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UniProtKB/Swiss-Prot entry Q9D906


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ATG7_MOUSE
Primary accession number Q9D906
Secondary accession numbers Q3TCD9 Q8K4Q5
Integrated into Swiss-Prot on March 29, 2005
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 51)
Name and origin of the protein
Protein name Autophagy-related protein 7
Synonyms APG7-like
Ubiquitin-activating enzyme E1-like protein
mAGP7
Gene name
Name: Atg7
Synonyms: Apg7l
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN GABARAPL1-ATG7 INTERMEDIATE CONJUGATE FORMATION, TISSUE SPECIFICITY, INTERACTION WITH ATG12, AND MUTAGENESIS OF CYS-567.
TISSUE=Brain;
DOI=10.1006/bbrc.2002.6645; PubMed=11890701 [NCBI, ExPASy, EBI, Israel, Japan]
Tanida I., Tanida-Miyake E., Nishitani T., Komatsu M., Yamazaki H., Ueno T., Kominami E.;
"Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs.";
Biochem. Biophys. Res. Commun. 292:256-262(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Pancreas, Spleen, and Urinary bladder;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH ATG10 AND ATG12.
DOI=10.1016/S0014-5793(02)03739-0; PubMed=12482611 [NCBI, ExPASy, EBI, Israel, Japan]
Mizushima N., Yoshimori T., Ohsumi Y.;
"Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-mediated yeast two-hybrid method.";
FEBS Lett. 532:450-454(2002).
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.
  • SUBUNIT: 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).
  • SUBCELLULAR LOCATION: Cytoplasm (Probable).
  • TISSUE SPECIFICITY: Widely expressed, especially in kidney, liver, lymph nodes and bone marrow.
  • DOMAIN: The C-terminal part of the protein is essential for the dimerization and interaction with ATG3 and ATG12 (By similarity).
  • SIMILARITY: Belongs to the ATG7 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB079385; BAC10416.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK007484; BAB25060.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK035604; BAC29122.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK161133; BAE36208.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK170769; BAE42018.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK172272; BAE42917.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058597; AAH58597.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_083111.1; -.
UniGene Mm.275332
3D structure databases
HSSP P12282; 1JW9. [HSSP ENTRY / PDB]
ModBase Q9D906.
Organism-specific databases
MGI MGI:1921494; Atg7.
Gene expression databases
ArrayExpress Q9D906; -.
CleanEx MM_ATG7; -.
GermOnline ENSMUSG00000030314; Mus musculus.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0004839; Molecular function: ubiquitin activating enzyme activity (inferred from direct assay from MGI).
GO:0007628; Biological process: adult walking behavior (inferred from mutant phenotype from MGI).
GO:0006520; Biological process: amino acid metabolic process (inferred from mutant phenotype from MGI).
GO:0006914; Biological process: autophagy (inferred from mutant phenotype from MGI).
GO:0055013; Biological process: cardiac muscle cell development (inferred from mutant phenotype from MGI).
GO:0021680; Biological process: cerebellar Purkinje cell layer development (inferred from mutant phenotype from MGI).
GO:0021987; Biological process: cerebral cortex development (inferred from mutant phenotype from MGI).
GO:0001889; Biological process: liver development (inferred from mutant phenotype from MGI).
GO:0016044; Biological process: membrane organization and biogenesis (inferred from mutant phenotype from MGI).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from mutant phenotype from MGI).
GO:0031175; Biological process: neurite development (inferred from mutant phenotype from MGI).
GO:0050877; Biological process: neurological system process (inferred from mutant phenotype from MGI).
GO:0006996; Biological process: organelle organization and biogenesis (inferred from mutant phenotype from MGI).
GO:0031401; Biological process: positive regulation of protein modification process (inferred from direct assay from MGI).
GO:0009791; Biological process: post-embryonic development (inferred from mutant phenotype from MGI).
GO:0030163; Biological process: protein catabolic process (inferred from mutant phenotype from MGI).
GO:0021860; Biological process: pyramidal neuron development (inferred from mutant phenotype from MGI).
GO:0031396; Biological process: regulation of protein ubiquitination (inferred from mutant phenotype from MGI).
GO:0042594; Biological process: response to starvation (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR006285; E1_like_Apg7.
IPR000594; ThiF_NAD_FAD_bd.
Graphical view of domain structure.
Pfam PF00899; ThiF; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01381; E1_like_apg7; 1.
BLOCKS Q9D906.
Genome annotation databases
Ensembl ENSMUSG00000030314; Mus musculus. [Contig view]
GeneID 74244; -.
KEGG mmu:74244; -.
Phylogenomic databases
HOGENOM Q9D906; -.
HOVERGEN Q9D906; -.
Other
SOURCE Atg7; Mus musculus.
ProtoNet Q9D906.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Autophagy; Cytoplasm; Protein transport; Transport; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   698  698     Autophagy-related protein 7. PRO_0000212807
ACT_SITE   567   567        Glycyl thioester intermediate (Potential). 
MUTAGEN   567   567        C->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. 
CONFLICT   22    22        F -> L (in Ref. 1; BAC10416). 
Sequence information
Length: 698 AA [This is the length of the unprocessed precursor] Molecular weight: 77520 Da [This is the MW of the unprocessed precursor] CRC64: 79D94EA7464C6ADB [This is a checksum on the sequence]
        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 

Q9D906 in FASTA format

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View entry in raw text format (no links)
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