ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P40344


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ATG3_YEAST
Primary accession number P40344
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 75)
Name and origin of the protein
Protein name Autophagy-related protein 3
Synonym Autophagy-related E2-like conjugation enzyme ATG3
Gene name
Name: ATG3
Synonyms: APG3, AUT1
OrderedLocusNames: YNR007C
ORFNames: N2040
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=9023185 [NCBI, ExPASy, EBI, Israel, Japan]
Schlumpberger M., Schaeffeler E., Straub M., Bredschneider M., Wolf D.H., Thumm M.;
"AUT1, a gene essential for autophagocytosis in the yeast Saccharomyces cerevisiae.";
J. Bacteriol. 179:1068-1076(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/yea.320101013; PubMed=7900425 [NCBI, ExPASy, EBI, Israel, Japan]
Verhasselt P., Aert R., Voet M., Volckaert G.;
"Twelve open reading frames revealed in the 23.6 kb segment flanking the centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
Yeast 10:1355-1361(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan]
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
FUNCTION.
DOI=10.1016/0014-5793(93)80398-E; PubMed=8224160 [NCBI, ExPASy, EBI, Israel, Japan]
Tsukada M., Ohsumi Y.;
"Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae.";
FEBS Lett. 333:169-174(1993).
[5]
FUNCTION.
DOI=10.1016/0014-5793(94)00672-5; PubMed=8050581 [NCBI, ExPASy, EBI, Israel, Japan]
Thumm M., Egner R., Koch B., Schlumpberger M., Straub M., Veenhuis M., Wolf D.H.;
"Isolation of autophagocytosis mutants of Saccharomyces cerevisiae.";
FEBS Lett. 349:275-280(1994).
[6]
FUNCTION, INTERACTION WITH ATG8, AND MUTAGENESIS OF CYS-234.
DOI=10.1038/35044114; PubMed=11100732 [NCBI, ExPASy, EBI, Israel, Japan]
Ichimura Y., Kirisako T., Takao T., Satomi Y., Shimonishi Y., Ishihara N., Mizushima N., Tanida I., Kominami E., Ohsumi M., Noda T., Ohsumi Y.;
"A ubiquitin-like system mediates protein lipidation.";
Nature 408:488-492(2000).
[7]
INTERACTION WITH ATG7.
DOI=10.1074/jbc.M007737200; PubMed=11139573 [NCBI, ExPASy, EBI, Israel, Japan]
Komatsu M., Tanida I., Ueno T., Ohsumi M., Ohsumi Y., Kominami E.;
"The C-terminal region of an Apg7p/Cvt2p is required for homodimerization and is essential for its E1 activity and E1-E2 complex formation.";
J. Biol. Chem. 276:9846-9854(2001).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1083/jcb.152.1.51; PubMed=11149920 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J., Huang W.-P., Klionsky D.J.;
"Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation complex.";
J. Cell Biol. 152:51-64(2001).
[9]
NOMENCLATURE.
DOI=10.1016/S1534-5807(03)00296-X; PubMed=14536056 [NCBI, ExPASy, EBI, Israel, Japan]
Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y., Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
"A unified nomenclature for yeast autophagy-related genes.";
Dev. Cell 5:539-545(2003).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
FUNCTION, AND MUTAGENESIS OF CYS-234.
DOI=10.1074/jbc.M405860200; PubMed=15277523 [NCBI, ExPASy, EBI, Israel, Japan]
Ichimura Y., Imamura Y., Emoto K., Umeda M., Noda T., Ohsumi Y.;
"In vivo and in vitro reconstitution of atg8 conjugation essential for autophagy.";
J. Biol. Chem. 279:40584-40592(2004).
Comments
  • FUNCTION: E2 conjugating enzyme responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt).
  • SUBUNIT: Interacts with ATG8 through an intermediate thioester bond between Cys-234 and the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme.
  • INTERACTION:
    Self; NbExp=1; IntAct=EBI-3381, EBI-3381;
    P38862:ATG7; NbExp=3; IntAct=EBI-3381, EBI-2677;
    P38182:ATG8; NbExp=1; IntAct=EBI-3381, EBI-2684;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • MISCELLANEOUS: Present with 3610 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the ATG3 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X77395; CAA54575.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71622; CAA96284.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S45130; S45130.
RefSeq NP_014404.1; -.
3D structure databases
PDB
2DYT; X-ray; 2.50 A; A=1-310.[ExPASy / RCSB / EBI]
PDBsum 2DYT; -.
ModBase P40344.
Protein-protein interaction databases
DIP DIP:1190N; -.
IntAct P40344; 13.
Organism-specific databases
CYGD YNR007c; -.
SGD S000005290; ATG3.
Yeast-GFP YNR007C.
Gene expression databases
ArrayExpress P40344; -.
GermOnline YNR007C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0019776; Molecular function: Atg8 ligase activity (inferred from mutant phenotype from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0000045; Biological process: autophagic vacuole formation (inferred from mutant phenotype from UniProtKB).
GO:0006501; Biological process: C-terminal protein lipidation (inferred from direct assay from SGD).
GO:0032258; Biological process: CVT pathway (inferred from mutant phenotype from SGD).
GO:0019941; Biological process: modification-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0034727; Biological process: piecemeal microautophagy of nucleus (inferred from mutant phenotype from SGD).
GO:0006612; Biological process: protein targeting to membrane (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR007135; Autophagy-rel_prot_3.
IPR019461; Autophagy-rel_prot_3_C.
IPR007134; Autophagy-rel_prot_3_N.
Graphical view of domain structure.
Pfam PF03987; Autophagy_act_C; 1.
PF10381; Autophagy_Cterm; 1.
PF03986; Autophagy_N; 1.
Pfam graphical view of domain structure.
Proteomic databases
PeptideAtlas P40344; -.
Genome annotation databases
Ensembl YNR007C; Saccharomyces cerevisiae. [Contig view]
GeneID 855741; -.
GenomeReviews Y13139_GR; YNR007C.
KEGG sce:YNR007C; -.
NMPDR fig|4932.3.peg.5484; -.
Phylogenomic databases
HOGENOM P40344; -.
OMA P40344; CKHANVM.
Other
NextBio 980136; -.
ProtoNet P40344.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Autophagy; Complete proteome; Cytoplasm; Protein transport; Transport; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   310  310     Autophagy-related protein 3. PRO_0000213586
ACT_SITE   234   234        Glycyl thioester intermediate (Potential). 
MUTAGEN   234   234        C->A: Loss of interaction with ATG8 and defect in autophagy and Cvt pathway. 
MUTAGEN   234   234        C->S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG3 (E2-like enzyme) and ATG8 (substrate), a stable complex with an O-ester bond is formed. 
HELIX   22    25  4      
HELIX   30    43  14      
STRAND   69    76  8      
TURN   80    82  3      
HELIX   130   141  12      
STRAND   167   176  10      
TURN   177   180  4      
STRAND   181   190  10      
HELIX   198   202  5      
TURN   207   209  3      
HELIX   210   213  4      
STRAND   214   218  5      
STRAND   222   224  3      
STRAND   227   231  5      
STRAND   235   237  3      
HELIX   239   264  26      
HELIX   283   285  3      
HELIX   286   297  12      
Sequence information
Length: 310 AA [This is the length of the unprocessed precursor] Molecular weight: 35887 Da [This is the MW of the unprocessed precursor] CRC64: 52CCFB216B18CF0C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIRSTLSSWR EYLTPITHKS TFLTTGQITP EEFVQAGDYL CHMFPTWKWN EESSDISYRD 

        70         80         90        100        110        120 
FLPKNKQFLI IRKVPCDKRA EQCVEVEGPD VIMKGFAEDG DEDDVLEYIG SETEHVQSTP 

       130        140        150        160        170        180 
AGGTKDSSID DIDELIQDME IKEEDENDDT EEFNAKGGLA KDMAQERYYD LYIAYSTSYR 

       190        200        210        220        230        240 
VPKMYIVGFN SNGSPLSPEQ MFEDISADYR TKTATIEKLP FYKNSVLSVS IHPCKHANVM 

       250        260        270        280        290        300 
KILLDKVRVV RQRRRKELQE EQELDGVGDW EDLQDDIDDS LRVDQYLIVF LKFITSVTPS 

       310 
IQHDYTMEGW 

P40344 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!