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Q9D906 (ATG7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Short name=APG7-like
Short name=mAGP7
Ubiquitin-activating enzyme E1-like protein
Gene names
Name:Atg7
Synonyms:Apg7l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length698 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 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Required 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. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Plays also a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Subunit structure

Homodimer. Interacts with ATG3 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5 By similarity. Forms intermediate conjugates with ATG8 family proteins such as GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, or GABARAPL1. Ref.1 Ref.4 Ref.7

Subcellular location

Cytoplasm By similarity. Preautophagosomal structure By similarity. Note: Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme. Ref.10

Tissue specificity

Widely expressed, especially in kidney, liver, lymph nodes and bone marrow. Ref.1

Domain

The C-terminal part of the protein is essential for the dimerization and interaction with ATG3 and ATG12 By similarity.

The N-terminal FAP motif (residues 11 to 13) is essential for the formation of the ATG89-PE and ATG5-ATG12 conjugates By similarity.

Post-translational modification

Acetylated by EP300 By similarity.

Disruption phenotype

Leads to hepatomegaly in liver and accumulation of abnormal organelles in hepatic cells. Ref.6

Sequence similarities

Belongs to the ATG7 family.

Ontologies

Keywords
   Biological processAutophagy
Protein transport
Transport
Ubl conjugation pathway
   Cellular componentCytoplasm
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from mutant phenotype PubMed 16625205. Source: MGI

autophagy

Inferred from mutant phenotype Ref.6PubMed 16885219PubMed 17450150Ref.8PubMed 20577052. Source: MGI

cardiac muscle cell development

Inferred from mutant phenotype PubMed 17450150. Source: MGI

cellular amino acid metabolic process

Inferred from mutant phenotype Ref.6. Source: MGI

central nervous system neuron axonogenesis

Inferred from mutant phenotype PubMed 20577052. Source: MGI

cerebellar Purkinje cell layer development

Inferred from mutant phenotype PubMed 16625205PubMed 20577052. Source: MGI

cerebral cortex development

Inferred from mutant phenotype PubMed 16625205. Source: MGI

liver development

Inferred from mutant phenotype Ref.6. Source: MGI

membrane organization

Inferred from mutant phenotype Ref.8. Source: MGI

mitochondrion organization

Inferred from mutant phenotype PubMed 21402742. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 16625205PubMed 17450150. Source: MGI

negative stranded viral RNA replication

Inferred from mutant phenotype PubMed 24550300. Source: MGI

neurological system process

Inferred from mutant phenotype PubMed 16625205. Source: MGI

neuron projection development

Inferred from mutant phenotype Ref.8. Source: MGI

organelle organization

Inferred from mutant phenotype Ref.6. Source: MGI

positive regulation of protein modification process

Inferred from direct assay Ref.4. Source: MGI

post-embryonic development

Inferred from mutant phenotype Ref.6PubMed 16625205. Source: MGI

protein catabolic process

Inferred from mutant phenotype Ref.6. Source: MGI

protein lipidation

Inferred from sequence orthology PubMed 12890687. Source: MGI

protein modification by small protein conjugation

Inferred from mutant phenotype Ref.6. Source: MGI

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

pyramidal neuron development

Inferred from mutant phenotype PubMed 16625205. Source: MGI

regulation of protein ubiquitination

Inferred from mutant phenotype PubMed 16625205. Source: MGI

response to starvation

Inferred from mutant phenotype Ref.6. Source: MGI

   Cellular_componentaxoneme

Inferred from direct assay Ref.10. Source: UniProtKB

pre-autophagosomal structure

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionAtg12 activating enzyme activity

Inferred from mutant phenotype Ref.13. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1Ref.4. Source: MGI

ubiquitin activating enzyme activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 698698Ubiquitin-like modifier-activating enzyme ATG7
PRO_0000212807

Regions

Motif11 – 133FAP motif

Sites

Active site5671Glycyl thioester intermediate Probable

Experimental info

Mutagenesis5671C → S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG7 (E1-like enzyme) and GABARAPL1 (MAP1LC3, GABARAP or GABARAPL; substrates), a stable complex with an O-ester bond is formed. Ref.1
Sequence conflict221F → L in BAC10416. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D906 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 79D94EA7464C6ADB

FASTA69877,520
        10         20         30         40         50         60 
MGDPGLAKLQ FAPFNSALDV GFWHELTQKK LNEYRLDEAP KDIKGYYYNG DSAGLPTRLT 

        70         80         90        100        110        120 
LEFSAFDMSA STPAHCCPAM GTLHNTNTLE AFKTADKKLL LEQSANEIWE AIKSGAALEN 

       130        140        150        160        170        180 
PMLLNKFLLL TFADLKKYHF YYWFCCPALC LPESIPLIRG PVSLDQRLSP KQIQALEHAY 

       190        200        210        220        230        240 
DDLCRAEGVT ALPYFLFKYD DDTVLVSLLK HYSDFFQGQR TKITVGVYDP CNLAQYPGWP 

       250        260        270        280        290        300 
LRNFLVLAAH RWSGSFQSVE VLCFRDRTMQ GARDVTHSII FEVKLPEMAF SPDCPKAVGW 

       310        320        330        340        350        360 
EKNQKGGMGP RMVNLSGCMD PKRLAESSVD LNLKLMCWRL VPTLDLDKVV SVKCLLLGAG 

       370        380        390        400        410        420 
TLGCNVARTL MGWGVRHVTF VDNAKISYSN PVRQPLYEFE DCLGGGKPKA LAAAERLQKI 

       430        440        450        460        470        480 
FPGVNARGFN MSIPMPGHPV NFSDVTMEQA RRDVEQLEQL IDNHDVIFLL MDTRESRWLP 

       490        500        510        520        530        540 
TVIAASKRKL VINAALGFDT FVVMRHGLKK PKQQGAGDLC PSHLVAPADL GSSLFANIPG 

       550        560        570        580        590        600 
YKLGCYFCND VVAPGDSTRD RTLDQQCTVS RPGLAVIAGA LAVELMVSVL QHPEGGYAIA 

       610        620        630        640        650        660 
SSSDDRMNEP PTSLGLVPHQ IRGFLSRFDN VLPVSLAFDK CTACSPKVLD QYEREGFTFL 

       670        680        690 
AKVFNSSHSF LEDLTGLTLL HQETQAAEIW DMSDEETV 

« Hide

References

« Hide 'large scale' references
[1]"Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs."
Tanida I., Tanida-Miyake E., Nishitani T., Komatsu M., Yamazaki H., Ueno T., Kominami E.
Biochem. Biophys. Res. Commun. 292:256-262(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN GABARAPL1-ATG7 INTERMEDIATE CONJUGATE FORMATION, TISSUE SPECIFICITY, INTERACTION WITH ATG12, MUTAGENESIS OF CYS-567.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Pancreas, Spleen and Urinary bladder.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[4]"Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-mediated yeast two-hybrid method."
Mizushima N., Yoshimori T., Ohsumi Y.
FEBS Lett. 532:450-454(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG10 AND ATG12.
[5]"Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8."
Yu L., Alva A., Su H., Dutt P., Freundt E., Welsh S., Baehrecke E.H., Lenardo M.J.
Science 304:1500-1502(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice."
Komatsu M., Waguri S., Ueno T., Iwata J., Murata S., Tanida I., Ezaki J., Mizushima N., Ohsumi Y., Uchiyama Y., Kominami E., Tanaka K., Chiba T.
J. Cell Biol. 169:425-434(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]"Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation mediated by human Atg4B, Atg7 and Atg3."
Tanida I., Sou Y.S., Minematsu-Ikeguchi N., Ueno T., Kominami E.
FEBS J. 273:2553-2562(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GABARAPL1.
[8]"Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration."
Komatsu M., Wang Q.J., Holstein G.R., Friedrich V.L. Jr., Iwata J., Kominami E., Chait B.T., Tanaka K., Yue Z.
Proc. Natl. Acad. Sci. U.S.A. 104:14489-14494(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation."
Zhang J., Randall M.S., Loyd M.R., Dorsey F.C., Kundu M., Cleveland J.L., Ney P.A.
Blood 114:157-164(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Functional interaction between autophagy and ciliogenesis."
Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I., Codogno P., Satir B.H., Satir P., Cuervo A.M.
Nature 502:194-200(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Autophagy regulates adipose mass and differentiation in mice."
Singh R., Xiang Y., Wang Y., Baikati K., Cuervo A.M., Luu Y.K., Tang Y., Pessin J.E., Schwartz G.J., Czaja M.J.
J. Clin. Invest. 119:3329-3339(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Adipose-specific deletion of autophagy-related gene 7 (atg7) in mice reveals a role in adipogenesis."
Zhang Y., Goldman S., Baerga R., Zhao Y., Komatsu M., Jin S.
Proc. Natl. Acad. Sci. U.S.A. 106:19860-19865(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death."
Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C., Debnath J.
Cell 142:590-600(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Atg7 induces basal autophagy and rescues autophagic deficiency in CryABR120G cardiomyocytes."
Pattison J.S., Osinska H., Robbins J.
Circ. Res. 109:151-160(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"The autophagy protein Atg7 is essential for hematopoietic stem cell maintenance."
Mortensen M., Soilleux E.J., Djordjevic G., Tripp R., Lutteropp M., Sadighi-Akha E., Stranks A.J., Glanville J., Knight S., Jacobsen S.E., Kranc K.R., Simon A.K.
J. Exp. Med. 208:455-467(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Lack of intestinal epithelial atg7 affects paneth cell granule formation but does not compromise immune homeostasis in the gut."
Wittkopf N., Gunther C., Martini E., Waldner M., Amann K.U., Neurath M.F., Becker C.
Clin. Dev. Immunol. 2012:278059-278059(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Atg7 modulates p53 activity to regulate cell cycle and survival during metabolic stress."
Lee I.H., Kawai Y., Fergusson M.M., Rovira I.I., Bishop A.J., Motoyama N., Cao L., Finkel T.
Science 336:225-228(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB079385 mRNA. Translation: BAC10416.1.
AK007484 mRNA. Translation: BAB25060.1.
AK035604 mRNA. Translation: BAC29122.1.
AK161133 mRNA. Translation: BAE36208.1.
AK170769 mRNA. Translation: BAE42018.1.
AK172272 mRNA. Translation: BAE42917.1.
BC058597 mRNA. Translation: AAH58597.1.
CCDSCCDS39598.1.
RefSeqNP_001240646.1. NM_001253717.1.
NP_001240647.1. NM_001253718.1.
NP_083111.1. NM_028835.4.
XP_006506772.1. XM_006506709.1.
XP_006506773.1. XM_006506710.1.
UniGeneMm.275332.

3D structure databases

ProteinModelPortalQ9D906.
SMRQ9D906. Positions 9-685.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid216602. 6 interactions.
IntActQ9D906. 2 interactions.
MINTMINT-4615793.

PTM databases

PhosphoSiteQ9D906.

Proteomic databases

MaxQBQ9D906.
PaxDbQ9D906.
PRIDEQ9D906.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032457; ENSMUSP00000032457; ENSMUSG00000030314.
ENSMUST00000182793; ENSMUSP00000138137; ENSMUSG00000030314.
ENSMUST00000182902; ENSMUSP00000138651; ENSMUSG00000030314.
GeneID74244.
KEGGmmu:74244.
UCSCuc009dhz.2. mouse.

Organism-specific databases

CTD10533.
MGIMGI:1921494. Atg7.

Phylogenomic databases

eggNOGCOG0476.
GeneTreeENSGT00390000017509.
HOGENOMHOG000162379.
HOVERGENHBG080877.
InParanoidQ9D906.
KOK08337.
OrthoDBEOG7X0VGG.
PhylomeDBQ9D906.
TreeFamTF105689.

Gene expression databases

BgeeQ9D906.
CleanExMM_ATG7.
GenevestigatorQ9D906.

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. SSF69572. 2 hits.
TIGRFAMsTIGR01381. E1_like_apg7. 1 hit.
ProtoNetSearch...

Other

ChiTaRSATG7. mouse.
NextBio340222.
PROQ9D906.
SOURCESearch...

Entry information

Entry nameATG7_MOUSE
AccessionPrimary (citable) accession number: Q9D906
Secondary accession number(s): Q3TCD9, Q8K4Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot