ID   ATG3_MOUSE              Reviewed;         314 AA.
AC   Q9CPX6; Q3TXJ9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-NOV-2011, entry version 65.
DE   RecName: Full=Ubiquitin-like-conjugating enzyme ATG3;
DE            EC=6.3.2.-;
DE   AltName: Full=Autophagy-related protein 3;
DE            Short=APG3-like;
GN   Name=Atg3; Synonyms=Apg3l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=21950715; PubMed=11825910; DOI=10.1074/jbc.M200385200;
RA   Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
RT   "Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
RT   substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the
RT   conjugation of hApg12p to hApg5p.";
RL   J. Biol. Chem. 277:13739-13744(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, and Colon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, CONJUGATION TO ATG12 AT LYS-243, AND MUTAGENESIS OF LYS-71;
RP   LYS-83; LYS-243; CYS-264; LYS-271 AND LYS-295.
RX   PubMed=20723759; DOI=10.1016/j.cell.2010.07.018;
RA   Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C.,
RA   Debnath J.;
RT   "ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and
RT   cell death.";
RL   Cell 142:590-600(2010).
CC   -!- FUNCTION: E2-like enzyme involved in autophagy and mitochondrial
CC       homeostasis. Catalyzes the conjugation of ATG8-like proteins
CC       (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to
CC       phosphatidylethanolamine (PE). PE-conjugation to ATG8-like
CC       proteins is essential for autophagy. Preferred substrate is
CC       MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing
CC       the conjugation of ATG12 to itself, ATG12 conjugation to ATG3
CC       playing a role in mitochondrial homeostasis but not in autophagy.
CC       ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-
CC       E2 complex with ATG3.
CC   -!- SUBUNIT: Interacts with ATG7 and ATG12. The complex, composed of
CC       ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5
CC       (By similarity).
CC   -!- INTERACTION:
CC       Q9CQY1:Atg12; NbExp=3; IntAct=EBI-2911810, EBI-2911788;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Conjugated to ATG12 at Lys-243. ATG12-conjugation plays a
CC       role in regulation of mitochondrial homeostasis and cell death,
CC       while it is not involved in PE-conjugation to ATG8-like proteins
CC       and autophagy.
CC   -!- SIMILARITY: Belongs to the ATG3 family.
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DR   EMBL; AB079386; BAC57452.1; -; mRNA.
DR   EMBL; AK005266; BAB23918.1; -; mRNA.
DR   EMBL; AK011409; BAB27600.1; -; mRNA.
DR   EMBL; AK078877; BAC37437.1; -; mRNA.
DR   EMBL; AK150914; BAE29952.1; -; mRNA.
DR   EMBL; AK159231; BAE34917.1; -; mRNA.
DR   EMBL; BC010809; AAH10809.1; -; mRNA.
DR   IPI; IPI00132142; -.
DR   RefSeq; NP_080678.1; NM_026402.3.
DR   UniGene; Mm.41775; -.
DR   ProteinModelPortal; Q9CPX6; -.
DR   SMR; Q9CPX6; 27-309.
DR   IntAct; Q9CPX6; 1.
DR   STRING; Q9CPX6; -.
DR   PhosphoSite; Q9CPX6; -.
DR   PRIDE; Q9CPX6; -.
DR   Ensembl; ENSMUST00000023343; ENSMUSP00000023343; ENSMUSG00000022663.
DR   GeneID; 67841; -.
DR   KEGG; mmu:67841; -.
DR   UCSC; uc007zii.1; mouse.
DR   CTD; 64422; -.
DR   MGI; MGI:1915091; Atg3.
DR   eggNOG; roNOG06532; -.
DR   GeneTree; ENSGT00390000010308; -.
DR   HOGENOM; HBG602769; -.
DR   HOVERGEN; HBG080876; -.
DR   InParanoid; Q9CPX6; -.
DR   OMA; DTYHNAG; -.
DR   OrthoDB; EOG4M398Z; -.
DR   PhylomeDB; Q9CPX6; -.
DR   NextBio; 325677; -.
DR   ArrayExpress; Q9CPX6; -.
DR   Bgee; Q9CPX6; -.
DR   CleanEx; MM_ATG3; -.
DR   Genevestigator; Q9CPX6; -.
DR   GermOnline; ENSMUSG00000022663; Mus musculus.
DR   GO; GO:0019777; F:Atg12 ligase activity; IDA:UniProtKB.
DR   GO; GO:0019776; F:Atg8 ligase activity; IMP:UniProtKB.
DR   GO; GO:0000045; P:autophagic vacuole assembly; IMP:UniProtKB.
DR   GO; GO:0043653; P:mitochondrial fragmentation involved in apoptosis; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007135; Autophagy-rel_prot_3.
DR   InterPro; IPR019461; Autophagy-rel_prot_3_C.
DR   InterPro; IPR007134; Autophagy-rel_prot_3_N.
DR   KO; K08343; -.
DR   Pfam; PF03987; Autophagy_act_C; 1.
DR   Pfam; PF10381; Autophagy_Cterm; 1.
DR   Pfam; PF03986; Autophagy_N; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Autophagy; Complete proteome; Cytoplasm; Isopeptide bond;
KW   Ligase; Phosphoprotein; Protein transport; Reference proteome;
KW   Transport; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    314       Ubiquitin-like-conjugating enzyme ATG3.
FT                                /FTId=PRO_0000213570.
FT   ACT_SITE    264    264       Glycyl thioester intermediate (Probable).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      18     18       Phosphotyrosine (By similarity).
FT   CROSSLNK    243    243       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ATG12).
FT   MUTAGEN      71     71       K->R: Does not affect ATG12 conjugation.
FT   MUTAGEN      83     83       K->R: Does not affect ATG12 conjugation.
FT   MUTAGEN     243    243       K->R: Abolishes ATG12 conjugation,
FT                                leading to an expansion in mitochondrial
FT                                mass and fragmented mitochondrial
FT                                morphology. Does not affect PE-
FT                                conjugation to ATG8-like proteins.
FT   MUTAGEN     264    264       C->A: Abolishes E2-like activity.
FT   MUTAGEN     271    271       K->R: Does not affect ATG12 conjugation.
FT   MUTAGEN     295    295       K->R: Does not affect ATG12 conjugation.
SQ   SEQUENCE   314 AA;  35796 MW;  EC5ECACD3247ED66 CRC64;
     MQNVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC PTWQWATGEE
     LKVKAYLPTD KQFLVTKNVP CYKRCKQMEY SDELEAIIEE DDGDGGWVDT YHNTGITGIT
     EAVKEITLES KDSIKLQDCS ALCDEEDEED EGEAADMEEY EESGLLETDE ATLDTRKIVE
     ACKAKADAGG EDAILQTRTY DLYITYDKYY QTPRLWLFGY DEQRQPLTVE HMYEDISQDH
     VKKTVTIENH PHLPPPPMCS VHPCRHAEVM KKIIETVAEG GGELGVHMYL LIFLKFVQAV
     IPTIEYDYTR HFTM
//