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Q5B0L1 (ATG15_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:AN5919
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence caution

The sequence EAA57782.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Putative lipase atg15
PRO_0000090368

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4121Helical; Signal-anchor for type II membrane protein; Potential
Topological domain42 – 603562Lumenal Potential
Compositional bias472 – 576105Thr-rich

Sites

Active site3211Charge relay system By similarity

Amino acid modifications

Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation2011N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation2811N-linked (GlcNAc...) Potential
Glycosylation3051N-linked (GlcNAc...) Potential
Glycosylation4671N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5B0L1 [UniParc].

Last modified October 19, 2011. Version 2.
Checksum: 38A12630C4010864

FASTA60365,804
        10         20         30         40         50         60 
MDQPHRRTRK WHLMDLSVST LLMSLALVLP SCVSAYQPVY FRSQEATPFI PPQVPSADPQ 

        70         80         90        100        110        120 
SLSGTHEFTL RHIVQRGAYE YPELHRRLDI KPNTQLRTVS EDGIEDNEPA VFNVPFVASS 

       130        140        150        160        170        180 
EPVTIERLAD RRLSVIEEHL AAARSAGSAV TLSSSQWTKD TLAGPNVTDK KTILTFAKMT 

       190        200        210        220        230        240 
ANDYIEVPGT EDWQDINGKL NYSTSFGWQN DGLRGHIYAD DTNSTIVISL KGTSPALFDG 

       250        260        270        280        290        300 
AGTTTNDKVN DNLYFSCCCG QGGSYLWREV CDCQKSAFNA NLTCIIEAMN DENRYYRASL 

       310        320        330        340        350        360 
DLYSNVTELY PNANVWLTGH SLGGAMASLL GLTFGLPVVT FEAVPEALPA ARLGLPTPPG 

       370        380        390        400        410        420 
YNPALPQARK FTGAYHFGHT ADPVYMGTCN GVSSVCTWGG YAMESACHTG QMCVYDTVAD 

       430        440        450        460        470        480 
KGWRVAIGTH RIKAVISDVI EVYDDLPQCA PEEECYDCEL WKFFRSNGSE ITTTSSTTTT 

       490        500        510        520        530        540 
STITTSTRTT TCKTPGWWGC LDDSTTTDPP TTTTTTSSTC KTPGWFGCKD PTSTTATTTT 

       550        560        570        580        590        600 
EAPTTTTTCK DPGWFGCRDP TSPTTSTAPQ TSTCETPGFF WGCYDTQTAV DHLITPAPIL 


IDL

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000101 Genomic DNA. Translation: EAA57782.1. Different initiation.
BN001301 Genomic DNA. Translation: CBF70571.1.
RefSeqXP_663523.1. XM_658431.1.

3D structure databases

ProteinModelPortalQ5B0L1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5B0L1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2870991.
KEGGani:AN5919.2.

Phylogenomic databases

OrthoDBEOG4F7RV2.
PhylomeDBQ5B0L1.

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_EMENI
AccessionPrimary (citable) accession number: Q5B0L1
Secondary accession number(s): C8V3K5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 19, 2011
Last modified: January 25, 2012
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents