRfig|4896.1.peg.3158.

Organism-specific databases

GeneDB_SpombeSPAC23C4.16c.

Phylogenomic databases

eggNOGfuNOG04745.
HOGENOMHBG398588.
OMACCCARID.
OrthoDBEOG973R85.
PhylomeDBO13934.

Enzyme and pathway databases

BRENDA3.1.1.3. 653.

Gene expression databases

ArrayExpressO13934.

Family and domain databases

InterProIPR002921. Lipase_3.
[Graphical view]
PfamPF01764. Lipase_3. 1 hit.
[Graphical view]
PROSITEPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATG15_SCHPO
AccessionPrimary (citable) accession number: O13934
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: January 1, 1998
Last modified: January 19, 2010
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents