Q9CPX6 (ATG3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-like-conjugating enzyme ATG3
EC=6.3.2.-

Alternative name(s):
Autophagy-related protein 3
Short name=APG3-like

Gene names

Name:	Atg3
Synonyms:	Apg3l

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E2-like enzyme involved in autophagy and mitochondrial homeostasis. Catalyzes the conjugation of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to phosphatidylethanolamine (PE). PE-conjugation to ATG8-like proteins is essential for autophagy. Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Ref.4
Subunit structure	Interacts with ATG7 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5 By similarity.
Subcellular location	Cytoplasm By similarity.
Post-translational modification	Conjugated to ATG12 at Lys-243. ATG12-conjugation plays a role in regulation of mitochondrial homeostasis and cell death, while it is not involved in PE-conjugation to ATG8-like proteins and autophagy.
Sequence similarities	Belongs to the ATG3 family.

Ontologies

Keywords
Biological process	Autophagy Protein transport Transport Ubl conjugation pathway
Cellular component	Cytoplasm
Molecular function	Ligase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	autophagic vacuole assembly Inferred from mutant phenotype Ref.4. Source: UniProtKB mitochondrial fragmentation involved in apoptosis Inferred from mutant phenotype Ref.4. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	Atg12 ligase activity Inferred from direct assay Ref.4. Source: UniProtKB Atg8 ligase activity Inferred from mutant phenotype Ref.4. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Atg12	Q9CQY1	3	EBI-2911810,EBI-2911788

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 314	314	Ubiquitin-like-conjugating enzyme ATG3		PRO_0000213570
Sites
	Active site	264	1	Glycyl thioester intermediate Probable
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	18	1	Phosphotyrosine By similarity
	Cross-link	243		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12)
Experimental info
	Mutagenesis	71	1	K → R: Does not affect ATG12 conjugation. Ref.4
	Mutagenesis	83	1	K → R: Does not affect ATG12 conjugation. Ref.4
	Mutagenesis	243	1	K → R: Abolishes ATG12 conjugation, leading to an expansion in mitochondrial mass and fragmented mitochondrial morphology. Does not affect PE-conjugation to ATG8-like proteins. Ref.4
	Mutagenesis	264	1	C → A: Abolishes E2-like activity. Ref.4
	Mutagenesis	271	1	K → R: Does not affect ATG12 conjugation. Ref.4
	Mutagenesis	295	1	K → R: Does not affect ATG12 conjugation. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9CPX6 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: EC5ECACD3247ED66	FASTA	314	35,796
	10 20 30 40 50 60 MQNVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC PTWQWATGEE 70 80 90 100 110 120 LKVKAYLPTD KQFLVTKNVP CYKRCKQMEY SDELEAIIEE DDGDGGWVDT YHNTGITGIT 130 140 150 160 170 180 EAVKEITLES KDSIKLQDCS ALCDEEDEED EGEAADMEEY EESGLLETDE ATLDTRKIVE 190 200 210 220 230 240 ACKAKADAGG EDAILQTRTY DLYITYDKYY QTPRLWLFGY DEQRQPLTVE HMYEDISQDH 250 260 270 280 290 300 VKKTVTIENH PHLPPPPMCS VHPCRHAEVM KKIIETVAEG GGELGVHMYL LIFLKFVQAV 310 IPTIEYDYTR HFTM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p." Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E. J. Biol. Chem. 277:13739-13744(2002) [PubMed: 11825910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow, Cerebellum and Colon.
[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]. Strain: FVB/N. Tissue: Kidney.
[4]	"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: 20723759] [Abstract] Cited for: FUNCTION, CONJUGATION TO ATG12 AT LYS-243, MUTAGENESIS OF LYS-71; LYS-83; LYS-243; CYS-264; LYS-271 AND LYS-295.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB079386 mRNA. Translation: BAC57452.1. AK005266 mRNA. Translation: BAB23918.1. AK011409 mRNA. Translation: BAB27600.1. AK078877 mRNA. Translation: BAC37437.1. AK150914 mRNA. Translation: BAE29952.1. AK159231 mRNA. Translation: BAE34917.1. BC010809 mRNA. Translation: AAH10809.1.
IPI	IPI00132142.
RefSeq	NP_080678.1. NM_026402.3.
UniGene	Mm.41775.
3D structure databases
ProteinModelPortal	Q9CPX6.
SMR	Q9CPX6. Positions 27-309.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9CPX6. 1 interaction.
STRING	Q9CPX6.
PTM databases
PhosphoSite	Q9CPX6.
Proteomic databases
PRIDE	Q9CPX6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023343; ENSMUSP00000023343; ENSMUSG00000022663.
GeneID	67841.
KEGG	mmu:67841.
UCSC	uc007zii.1. mouse.
Organism-specific databases
CTD	64422.
MGI	MGI:1915091. Atg3.
Phylogenomic databases
eggNOG	roNOG06532.
GeneTree	ENSGT00390000010308.
HOGENOM	HBG602769.
HOVERGEN	HBG080876.
InParanoid	Q9CPX6.
OMA	DTYHNAG.
OrthoDB	EOG4M398Z.
PhylomeDB	Q9CPX6.
Gene expression databases
ArrayExpress	Q9CPX6.
Bgee	Q9CPX6.
CleanEx	MM_ATG3.
Genevestigator	Q9CPX6.
GermOnline	ENSMUSG00000022663. Mus musculus.
Family and domain databases
InterPro	IPR007135. Autophagy-rel_prot_3. IPR019461. Autophagy-rel_prot_3_C. IPR007134. Autophagy-rel_prot_3_N. [Graphical view]
KO	K08343.
Pfam	PF03987. Autophagy_act_C. 1 hit. PF10381. Autophagy_Cterm. 1 hit. PF03986. Autophagy_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	325677.
SOURCE	Search...

Entry information

Entry name

ATG3_MOUSE

Accession

Primary (citable) accession number: Q9CPX6
Secondary accession number(s): Q3TXJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	June 1, 2001
Last modified:	November 16, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program