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Protein

Ubiquitin-like modifier-activating enzyme ATG7

Gene

ATG7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Plays a role in the regulation of filamentous growth and chronological longevity.21 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei507Glycyl thioester intermediate1

GO - Molecular functioni

  • Atg12 activating enzyme activity Source: SGD
  • Atg8 activating enzyme activity Source: SGD

GO - Biological processi

  • autophagy Source: SGD
  • cellular response to nitrogen starvation Source: GO_Central
  • C-terminal protein lipidation Source: SGD
  • CVT pathway Source: SGD
  • late nucleophagy Source: SGD
  • macroautophagy Source: SGD
  • mitophagy Source: SGD
  • piecemeal microautophagy of nucleus Source: SGD
  • protein catabolic process Source: GO_Central
  • protein modification by small protein conjugation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-31205-MONOMER.
ReactomeiR-SCE-1632852. Macroautophagy.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ATG7
Synonyms:APG7, CVT2
Ordered Locus Names:YHR171W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR171W.
SGDiS000001214. ATG7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • extrinsic component of pre-autophagosomal structure membrane Source: UniProtKB
  • membrane Source: SGD
  • pre-autophagosomal structure Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi333G → A: Loss of interaction with ATG8 and ATG12, and no more ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. 2 Publications1
Mutagenesisi443R → A: Loss of interaction with ATG8. 1 Publication1
Mutagenesisi466S → A: Loss of interaction with ATG8; when associated with F-486 and A-490. 1 Publication1
Mutagenesisi486Y → F: Loss of interaction with ATG8; when associated with A-466 and A-490. 1 Publication1
Mutagenesisi490D → A: Loss of interaction with ATG8; when associated with A-466 and F-486. 1 Publication1
Mutagenesisi507C → A: Loss of interaction with ATG8 and ATG12 and no more formation of ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. 3 Publications1
Mutagenesisi507C → 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. 3 Publications1
Mutagenesisi550R → A: Loss of interaction with ATG8. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002128221 – 630Ubiquitin-like modifier-activating enzyme ATG7Add BLAST630

Proteomic databases

MaxQBiP38862.
PRIDEiP38862.
TopDownProteomicsiP38862.

Interactioni

Subunit structurei

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 ATG3.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATG12P383163EBI-2677,EBI-2692
ATG3P403444EBI-2677,EBI-3381
ATG8P381824EBI-2677,EBI-2684

Protein-protein interaction databases

BioGridi36605. 46 interactors.
DIPiDIP-1196N.
IntActiP38862. 6 interactors.
MINTiMINT-388374.

Structurei

Secondary structure

1630
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 17Combined sources6
Helixi19 – 29Combined sources11
Turni32 – 34Combined sources3
Beta strandi36 – 46Combined sources11
Beta strandi48 – 50Combined sources3
Beta strandi56 – 62Combined sources7
Helixi64 – 67Combined sources4
Beta strandi68 – 70Combined sources3
Beta strandi78 – 89Combined sources12
Helixi90 – 95Combined sources6
Helixi98 – 113Combined sources16
Helixi117 – 119Combined sources3
Beta strandi123 – 130Combined sources8
Turni131 – 134Combined sources4
Beta strandi135 – 148Combined sources14
Beta strandi151 – 157Combined sources7
Helixi159 – 164Combined sources6
Helixi165 – 174Combined sources10
Beta strandi179 – 183Combined sources5
Beta strandi189 – 191Combined sources3
Helixi194 – 200Combined sources7
Beta strandi202 – 206Combined sources5
Helixi219 – 229Combined sources11
Beta strandi235 – 241Combined sources7
Beta strandi243 – 245Combined sources3
Beta strandi248 – 256Combined sources9
Beta strandi263 – 265Combined sources3
Beta strandi269 – 273Combined sources5
Beta strandi279 – 281Combined sources3
Beta strandi284 – 287Combined sources4
Helixi289 – 291Combined sources3
Helixi294 – 312Combined sources19
Helixi319 – 323Combined sources5
Beta strandi326 – 330Combined sources5
Helixi334 – 345Combined sources12
Beta strandi350 – 354Combined sources5
Turni364 – 366Combined sources3
Helixi372 – 374Combined sources3
Beta strandi376 – 378Combined sources3
Helixi379 – 390Combined sources12
Beta strandi391 – 393Combined sources3
Beta strandi395 – 399Combined sources5
Helixi413 – 429Combined sources17
Beta strandi431 – 435Combined sources5
Beta strandi438 – 440Combined sources3
Helixi441 – 443Combined sources3
Helixi444 – 452Combined sources9
Beta strandi456 – 462Combined sources7
Beta strandi464 – 471Combined sources8
Helixi486 – 489Combined sources4
Beta strandi490 – 492Combined sources3
Beta strandi494 – 496Combined sources3
Turni498 – 500Combined sources3
Helixi504 – 508Combined sources5
Helixi513 – 529Combined sources17
Beta strandi537 – 540Combined sources4
Beta strandi547 – 552Combined sources6
Turni553 – 556Combined sources4
Beta strandi557 – 561Combined sources5
Turni570 – 572Combined sources3
Helixi574 – 583Combined sources10
Helixi585 – 593Combined sources9
Helixi595 – 602Combined sources8
Helixi604 – 612Combined sources9
Helixi616 – 618Combined sources3
Helixi627 – 629Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP38862.
SMRiP38862.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38862.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni591 – 630HomodimerizationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi331 – 336GXGXXG motif6

Domaini

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 similaritiesi

Belongs to the ATG7 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000017509.
HOGENOMiHOG000162379.
InParanoidiP38862.
KOiK08337.
OMAiSGWERNV.
OrthoDBiEOG092C0R44.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006285. Atg7.
IPR032197. Atg7_N.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PANTHERiPTHR10953:SF3. PTHR10953:SF3. 1 hit.
PfamiPF16420. ATG7_N. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
TIGRFAMsiTIGR01381. E1_like_apg7. 1 hit.

Sequencei

Sequence statusi: Complete.

P38862-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSERVLSYA PAFKSFLDTS FFQELSRLKL DVLKLDSTCQ PLTVNLDLHN
60 70 80 90 100
IPKSADQVPL FLTNRSFEKH NNKRTNEVPL QGSIFNFNVL DEFKNLDKQL
110 120 130 140 150
FLHQRALECW EDGIKDINKC VSFVIISFAD LKKYRFYYWL GVPCFQRPSS
160 170 180 190 200
TVLHVRPEPS LKGLFSKCQK WFDVNYSKWV CILDADDEIV NYDKCIIRKT
210 220 230 240 250
KVLAIRDTST MENVPSALTK NFLSVLQYDV PDLIDFKLLI IRQNEGSFAL
260 270 280 290 300
NATFASIDPQ SSSSNPDMKV SGWERNVQGK LAPRVVDLSS LLDPLKIADQ
310 320 330 340 350
SVDLNLKLMK WRILPDLNLD IIKNTKVLLL GAGTLGCYVS RALIAWGVRK
360 370 380 390 400
ITFVDNGTVS YSNPVRQALY NFEDCGKPKA ELAAASLKRI FPLMDATGVK
410 420 430 440 450
LSIPMIGHKL VNEEAQHKDF DRLRALIKEH DIIFLLVDSR ESRWLPSLLS
460 470 480 490 500
NIENKTVINA ALGFDSYLVM RHGNRDEQSS KQLGCYFCHD VVAPTDSLTD
510 520 530 540 550
RTLDQMCTVT RPGVAMMASS LAVELMTSLL QTKYSGSETT VLGDIPHQIR
560 570 580 590 600
GFLHNFSILK LETPAYEHCP ACSPKVIEAF TDLGWEFVKK ALEHPLYLEE
610 620 630
ISGLSVIKQE VERLGNDVFE WEDDESDEIA
Length:630
Mass (Da):71,428
Last modified:February 1, 1995 - v1
Checksum:i561EEC94F0ED57F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017925 Genomic DNA. Translation: BAA33474.1.
U00027 Genomic DNA. Translation: AAB68016.1.
BK006934 Genomic DNA. Translation: DAA06864.1.
PIRiS48910.
RefSeqiNP_012041.1. NM_001179302.1.

Genome annotation databases

EnsemblFungiiYHR171W; YHR171W; YHR171W.
GeneIDi856576.
KEGGisce:YHR171W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017925 Genomic DNA. Translation: BAA33474.1.
U00027 Genomic DNA. Translation: AAB68016.1.
BK006934 Genomic DNA. Translation: DAA06864.1.
PIRiS48910.
RefSeqiNP_012041.1. NM_001179302.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP38862.
SMRiP38862.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36605. 46 interactors.
DIPiDIP-1196N.
IntActiP38862. 6 interactors.
MINTiMINT-388374.

Proteomic databases

MaxQBiP38862.
PRIDEiP38862.
TopDownProteomicsiP38862.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR171W; YHR171W; YHR171W.
GeneIDi856576.
KEGGisce:YHR171W.

Organism-specific databases

EuPathDBiFungiDB:YHR171W.
SGDiS000001214. ATG7.

Phylogenomic databases

GeneTreeiENSGT00390000017509.
HOGENOMiHOG000162379.
InParanoidiP38862.
KOiK08337.
OMAiSGWERNV.
OrthoDBiEOG092C0R44.

Enzyme and pathway databases

BioCyciYEAST:G3O-31205-MONOMER.
ReactomeiR-SCE-1632852. Macroautophagy.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiP38862.
PROiP38862.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006285. Atg7.
IPR032197. Atg7_N.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PANTHERiPTHR10953:SF3. PTHR10953:SF3. 1 hit.
PfamiPF16420. ATG7_N. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
TIGRFAMsiTIGR01381. E1_like_apg7. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiATG7_YEAST
AccessioniPrimary (citable) accession number: P38862
Secondary accession number(s): D3DLC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.