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Reviewed, UniProtKB/Swiss-Prot Q9D906 (ATG7_MOUSE)

Last modified February 9, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Autophagy-related protein 7
Alternative name(s):
    APG7-like
      Short name=mAGP7
    Ubiquitin-activating enzyme E1-like protein
Gene names
Name: Atg7
Synonyms: Apg7l
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length698 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Functions as an E1 enzyme essential for multisubstrates such as GABARAPL1 and ATG12. Forms intermediate conjugates with GABARAPL1 (GABARAPL2, GABARAP or MAP1ALC3). Formation of the final GABARAPL1-PE conjugate is essential for autophagy. Ref.1

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. Ref.1 Ref.4

Subcellular location

Cytoplasm Probable.

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.

Sequence similarities

Belongs to the ATG7 family.

Ontologies

Keywords
   Biological processAutophagy
Protein transport
Transport
Ubl conjugation pathway
   Cellular componentCytoplasm
   PTMAcetylation
Gene Ontology (GO)
   Biological processadult walking behavior

Inferred from mutant phenotype. Source: MGI

autophagy

Inferred from mutant phenotype. Source: MGI

cardiac muscle cell development

Inferred from mutant phenotype. Source: MGI

cellular amino acid metabolic process

Inferred from mutant phenotype. Source: MGI

cerebellar Purkinje cell layer development

Inferred from mutant phenotype. Source: MGI

cerebral cortex development

Inferred from mutant phenotype. Source: MGI

liver development

Inferred from mutant phenotype. Source: MGI

membrane organization

Inferred from mutant phenotype. Source: MGI

modification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of apoptosis

Inferred from mutant phenotype. Source: MGI

neurological system process

Inferred from mutant phenotype. Source: MGI

neuron projection development

Inferred from mutant phenotype. Source: MGI

organelle organization

Inferred from mutant phenotype. Source: MGI

positive regulation of protein modification process Ref.4

Inferred from direct assay. Source: MGI

post-embryonic development

Inferred from mutant phenotype. Source: MGI

protein modification by small protein conjugation

Inferred from mutant phenotype. Source: MGI

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

pyramidal neuron development

Inferred from mutant phenotype. Source: MGI

regulation of protein ubiquitination

Inferred from mutant phenotype. Source: MGI

response to starvation

Inferred from mutant phenotype. Source: MGI

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding Ref.1 Ref.4

Inferred from physical interaction. Source: MGI

ubiquitin activating enzyme activity Ref.1

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 698698Autophagy-related protein 7
PRO_0000212807

Sites

Active site5671Glycyl thioester intermediate Potential

Amino acid modifications

Modified residue3021N6-acetyllysine By similarity

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
Q9D906-1 [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: 11890701] [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: 16141072] [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: 15489334] [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: 12482611] [Abstract]
Cited for: INTERACTION WITH ATG10 AND ATG12.
+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.
IPIIPI00463195.
RefSeqNP_083111.1.
UniGeneMm.275332

3D structure databases

SMRQ9D906. Positions 26-63, 345-592.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9D906.

Proteomic databases

PRIDEQ9D906.

Genome annotation databases

EnsemblENSMUST00000032457; ENSMUSP00000032457; ENSMUSG00000030314; Mus musculus. [Genome view]
GeneID74244.
KEGGmmu:74244.
UCSCuc009dhz.1. mouse.

Organism-specific databases

CTD74244.
MGIMGI:1921494. Atg7.

Phylogenomic databases

HOGENOMHBG619497.
HOVERGENQ9D906.
InParanoidQ9D906.
OMAANEIWES.
OrthoDBEOG9R7XXG.
PhylomeDBQ9D906.

Gene expression databases

ArrayExpressQ9D906.
BgeeQ9D906.
CleanExMM_ATG7.
GenevestigatorQ9D906.
GermOnlineENSMUSG00000030314. Mus musculus.

Family and domain databases

InterProIPR006285. E1-like_Apg7.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR000594. ThiF_NAD_FAD_bd.
[Graphical view]
PfamPF00899. ThiF. 1 hit.
[Graphical view]
TIGRFAMsTIGR01381. E1_like_apg7. 1 hit.
ProtoNetSearch...

Other Resources

NextBio340222.
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: February 9, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents