ATG10_MOUSE
ID ATG10_MOUSE Reviewed; 215 AA.
AC Q8R1P4; Q8BPA9; Q9D3J7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Ubiquitin-like-conjugating enzyme ATG10;
DE EC=2.3.2.-;
DE AltName: Full=Autophagy-related protein 10;
DE Short=APG10-like;
DE Short=mAPG10;
GN Name=Atg10; Synonyms=Apg10l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ATG12; ATG5 AND ATG7, AND
RP MUTAGENESIS OF CYS-165.
RX PubMed=12482611; DOI=10.1016/s0014-5793(02)03739-0;
RA Mizushima N., Yoshimori T., Ohsumi Y.;
RT "Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-
RT mediated yeast two-hybrid method.";
RL FEBS Lett. 532:450-454(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ATG12 AND MAP1LC3A,
RP AND MUTAGENESIS OF CYS-165.
RC TISSUE=Brain;
RX PubMed=12890687; DOI=10.1074/jbc.m300550200;
RA Nemoto T., Tanida I., Tanida-Miyake E., Minematsu-Ikeguchi N., Yokota M.,
RA Ohsumi M., Ueno T., Kominami E.;
RT "The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation,
RT facilitates MAP-LC3 modification.";
RL J. Biol. Chem. 278:39517-39526(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Pituitary;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary cancer;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF CYS-165.
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 cell
RT death.";
RL Cell 142:590-600(2010).
RN [6]
RP FUNCTION.
RX PubMed=21367888; DOI=10.1128/jvi.02032-10;
RA Jiang H., White E.J., Rios-Vicil C.I., Xu J., Gomez-Manzano C., Fueyo J.;
RT "Human adenovirus type 5 induces cell lysis through autophagy and
RT autophagy-triggered caspase activity.";
RL J. Virol. 85:4720-4729(2011).
CC -!- FUNCTION: E2-like enzyme involved in autophagy. Acts as an E2-like
CC enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12
CC conjugation to ATG5 is required for autophagy. Likely serves as an
CC ATG5-recognition molecule. Not involved in ATG12 conjugation to ATG3.
CC Plays a role in adenovirus-mediated cell lysis.
CC {ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:20723759,
CC ECO:0000269|PubMed:21367888}.
CC -!- SUBUNIT: Interacts with MAP1LC3A. By interacting with MAP1LC3A, it
CC plays a role in the conjugation of ATG12 to ATG5. Also able to directly
CC interact either with ATG5 or ATG7. {ECO:0000269|PubMed:12482611,
CC ECO:0000269|PubMed:12890687}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATG10 family. {ECO:0000305}.
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DR EMBL; AB091691; BAC55163.1; -; mRNA.
DR EMBL; AB079383; BAC77060.1; -; mRNA.
DR EMBL; AK017355; BAB30705.1; -; mRNA.
DR EMBL; AK077333; BAC36756.1; -; mRNA.
DR EMBL; BC023455; AAH23455.1; -; mRNA.
DR RefSeq; NP_080046.3; NM_025770.3.
DR RefSeq; XP_006517389.1; XM_006517326.3.
DR AlphaFoldDB; Q8R1P4; -.
DR SMR; Q8R1P4; -.
DR BioGRID; 211724; 5.
DR IntAct; Q8R1P4; 3.
DR MINT; Q8R1P4; -.
DR STRING; 10090.ENSMUSP00000022119; -.
DR iPTMnet; Q8R1P4; -.
DR PhosphoSitePlus; Q8R1P4; -.
DR MaxQB; Q8R1P4; -.
DR PaxDb; Q8R1P4; -.
DR PRIDE; Q8R1P4; -.
DR ProteomicsDB; 265160; -.
DR DNASU; 66795; -.
DR GeneID; 66795; -.
DR KEGG; mmu:66795; -.
DR UCSC; uc007rjr.1; mouse.
DR CTD; 83734; -.
DR MGI; MGI:1914045; Atg10.
DR eggNOG; KOG4741; Eukaryota.
DR InParanoid; Q8R1P4; -.
DR OrthoDB; 1538225at2759; -.
DR PhylomeDB; Q8R1P4; -.
DR TreeFam; TF314016; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 66795; 19 hits in 72 CRISPR screens.
DR ChiTaRS; Atg10; mouse.
DR PRO; PR:Q8R1P4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8R1P4; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0061651; F:Atg12 conjugating enzyme activity; IDA:FlyBase.
DR GO; GO:0019777; F:Atg12 transferase activity; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0006983; P:ER overload response; ISO:MGI.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0031401; P:positive regulation of protein modification process; IDA:MGI.
DR GO; GO:0006497; P:protein lipidation; IDA:MGI.
DR GO; GO:0032446; P:protein modification by small protein conjugation; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007135; Atg3/Atg10.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Protein transport; Reference proteome; Transferase;
KW Transport; Ubl conjugation pathway.
FT CHAIN 1..215
FT /note="Ubiquitin-like-conjugating enzyme ATG10"
FT /id="PRO_0000096184"
FT ACT_SITE 165
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 165
FT /note="C->S: Instead of the formation of an intermediate
FT complex with a thiol ester bond between ATG10 (E2-like
FT enzyme) and ATG12 (substrate), a stable complex with an O-
FT ester bond is formed. Does not affect ATG12 conjugation to
FT ATG3."
FT /evidence="ECO:0000269|PubMed:12482611,
FT ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:20723759"
FT CONFLICT 42
FT /note="M -> I (in Ref. 3; BAB30705)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..54
FT /note="AS -> TL (in Ref. 2; BAC77060 and 3; BAB30705/
FT BAC36756)"
FT /evidence="ECO:0000305"
FT CONFLICT 58..61
FT /note="Missing (in Ref. 2; BAC77060 and 3; BAB30705/
FT BAC36756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 215 AA; 24577 MW; 8239CC22A8727B2C CRC64;
MEDEFFGEKS FQHYCAEFIR HSQQIGDGWE WRTAKECSDG YMCKTQFRIK NEASTPHVGT
PASVLTCLPT EENLELPMDD SEVTRPAAVA EVIKHEYHVL YSCSYQVPVL YFRASFLDGR
PLALEDIWEG VHECYKPRLL QGPWDTITQQ EHPILGQPFF VLHPCKTNEF MTAVLKNSQK
INRNVNYITS WLSLVGPVVG LNLPLSYAKA TSQSE
