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Reviewed, UniProtKB/Swiss-Prot Q9CPX6 (ATG3_MOUSE)

Last modified June 16, 2009. Version 45. 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 3
Alternative name(s):
    APG3-like
Gene names
Name: Atg3
Synonyms: Apg3l
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

GABARAPL1 (GABARAPL2 or GABARAP or MAP1LC3)-modifier protein conjugating enzyme involved in its E2-like covalent binding to PE. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3 (E2-like enzyme). Preferred substrate is MAP1LC3A. Formation of the GABARAPL1-PE conjugate is essential for autophagy By similarity.

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.

Sequence similarities

Belongs to the ATG3 family.

Ontologies

Keywords
   Biological processAutophagy
Protein transport
Transport
Ubl conjugation pathway
   Cellular componentCytoplasm
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processautophagy

Inferred from electronic annotation. Source: UniProtKB-KW

modification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Autophagy-related protein 3
PRO_0000213570

Sites

Active site2641Glycyl thioester intermediate Potential

Amino acid modifications

Modified residue181Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CPX6-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: EC5ECACD3247ED66

FASTA31435,796
        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 

« Hide

References

« Hide 'large scale' references
[1]"Murine Apg3p is an authentic E2 enzyme for Apg8p homologs."
Tanida I., Nishitani T., Tanida-Miyake E., Ueno T., Kominami E.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
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. 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.
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.

Cross-references

Sequence databases

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.
IPIIPI00132142.
RefSeqNP_080678.1.
UniGeneMm.41775

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ9CPX6.

Proteomic databases

PRIDEQ9CPX6.

Genome annotation databases

EnsemblENSMUSG00000022663. Mus musculus. [Contig view]
GeneID67841.
KEGGmmu:67841.

Organism-specific databases

MGIMGI:1915091. Atg3.

Phylogenomic databases

HOGENOMQ9CPX6.
HOVERGENQ9CPX6.
OMAQ9CPX6. YHNTGIA.

Gene expression databases

ArrayExpressQ9CPX6.
BgeeQ9CPX6.
CleanExMM_ATG3.
GermOnlineENSMUSG00000022663. Mus musculus.

Family and domain databases

InterProIPR007135. Autophagy-rel_prot_3.
IPR019461. Autophagy-rel_prot_3_C.
IPR007134. Autophagy-rel_prot_3_N.
[Graphical view]
PfamPF03987. Autophagy_act_C. 1 hit.
PF10381. Autophagy_Cterm. 1 hit.
PF03986. Autophagy_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio325677.
SOURCESearch...

Entry information

Entry nameATG3_MOUSE
AccessionPrimary (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: June 16, 2009
This is version 45 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