Q9D906 (ATG7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	698 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as an E1 enzyme essential for multisubstrates such as ATG8-like proteins and ATG12. Forms intermediate conjugates with ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). PE-conjugation to ATG8-like proteins is essential for autophagy. Also acts as an E1 enzyme for ATG12 conjugation to ATG5 and ATG3. Ref.1 Ref.5
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 process	Autophagy Protein transport Transport Ubl conjugation pathway
Cellular component	Cytoplasm
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult walking behavior Inferred from mutant phenotype PubMed 16625205. Source: MGI autophagy Inferred from mutant phenotype PubMed 15866887PubMed 16885219PubMed 17450150PubMed 17726112PubMed 20577052. Source: MGI cardiac muscle cell development Inferred from mutant phenotype PubMed 17450150. Source: MGI cellular amino acid metabolic process Inferred from mutant phenotype PubMed 15866887. Source: MGI cellular membrane organization Inferred from mutant phenotype PubMed 17726112. 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 PubMed 15866887. Source: MGI negative regulation of apoptotic process Inferred from mutant phenotype PubMed 16625205PubMed 17450150. Source: MGI neurological system process Inferred from mutant phenotype PubMed 16625205. Source: MGI organelle organization Inferred from mutant phenotype PubMed 15866887. Source: MGI positive regulation of macroautophagy Inferred from electronic annotation. Source: Compara positive regulation of protein modification process Inferred from direct assay Ref.4. Source: MGI post-embryonic development Inferred from mutant phenotype PubMed 15866887PubMed 16625205. Source: MGI protein catabolic process Inferred from mutant phenotype PubMed 15866887. Source: MGI protein lipidation Inferred from sequence orthology PubMed 12890687. Source: MGI protein modification by small protein conjugation Inferred from mutant phenotype PubMed 15866887. 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 PubMed 15866887. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	APG12 activating enzyme activity Inferred from mutant phenotype Ref.5. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro ubiquitin activating enzyme activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 698	698	Ubiquitin-like modifier-activating enzyme ATG7		PRO_0000212807
Sites
	Active site	567	1	Glycyl thioester intermediate Probable
Experimental info
	Mutagenesis	567	1	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. Ref.1
	Sequence conflict	22	1	F → L in BAC10416. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9D906 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 79D94EA7464C6ADB	FASTA	698	77,520
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
+	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.
IPI	IPI00463195.
RefSeq	NP_001240646.1. NM_001253717.1. NP_001240647.1. NM_001253718.1. NP_083111.1. NM_028835.4.
UniGene	Mm.275332.
3D structure databases
ProteinModelPortal	Q9D906.
SMR	Q9D906. Positions 9-685.
ModBase	Search...
PTM databases
PhosphoSite	Q9D906.
Proteomic databases
PaxDb	Q9D906.
PRIDE	Q9D906.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032457; ENSMUSP00000032457; ENSMUSG00000030314. ENSMUST00000169310; ENSMUSP00000133215; ENSMUSG00000030314.
GeneID	74244.
KEGG	mmu:74244.
UCSC	uc009dhz.1. mouse.
Organism-specific databases
CTD	10533.
MGI	MGI:1921494. Atg7.
Phylogenomic databases
eggNOG	COG0476.
GeneTree	ENSGT00390000017509.
HOGENOM	HOG000162379.
HOVERGEN	HBG080877.
InParanoid	Q9D906.
KO	K08337.
OMA	RDVTHSI.
OrthoDB	EOG43N7C8.
Gene expression databases
Bgee	Q9D906.
CleanEx	MM_ATG7.
Genevestigator	Q9D906.
GermOnline	ENSMUSG00000030314. Mus musculus.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR006285. Atg7. IPR009036. Molybdenum_cofac_synth_MoeB. IPR016040. NAD(P)-bd_dom. IPR000594. ThiF_NAD_FAD-bd. [Graphical view]
PANTHER	PTHR10953:SF3. PTHR10953:SF3. 1 hit.
Pfam	PF00899. ThiF. 1 hit. [Graphical view]
SUPFAM	SSF69572. MoeB. 1 hit.
TIGRFAMs	TIGR01381. E1_like_apg7. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	ATG7. mouse.
NextBio	340222.
SOURCE	Search...

Entry information

Entry name

ATG7_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program