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P38862 (ATG7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-like modifier-activating enzyme ATG7
Alternative name(s):
ATG12-activating enzyme E1 ATG7
Autophagy-related protein 7
Cytoplasm to vacuole targeting protein 2
Gene names
Name:ATG7
Synonyms:APG7, CVT2
Ordered Locus Names:YHR171W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13

Subunit structure

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. Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm Ref.6 Ref.7.

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.

The GxGxxG motif is important for the function, possibly through binding with ATP.

Sequence similarities

Belongs to the ATG7 family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 630630Ubiquitin-like modifier-activating enzyme ATG7
PRO_0000212822

Regions

Region591 – 63040Homodimerization
Motif331 – 3366GXGXXG motif

Sites

Active site5071Glycyl thioester intermediate Probable

Experimental info

Mutagenesis3331G → A: Loss of interaction with ATG8 and ATG12, and no more ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. Ref.7 Ref.8
Mutagenesis5071C → A: Loss of interaction with ATG8 and ATG12 and no more formation of ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. Ref.7 Ref.8 Ref.13
Mutagenesis5071C → 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. Ref.7 Ref.8 Ref.13

Secondary structure

......................................................................................................................... 630
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38862 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 561EEC94F0ED57F5

FASTA63071,428
        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 

« Hide

References

« Hide 'large scale' references
[1]"A protein conjugation system essential for autophagy."
Mizushima N., Noda T., Yoshimori T., Tanaka Y., Ishii T., George M.D., Klionsky D.J., Ohsumi M., Ohsumi Y.
Nature 395:395-398(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: ATCC 26109 / X2180.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
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. expand/collapse author list , 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.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae."
Tsukada M., Ohsumi Y.
FEBS Lett. 333:169-174(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway."
Harding T.M., Morano K.A., Scott S.V., Klionsky D.J.
J. Cell Biol. 131:591-602(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways."
Kim J., Dalton V.M., Eggerton K.P., Scott S.V., Klionsky D.J.
Mol. Biol. Cell 10:1337-1351(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Apg7p/Cvt2p: a novel protein-activating enzyme essential for autophagy."
Tanida I., Mizushima N., Kiyooka M., Ohsumi M., Ueno T., Ohsumi Y., Kominami E.
Mol. Biol. Cell 10:1367-1379(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG12, MUTAGENESIS OF GLY-333 AND CYS-507.
[8]"A ubiquitin-like system mediates protein lipidation."
Ichimura Y., Kirisako T., Takao T., Satomi Y., Shimonishi Y., Ishihara N., Mizushima N., Tanida I., Kominami E., Ohsumi M., Noda T., Ohsumi Y.
Nature 408:488-492(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATG8, MUTAGENESIS OF GLY-333 AND CYS-507.
[9]"The C-terminal region of an Apg7p/Cvt2p is required for homodimerization and is essential for its E1 activity and E1-E2 complex formation."
Komatsu M., Tanida I., Ueno T., Ohsumi M., Ohsumi Y., Kominami E.
J. Biol. Chem. 276:9846-9854(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, INTERACTION WITH ATG3; ATG8 AND ATG12.
[10]"Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation complex."
Kim J., Huang W.-P., Klionsky D.J.
J. Cell Biol. 152:51-64(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"A unified nomenclature for yeast autophagy-related genes."
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.
Dev. Cell 5:539-545(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[12]"The carboxyl terminal 17 amino acids within Apg7 are essential for Apg8 lipidation, but not for Apg12 conjugation."
Yamazaki-Sato H., Tanida I., Ueno T., Kominami E.
FEBS Lett. 551:71-77(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"In vivo and in vitro reconstitution of atg8 conjugation essential for autophagy."
Ichimura Y., Imamura Y., Emoto K., Umeda M., Noda T., Ohsumi Y.
J. Biol. Chem. 279:40584-40592(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-507.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB017925 Genomic DNA. Translation: BAA33474.1.
U00027 Genomic DNA. Translation: AAB68016.1.
BK006934 Genomic DNA. Translation: DAA06864.1.
PIRS48910.
RefSeqNP_012041.1. NM_001179302.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LI5NMR-B601-630[»]
3RUIX-ray1.91A293-630[»]
3RUJX-ray2.10A1-294[»]
3T7EX-ray2.25A289-630[»]
3T7FX-ray1.89A1-289[»]
3T7GX-ray2.08A/B1-289[»]
3T7HX-ray1.60A/B1-289[»]
3VH1X-ray3.00A1-595[»]
3VH2X-ray3.30A1-613[»]
3VH3X-ray2.00A295-630[»]
3VH4X-ray2.65A295-630[»]
4GSJX-ray1.70A1-289[»]
4GSKX-ray2.90A/B1-613[»]
4GSLX-ray2.70A/B1-613[»]
ProteinModelPortalP38862.
SMRP38862. Positions 1-630.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1196N.
IntActP38862. 7 interactions.
MINTMINT-388374.
STRING4932.YHR171W.

Proteomic databases

PaxDbP38862.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR171W; YHR171W; YHR171W.
GeneID856576.
KEGGsce:YHR171W.

Organism-specific databases

CYGDYHR171w.
SGDS000001214. ATG7.

Phylogenomic databases

eggNOGCOG0476.
GeneTreeENSGT00390000017509.
HOGENOMHOG000162379.
KOK08337.
OMAPMIGHPV.
OrthoDBEOG476P7D.

Gene expression databases

GenevestigatorP38862.
GermOnlineYHR171W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR006285. Atg7.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PANTHERPTHR10953:SF3. PTHR10953:SF3. 1 hit.
PfamPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMSSF69572. MoeB. 1 hit.
TIGRFAMsTIGR01381. E1_like_apg7. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP38862.
NextBio982432.

Entry information

Entry nameATG7_YEAST
AccessionPrimary (citable) accession number: P38862
Secondary accession number(s): D3DLC0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 3, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families