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Protein

Ubiquitin-like modifier-activating enzyme atg7

Gene

ATG7

Organism
Arabidopsis thaliana (Mouse-ear cress)
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. Involved in the senescence process.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei558 – 5581Glycyl thioester intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

  • autophagy Source: TAIR
  • cellular response to nitrogen starvation Source: GO_Central
  • C-terminal protein lipidation Source: GO_Central
  • defense response to fungus Source: TAIR
  • late nucleophagy Source: GO_Central
  • leaf senescence Source: TAIR
  • macroautophagy Source: GO_Central
  • mitochondrion degradation Source: GO_Central
  • piecemeal microautophagy of nucleus Source: GO_Central
  • protein catabolic process Source: GO_Central
  • protein lipidation Source: TAIR
  • protein modification by small protein conjugation Source: GO_Central
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme atg7
Alternative name(s):
ATG12-activating enzyme E1 atg7
Autophagy-related protein 7
Short name:
AtAPG7
Gene namesi
Name:ATG7
Synonyms:APG7
Ordered Locus Names:At5g45900
ORF Names:K15I22.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G45900.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 697697Ubiquitin-like modifier-activating enzyme atg7PRO_0000286939Add
BLAST

Proteomic databases

PaxDbiQ94CD5.
PRIDEiQ94CD5.

Expressioni

Tissue specificityi

Constitutively expressed (at protein level).1 Publication

Developmental stagei

Up-regulated during leaf senescence.1 Publication

Gene expression databases

GenevestigatoriQ94CD5.

Interactioni

Subunit structurei

Homodimer. Interacts with ATG8 through a thioester bond between Cys-558 and the C-terminal glycine of ATG8 and with ATG12 through a thioester bond between Cys-558 and the C-terminal glycine of ATG12. Interacts also with ATG3 (By similarity).By similarity

Protein-protein interaction databases

BioGridi19879. 4 interactions.
IntActiQ94CD5. 3 interactions.
MINTiMINT-8414464.
STRINGi3702.AT5G45900.1-P.

Structurei

Secondary structure

1
697
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 203Combined sources
Helixi22 – 3413Combined sources
Turni35 – 384Combined sources
Beta strandi43 – 497Combined sources
Beta strandi61 – 633Combined sources
Helixi65 – 673Combined sources
Beta strandi86 – 9813Combined sources
Helixi99 – 1046Combined sources
Helixi108 – 12316Combined sources
Helixi126 – 1294Combined sources
Helixi131 – 1333Combined sources
Beta strandi137 – 1448Combined sources
Turni145 – 1484Combined sources
Beta strandi149 – 15911Combined sources
Beta strandi166 – 1727Combined sources
Helixi173 – 1764Combined sources
Helixi179 – 19416Combined sources
Beta strandi203 – 2097Combined sources
Beta strandi214 – 2174Combined sources
Helixi219 – 2213Combined sources
Helixi222 – 2254Combined sources
Beta strandi230 – 2378Combined sources
Helixi250 – 26112Combined sources
Beta strandi264 – 2718Combined sources
Turni280 – 2823Combined sources
Beta strandi284 – 2896Combined sources
Beta strandi304 – 3074Combined sources
Beta strandi317 – 3204Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VX8X-ray3.11A/D7-325[»]
ProteinModelPortaliQ94CD5.
SMRiQ94CD5. Positions 7-674.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni656 – 69742HomodimerizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi364 – 3696GXGXXG motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi685 – 6928Poly-Asp

Domaini

The C-terminal residues are required for homodimerization, as well as the interactions with ATG3, ATG8 and ATG12.By similarity
The GxGxxG motif is important for the function, possibly through binding with ATP.

Sequence similaritiesi

Belongs to the ATG7 family.Curated

Phylogenomic databases

eggNOGiCOG0476.
HOGENOMiHOG000162379.
InParanoidiQ94CD5.
KOiK08337.
OMAiEGYNMSI.
PhylomeDBiQ94CD5.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006285. Atg7.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PANTHERiPTHR10953:SF3. PTHR10953:SF3. 1 hit.
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
TIGRFAMsiTIGR01381. E1_like_apg7. 1 hit.

Sequencei

Sequence statusi: Complete.

Q94CD5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKETPAII LQFAPLNSSV DEGFWHSFSS LKLDKLGIDD SPISITGFYG
60 70 80 90 100
PCGHPQVSNH LTLLSESLPL DEQSLIASTS HGNRNKCPVP GILYNTNTVE
110 120 130 140 150
SFNKLDKQSL LKAEANKIWE DIQSGKALED PSVLPRFLVI SFADLKKWSF
160 170 180 190 200
RYWFAFPAFV LDPPVSLIEL KPASEYFSSE EAESVSAACN DWRDSDLTTD
210 220 230 240 250
VPFFLVSVSS DSKASIRHLK DLEACQGDHQ KLLFGFYDPC HLPSNPGWPL
260 270 280 290 300
RNYLALIRSR WNLETVWFFC YRESRGFADL NLSLVGQASI TLSSGESAET
310 320 330 340 350
VPNSVGWELN KGKRVPRSIS LANSMDPTRL AVSAVDLNLK LMRWRALPSL
360 370 380 390 400
NLNVLSSVKC LLLGAGTLGC QVARTLMGWG IRNITFVDYG KVAMSNPVRQ
410 420 430 440 450
SLYNFEDCLG RGEFKAVAAV KSLKQIFPAM ETSGVVMAIP MPGHPISSQE
460 470 480 490 500
EDSVLGDCKR LSELIESHDA VFLLTDTRES RWLPSLLCAN ANKIAINAAL
510 520 530 540 550
GFDSYMVMRH GAGPTSLSDD MQNLDINKTN TQRLGCYFCN DVVAPQDSMT
560 570 580 590 600
DRTLDQQCTV TRPGLAPIAG ALAVELLVGV LQHPLGINAK GDNSSLSNTG
610 620 630 640 650
NNDDSPLGIL PHQIRGSVSQ FSQITLLGQA SNSCTACSET VISEYRERGN
660 670 680 690
SFILEAINHP TYLEDLTGLT ELKKAANSFN LDWEDDDTDD DDVAVDL
Length:697
Mass (Da):76,522
Last modified:December 1, 2001 - v1
Checksum:iF9855AED0F9007FB
GO

Sequence cautioni

The sequence BAB09318.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF492761 mRNA. Translation: AAM70190.1.
AB073173 mRNA. Translation: BAB88385.1.
AB016870 Genomic DNA. Translation: BAB09318.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED95313.1.
AY034945 mRNA. Translation: AAK59451.1.
AY150456 mRNA. Translation: AAN12897.1.
RefSeqiNP_568652.1. NM_123958.2.
UniGeneiAt.7711.

Genome annotation databases

EnsemblPlantsiAT5G45900.1; AT5G45900.1; AT5G45900.
GeneIDi834630.
KEGGiath:AT5G45900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF492761 mRNA. Translation: AAM70190.1.
AB073173 mRNA. Translation: BAB88385.1.
AB016870 Genomic DNA. Translation: BAB09318.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED95313.1.
AY034945 mRNA. Translation: AAK59451.1.
AY150456 mRNA. Translation: AAN12897.1.
RefSeqiNP_568652.1. NM_123958.2.
UniGeneiAt.7711.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VX8X-ray3.11A/D7-325[»]
ProteinModelPortaliQ94CD5.
SMRiQ94CD5. Positions 7-674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19879. 4 interactions.
IntActiQ94CD5. 3 interactions.
MINTiMINT-8414464.
STRINGi3702.AT5G45900.1-P.

Proteomic databases

PaxDbiQ94CD5.
PRIDEiQ94CD5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G45900.1; AT5G45900.1; AT5G45900.
GeneIDi834630.
KEGGiath:AT5G45900.

Organism-specific databases

TAIRiAT5G45900.

Phylogenomic databases

eggNOGiCOG0476.
HOGENOMiHOG000162379.
InParanoidiQ94CD5.
KOiK08337.
OMAiEGYNMSI.
PhylomeDBiQ94CD5.

Miscellaneous databases

PROiQ94CD5.

Gene expression databases

GenevestigatoriQ94CD5.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006285. Atg7.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PANTHERiPTHR10953:SF3. PTHR10953:SF3. 1 hit.
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
TIGRFAMsiTIGR01381. E1_like_apg7. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The APG8/12-activating enzyme APG7 is required for proper nutrient recycling and senescence in Arabidopsis thaliana."
    Doelling J.H., Walker J.M., Friedman E.M., Thompson A.R., Vierstra R.D.
    J. Biol. Chem. 277:33105-33114(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  2. "Leaf senescence and starvation-induced chlorosis are accelerated by the disruption of an Arabidopsis autophagy gene."
    Hanaoka H., Noda T., Shirano Y., Kato T., Hayashi H., Shibata D., Tabata S., Ohsumi Y.
    Plant Physiol. 129:1181-1193(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE, GENE FAMILY.
  3. "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones."
    Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S.
    DNA Res. 5:379-391(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiATG7_ARATH
AccessioniPrimary (citable) accession number: Q94CD5
Secondary accession number(s): Q9FJ46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: December 1, 2001
Last modified: February 4, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.