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Ubiquitin-like protein ATG12 (Autophagy-related protein 12) (APG12-like)

 ATG12_MOUSE             Reviewed;         141 AA.
Q9CQY1; Q3TKE5; Q9D7Y5;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-FEB-2018, entry version 139.
RecName: Full=Ubiquitin-like protein ATG12;
AltName: Full=Autophagy-related protein 12;
Short=APG12-like;
Name=Atg12; Synonyms=Apg12, Apg12l;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CONJUGATION TO ATG5, FUNCTION OF THE
ATG12/ATG5 CONJUGATE, AND SUBCELLULAR LOCATION.
PubMed=11266458; DOI=10.1083/jcb.152.4.657;
Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y.,
Suzuki K., Tokuhisa T., Ohsumi Y., Yoshimori T.;
"Dissection of autophagosome formation using Apg5-deficient mouse
embryonic stem cells.";
J. Cell Biol. 152:657-668(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Blastocyst, Placenta, Stomach, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH ATG10, AND CONJUGATION TO ATG5.
PubMed=12482611; DOI=10.1016/S0014-5793(02)03739-0;
Mizushima N., Yoshimori T., Ohsumi Y.;
"Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the
conjugation-mediated yeast two-hybrid method.";
FEBS Lett. 532:450-454(2002).
[5]
CONJUGATION TO ATG5 BY ATG10, AND FUNCTION.
PubMed=12890687; DOI=10.1074/jbc.M300550200;
Nemoto T., Tanida I., Tanida-Miyake E., Minematsu-Ikeguchi N.,
Yokota M., Ohsumi M., Ueno T., Kominami E.;
"The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation,
facilitates MAP-LC3 modification.";
J. Biol. Chem. 278:39517-39526(2003).
[6]
IDENTIFICATION IN A COMPLEX WITH ATG5 AND ATG16L.
PubMed=12665549; DOI=10.1242/jcs.00381;
Mizushima N., Kuma A., Kobayashi Y., Yamamoto A., Matsubae M.,
Takao T., Natsume T., Ohsumi Y., Yoshimori T.;
"Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic
isolation membrane with the Apg12-Apg5 conjugate.";
J. Cell Sci. 116:1679-1688(2003).
[7]
FUNCTION IN VIRAL INFECTION.
PubMed=17709747; DOI=10.1073/pnas.0704014104;
Jounai N., Takeshita F., Kobiyama K., Sawano A., Miyawaki A.,
Xin K.Q., Ishii K.J., Kawai T., Akira S., Suzuki K., Okuda K.;
"The Atg5-Atg12 conjugate associates with innate antiviral immune
responses.";
Proc. Natl. Acad. Sci. U.S.A. 104:14050-14055(2007).
[8]
DOMAIN.
PubMed=18704115; DOI=10.1038/embor.2008.163;
Geng J., Klionsky D.J.;
"The Atg8 and Atg12 ubiquitin-like conjugation systems in
macroautophagy. 'Protein modifications: beyond the usual suspects'
review series.";
EMBO Rep. 9:859-864(2008).
[9]
CONJUGATION TO ATG5.
PubMed=18768753; DOI=10.1091/mbc.E08-03-0309;
Sou Y.S., Waguri S., Iwata J., Ueno T., Fujimura T., Hara T.,
Sawada N., Yamada A., Mizushima N., Uchiyama Y., Kominami E.,
Tanaka K., Komatsu M.;
"The Atg8 conjugation system is indispensable for proper development
of autophagic isolation membranes in mice.";
Mol. Biol. Cell 19:4762-4775(2008).
[10]
CONJUGATION TO ATG5.
PubMed=19417210; DOI=10.1182/blood-2008-04-151639;
Zhang J., Randall M.S., Loyd M.R., Dorsey F.C., Kundu M.,
Cleveland J.L., Ney P.A.;
"Mitochondrial clearance is regulated by Atg7-dependent and
-independent mechanisms during reticulocyte maturation.";
Blood 114:157-164(2009).
[11]
FUNCTION.
PubMed=20723759; DOI=10.1016/j.cell.2010.07.018;
Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C.,
Debnath J.;
"ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and
cell death.";
Cell 142:590-600(2010).
-!- FUNCTION: Ubiquitin-like protein involved in autophagy vesicles
formation. Conjugation with ATG5 through a ubiquitin-like
conjugating system involving also ATG7 as an E1-like activating
enzyme and ATG10 as an E2-like conjugating enzyme, is essential
for its function. The ATG12-ATG5 conjugate acts as an E3-like
enzyme which is required for lipidation of ATG8 family proteins
and their association to the vesicle membranes.
{ECO:0000269|PubMed:11266458, ECO:0000269|PubMed:12890687,
ECO:0000269|PubMed:20723759}.
-!- FUNCTION: (Microbial infection) May act as a proviral factor. In
association with ATG5, negatively regulates the innate antiviral
immune response by impairing the type I IFN production pathway
upon vesicular stomatitis virus (VSV) infection.
{ECO:0000269|PubMed:17709747}.
-!- SUBUNIT: Forms a conjugate with ATG5 (PubMed:11266458,
PubMed:12482611, PubMed:12890687, PubMed:12665549,
PubMed:18768753, PubMed:19417210). The ATG12-ATG5 conjugate forms
a complex with several units of ATG16L (PubMed:12665549).
Interacts with DHX58/RIG-1, IFIH1/MDA5 and MAVS/IPS-1 in monomeric
form as well as in ATG12-ATG5 conjugate. The interaction with MAVS
is further enhanced upon vesicular stomatitis virus (VSV)
infection. Interacts with ATG3 and ATG7 (By similarity). Interacts
with ATG10 (PubMed:12482611). Interacts with TECPR1 (By
similarity). {ECO:0000250|UniProtKB:O94817,
ECO:0000269|PubMed:11266458, ECO:0000269|PubMed:12482611,
ECO:0000269|PubMed:12665549, ECO:0000269|PubMed:12890687,
ECO:0000269|PubMed:18768753, ECO:0000269|PubMed:19417210}.
-!- INTERACTION:
Q9CPX6:Atg3; NbExp=5; IntAct=EBI-2911788, EBI-2911810;
Q99J83:Atg5; NbExp=4; IntAct=EBI-2911788, EBI-2911848;
Q9WU78-1:Pdcd6ip; NbExp=3; IntAct=EBI-2911788, EBI-15788421;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
structure membrane {ECO:0000250|UniProtKB:O94817}; Peripheral
membrane protein {ECO:0000250|UniProtKB:O94817}. Note=TECPR1
recruits the ATG12-ATG5 conjugate to the autolysosomal membrane.
{ECO:0000250|UniProtKB:O94817}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: Shares weak sequence similarity with ubiquitin family, but
contains an 'ubiquitin superfold' and the C-terminal Gly is
required for isopeptide linkage. {ECO:0000269|PubMed:18704115}.
-!- PTM: Acetylated by EP300. {ECO:0000250}.
-!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AB066216; BAB62092.1; -; mRNA.
EMBL; AK008698; BAB25839.1; -; mRNA.
EMBL; AK016474; BAB30256.1; -; mRNA.
EMBL; AK005405; BAB24005.1; -; mRNA.
EMBL; AK167027; BAE39200.1; -; mRNA.
EMBL; BC070470; AAH70470.1; -; mRNA.
CCDS; CCDS37811.1; -.
RefSeq; NP_080493.2; NM_026217.3.
UniGene; Mm.9852; -.
ProteinModelPortal; Q9CQY1; -.
SMR; Q9CQY1; -.
BioGrid; 212249; 4.
CORUM; Q9CQY1; -.
DIP; DIP-57729N; -.
IntAct; Q9CQY1; 10.
MINT; Q9CQY1; -.
STRING; 10090.ENSMUSP00000038489; -.
iPTMnet; Q9CQY1; -.
PhosphoSitePlus; Q9CQY1; -.
MaxQB; Q9CQY1; -.
PaxDb; Q9CQY1; -.
PeptideAtlas; Q9CQY1; -.
PRIDE; Q9CQY1; -.
Ensembl; ENSMUST00000035648; ENSMUSP00000038489; ENSMUSG00000032905.
GeneID; 67526; -.
KEGG; mmu:67526; -.
UCSC; uc008evu.1; mouse.
CTD; 9140; -.
MGI; MGI:1914776; Atg12.
eggNOG; KOG3439; Eukaryota.
eggNOG; ENOG4111ND7; LUCA.
GeneTree; ENSGT00390000016654; -.
HOGENOM; HOG000234863; -.
HOVERGEN; HBG080875; -.
InParanoid; Q9CQY1; -.
KO; K08336; -.
OMA; IHYCKSQ; -.
OrthoDB; EOG091G0XR8; -.
PhylomeDB; Q9CQY1; -.
TreeFam; TF325131; -.
Reactome; R-MMU-1632852; Macroautophagy.
Reactome; R-MMU-5205685; Pink/Parkin Mediated Mitophagy.
Reactome; R-MMU-8934903; Receptor Mediated Mitophagy.
ChiTaRS; Atg12; mouse.
PRO; PR:Q9CQY1; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000032905; -.
CleanEx; MM_ATG12; -.
Genevisible; Q9CQY1; MM.
GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
GO; GO:0005776; C:autophagosome; ISO:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IMP:ParkinsonsUK-UCL.
GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
GO; GO:0019776; F:Atg8 ligase activity; IBA:GO_Central.
GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
GO; GO:0006914; P:autophagy; TAS:MGI.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
CDD; cd01612; APG12_C; 1.
InterPro; IPR007242; Atg12.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR13385; PTHR13385; 1.
Pfam; PF04110; APG12; 1.
SUPFAM; SSF54236; SSF54236; 1.
1: Evidence at protein level;
Acetylation; Autophagy; Complete proteome; Cytoplasm; Isopeptide bond;
Membrane; Reference proteome; Ubl conjugation pathway.
CHAIN 1 141 Ubiquitin-like protein ATG12.
/FTId=PRO_0000212472.
CROSSLNK 141 141 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
protein).
CONFLICT 44 48 GTEEP -> ERGT (in Ref. 2; BAB25839).
{ECO:0000305}.
SEQUENCE 141 AA; 15207 MW; 440F9A625624A78B CRC64;
MSEDSEVVLQ LPSAPVGAGG ESLPELSPET ATPEPPSSAA VSPGTEEPPG DTKKKIDILL
KAVGDTPIMK TKKWAVERTR TIQGLIDFIK KFLKLVASEQ LFIYVNQSFA PSPDQEVGTL
YECFGSDGKL VLHYCKSQAW G


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