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UniProtKB/Swiss-Prot entry P38862


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

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Entry information
Entry name ATG7_YEAST
Primary accession number P38862
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 74)
Name and origin of the protein
Protein name Autophagy-related protein 7
Synonyms Autophagy-related E1-like-activating enzyme ATG7
Cytoplasm to vacuole targeting protein 2
ATG12-activating E2-like enzyme
Gene name
Name: ATG7
Synonyms: APG7, CVT2
OrderedLocusNames: YHR171W
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.
STRAIN=ATCC 26109 / X2180;
DOI=10.1038/26506; PubMed=9759731 [NCBI, ExPASy, EBI, Israel, Japan]
Mizushima N., Noda T., Yoshimori T., Tanaka Y., Ishii T., George M.D., Klionsky D.J., Ohsumi M., Ohsumi Y.;
"A protein conjugation system essential for autophagy.";
Nature 395:395-398(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
DOI=10.1126/science.8091229; PubMed=8091229 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.";
Science 265:2077-2082(1994).
[3]
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).
[4]
FUNCTION.
DOI=10.1083/jcb.131.3.591; PubMed=7593182 [NCBI, ExPASy, EBI, Israel, Japan]
Harding T.M., Morano K.A., Scott S.V., Klionsky D.J.;
"Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway.";
J. Cell Biol. 131:591-602(1995).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10233148 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J., Dalton V.M., Eggerton K.P., Scott S.V., Klionsky D.J.;
"Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways.";
Mol. Biol. Cell 10:1337-1351(1999).
[6]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG12, AND MUTAGENESIS OF GLY-333 AND CYS-507.
PubMed=10233150 [NCBI, ExPASy, EBI, Israel, Japan]
Tanida I., Mizushima N., Kiyooka M., Ohsumi M., Ueno T., Ohsumi Y., Kominami E.;
"Apg7p/Cvt2p: a novel protein-activating enzyme essential for autophagy.";
Mol. Biol. Cell 10:1367-1379(1999).
[7]
FUNCTION, INTERACTION WITH ATG8, AND MUTAGENESIS OF GLY-333 AND CYS-507.
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).
[8]
HOMODIMERIZATION, AND INTERACTION WITH ATG3; ATG8 AND ATG12.
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).
[9]
FUNCTION.
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).
[10]
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).
[11]
FUNCTION.
DOI=10.1016/S0014-5793(03)00899-8; PubMed=12965207 [NCBI, ExPASy, EBI, Israel, Japan]
Yamazaki-Sato H., Tanida I., Ueno T., Kominami E.;
"The carboxyl terminal 17 amino acids within Apg7 are essential for Apg8 lipidation, but not for Apg12 conjugation.";
FEBS Lett. 551:71-77(2003).
[12]
FUNCTION, AND MUTAGENESIS OF CYS-507.
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: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes.
  • SUBUNIT: Homodimer. Interacts with ATG8 through a thioester bond between Cys-507 and the C-terminal 'Gly-116' of ATG8 and with ATG12 through a thioester bond between Cys-507 and the C-terminal 'Gly-186' of ATG12. Interacts also with ATG3.
  • INTERACTION:
    Self; NbExp=1; IntAct=EBI-2677, EBI-2677;
    P38316:ATG12; NbExp=3; IntAct=EBI-2677, EBI-2692;
    P40344:ATG3; NbExp=3; IntAct=EBI-2677, EBI-3381;
    P38182:ATG8; NbExp=2; IntAct=EBI-2677, EBI-2684;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • DOMAIN: The C-terminal 40 residues are required for homodimerization, as well as the interactions with ATG3, ATG8 and ATG12; and the C-terminal 17 residues are required for the ATG8 lipidation.
  • DOMAIN: The GxGxxG motif is important for the function, possibly through binding with ATP.
  • SIMILARITY: Belongs to the ATG7 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
AB017925; BAA33474.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00027; AAB68016.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S48910; S48910.
RefSeq NP_012041.1; -.
3D structure databases
HSSP P12282; 1JWA. [HSSP ENTRY / PDB]
ModBase P38862.
Protein-protein interaction databases
DIP DIP:1196N; -.
IntAct P38862; 7.
Organism-specific databases
CYGD YHR171w; -.
SGD S000001214; ATG7.
Yeast-GFP YHR171W.
Gene expression databases
GermOnline YHR171W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from SGD).
GO:0016020; Cellular component: membrane (inferred from direct assay from SGD).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0000407; Cellular component: pre-autophagosomal structure (inferred from direct assay from SGD).
GO:0019778; Molecular function: APG12 activating enzyme activity (inferred from mutant phenotype from SGD).
GO:0019779; Molecular function: APG8 activating enzyme activity (inferred from mutant phenotype from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
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:0016236; Biological process: macroautophagy (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:0032446; Biological process: protein modification by small protein conjugation (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR006285; E1-like_Apg7.
IPR016040; NAD(P)-bd_dom.
IPR000594; ThiF_NAD_FAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00899; ThiF; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01381; E1_like_apg7; 1.
Genome annotation databases
Ensembl YHR171W; Saccharomyces cerevisiae. [Contig view]
GeneID 856576; -.
GenomeReviews U00093_GR; YHR171W.
KEGG sce:YHR171W; -.
NMPDR fig|4932.3.peg.3206; -.
Phylogenomic databases
HOGENOM P38862; -.
OMA P38862; GHTIDEK.
Other
NextBio 982432; -.
ProtoNet P38862.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Autophagy; Complete proteome; Cytoplasm; Protein transport; Transport; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   630  630     Autophagy-related protein 7. PRO_0000212822
REGION   591   630  40     Homodimerization. 
MOTIF   331   336  6     GXGXXG motif. 
ACT_SITE   507   507        Glycyl thioester intermediate (Probable). 
MUTAGEN   333   333        G->A: Loss of interaction with ATG8 and ATG12, and no more ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. 
MUTAGEN   507   507        C->A: Loss of interaction with ATG8 and ATG12 and no more formation of ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. 
MUTAGEN   507   507        C->S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG7 (E1-like enzyme) and ATG8 (substrate) or between ATG7 and ATG12 (substrate), a stable complex with an O-ester bond is formed. No more formation of ATG12-ATG5 conjugate. 
Sequence information
Length: 630 AA [This is the length of the unprocessed precursor] Molecular weight: 71428 Da [This is the MW of the unprocessed precursor] CRC64: 561EEC94F0ED57F5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSERVLSYA PAFKSFLDTS FFQELSRLKL DVLKLDSTCQ PLTVNLDLHN IPKSADQVPL 

        70         80         90        100        110        120 
FLTNRSFEKH NNKRTNEVPL QGSIFNFNVL DEFKNLDKQL FLHQRALECW EDGIKDINKC 

       130        140        150        160        170        180 
VSFVIISFAD LKKYRFYYWL GVPCFQRPSS TVLHVRPEPS LKGLFSKCQK WFDVNYSKWV 

       190        200        210        220        230        240 
CILDADDEIV NYDKCIIRKT KVLAIRDTST MENVPSALTK NFLSVLQYDV PDLIDFKLLI 

       250        260        270        280        290        300 
IRQNEGSFAL NATFASIDPQ SSSSNPDMKV SGWERNVQGK LAPRVVDLSS LLDPLKIADQ 

       310        320        330        340        350        360 
SVDLNLKLMK WRILPDLNLD IIKNTKVLLL GAGTLGCYVS RALIAWGVRK ITFVDNGTVS 

       370        380        390        400        410        420 
YSNPVRQALY NFEDCGKPKA ELAAASLKRI FPLMDATGVK LSIPMIGHKL VNEEAQHKDF 

       430        440        450        460        470        480 
DRLRALIKEH DIIFLLVDSR ESRWLPSLLS NIENKTVINA ALGFDSYLVM RHGNRDEQSS 

       490        500        510        520        530        540 
KQLGCYFCHD VVAPTDSLTD RTLDQMCTVT RPGVAMMASS LAVELMTSLL QTKYSGSETT 

       550        560        570        580        590        600 
VLGDIPHQIR GFLHNFSILK LETPAYEHCP ACSPKVIEAF TDLGWEFVKK ALEHPLYLEE 

       610        620        630 
ISGLSVIKQE VERLGNDVFE WEDDESDEIA 

P38862 in FASTA format

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