ATG5_MOUSE
ID ATG5_MOUSE Reviewed; 275 AA.
AC Q99J83;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Autophagy protein 5;
DE AltName: Full=APG5-like;
GN Name=Atg5; Synonyms=Apg5l;
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], FUNCTION, CONJUGATION TO ATG12, AND MUTAGENESIS
RP OF LYS-130.
RC TISSUE=Embryonic stem cell;
RX PubMed=11266458; DOI=10.1083/jcb.152.4.657;
RA Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y., Suzuki K.,
RA Tokuhisa T., Ohsumi Y., Yoshimori T.;
RT "Dissection of autophagosome formation using Apg5-deficient mouse embryonic
RT stem cells.";
RL J. Cell Biol. 152:657-668(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP INTERACTION WITH ATG10, AND CONJUGATION TO ATG12.
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 [5]
RP CONJUGATION TO ATG12 BY ATG10, AND FUNCTION.
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 [6]
RP IDENTIFICATION IN A COMPLEX WITH ATG12 AND ATG16L1.
RX PubMed=12665549; DOI=10.1242/jcs.00381;
RA Mizushima N., Kuma A., Kobayashi Y., Yamamoto A., Matsubae M., Takao T.,
RA Natsume T., Ohsumi Y., Yoshimori T.;
RT "Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic
RT isolation membrane with the Apg12-Apg5 conjugate.";
RL J. Cell Sci. 116:1679-1688(2003).
RN [7]
RP FUNCTION.
RX PubMed=17912025; DOI=10.4161/auto.4964;
RA Nishiyama J., Miura E., Mizushima N., Watanabe M., Yuzaki M.;
RT "Aberrant membranes and double-membrane structures accumulate in the axons
RT of Atg5-null Purkinje cells before neuronal death.";
RL Autophagy 3:591-596(2007).
RN [8]
RP FUNCTION.
RX PubMed=17190837; DOI=10.1084/jem.20061303;
RA Pua H.H., Dzhagalov I., Chuck M., Mizushima N., He Y.W.;
RT "A critical role for the autophagy gene Atg5 in T cell survival and
RT proliferation.";
RL J. Exp. Med. 204:25-31(2007).
RN [9]
RP FUNCTION IN VIRAL INFECTION.
RX PubMed=17709747; DOI=10.1073/pnas.0704014104;
RA Jounai N., Takeshita F., Kobiyama K., Sawano A., Miyawaki A., Xin K.Q.,
RA Ishii K.J., Kawai T., Akira S., Suzuki K., Okuda K.;
RT "The Atg5-Atg12 conjugate associates with innate antiviral immune
RT responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14050-14055(2007).
RN [10]
RP FUNCTION.
RX PubMed=18188005; DOI=10.4161/auto.5474;
RA Miller B.C., Zhao Z., Stephenson L.M., Cadwell K., Pua H.H., Lee H.K.,
RA Mizushima N.N., Iwasaki A., He Y.W., Swat W., Virgin H.W.;
RT "The autophagy gene ATG5 plays an essential role in B lymphocyte
RT development.";
RL Autophagy 4:309-314(2008).
RN [11]
RP CONJUGATION TO ATG12.
RX PubMed=18768753; DOI=10.1091/mbc.e08-03-0309;
RA Sou Y.S., Waguri S., Iwata J., Ueno T., Fujimura T., Hara T., Sawada N.,
RA Yamada A., Mizushima N., Uchiyama Y., Kominami E., Tanaka K., Komatsu M.;
RT "The Atg8 conjugation system is indispensable for proper development of
RT autophagic isolation membranes in mice.";
RL Mol. Biol. Cell 19:4762-4775(2008).
RN [12]
RP CONJUGATION TO ATG12.
RX PubMed=19417210; DOI=10.1182/blood-2008-04-151639;
RA Zhang J., Randall M.S., Loyd M.R., Dorsey F.C., Kundu M., Cleveland J.L.,
RA Ney P.A.;
RT "Mitochondrial clearance is regulated by Atg7-dependent and -independent
RT mechanisms during reticulocyte maturation.";
RL Blood 114:157-164(2009).
RN [13]
RP FUNCTION.
RX PubMed=19844159; DOI=10.4161/auto.5.8.9991;
RA Baerga R., Zhang Y., Chen P.H., Goldman S., Jin S.;
RT "Targeted deletion of autophagy-related 5 (atg5) impairs adipogenesis in a
RT cellular model and in mice.";
RL Autophagy 5:1118-1130(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP FUNCTION.
RX PubMed=20171125; DOI=10.1016/j.immuni.2009.12.006;
RA Lee H.K., Mattei L.M., Steinberg B.E., Alberts P., Lee Y.H., Chervonsky A.,
RA Mizushima N., Grinstein S., Iwasaki A.;
RT "In vivo requirement for Atg5 in antigen presentation by dendritic cells.";
RL Immunity 32:227-239(2010).
RN [16]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=24089209; DOI=10.1038/nature12639;
RA Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I.,
RA Codogno P., Satir B.H., Satir P., Cuervo A.M.;
RT "Functional interaction between autophagy and ciliogenesis.";
RL Nature 502:194-200(2013).
RN [17]
RP FUNCTION.
RX PubMed=24089205; DOI=10.1038/nature12606;
RA Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
RA Zhong Q.;
RT "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar
RT satellites.";
RL Nature 502:254-257(2013).
RN [18]
RP INTERACTION WITH BSN.
RX PubMed=28231469; DOI=10.1016/j.neuron.2017.01.026;
RA Okerlund N.D., Schneider K., Leal-Ortiz S., Montenegro-Venegas C.,
RA Kim S.A., Garner L.C., Waites C.L., Gundelfinger E.D., Reimer R.J.,
RA Garner C.C.;
RT "Bassoon Controls Presynaptic Autophagy through Atg5.";
RL Neuron 93:897-913(2017).
RN [19]
RP INTERACTION WITH ATG16L2, AND IDENTIFICATION IN A COMPLEX WITH ATG12 AND
RP ATG16L2.
RX PubMed=22082872; DOI=10.4161/auto.7.12.18025;
RA Ishibashi K., Fujita N., Kanno E., Omori H., Yoshimori T., Itoh T.,
RA Fukuda M.;
RT "Atg16L2, a novel isoform of mammalian Atg16L that is not essential for
RT canonical autophagy despite forming an Atg12-5-16L2 complex.";
RL Autophagy 7:1500-1513(2011).
CC -!- FUNCTION: Involved in autophagic vesicle formation. Conjugation with
CC ATG12, through a ubiquitin-like conjugating system involving ATG7 as an
CC E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme,
CC is essential for its function. The ATG12-ATG5 conjugate acts as an E3-
CC like enzyme which is required for lipidation of ATG8 family proteins
CC and their association to the vesicle membranes. Involved in
CC mitochondrial quality control after oxidative damage, and in subsequent
CC cellular longevity. Plays a critical role in multiple aspects of
CC lymphocyte development and is essential for both B and T lymphocyte
CC survival and proliferation. Required for optimal processing and
CC presentation of antigens for MHC II. Involved in the maintenance of
CC axon morphology and membrane structures, as well as in normal adipocyte
CC differentiation. Promotes primary ciliogenesis through removal of OFD1
CC from centriolar satellites and degradation of IFT20 via the autophagic
CC pathway. {ECO:0000269|PubMed:11266458, ECO:0000269|PubMed:12890687,
CC ECO:0000269|PubMed:17190837, ECO:0000269|PubMed:17912025,
CC ECO:0000269|PubMed:18188005, ECO:0000269|PubMed:19844159,
CC ECO:0000269|PubMed:20171125, ECO:0000269|PubMed:24089205,
CC ECO:0000269|PubMed:24089209}.
CC -!- FUNCTION: May play an important role in the apoptotic process, possibly
CC within the modified cytoskeleton. Its expression is a relatively late
CC event in the apoptotic process, occurring downstream of caspase
CC activity. Plays a crucial role in IFN-gamma-induced autophagic cell
CC death by interacting with FADD (By similarity).
CC {ECO:0000250|UniProtKB:Q9H1Y0}.
CC -!- FUNCTION: (Microbial infection) May act as a proviral factor. In
CC association with ATG12, negatively regulates the innate antiviral
CC immune response by impairing the type I IFN production pathway upon
CC vesicular stomatitis virus (VSV) infection.
CC {ECO:0000269|PubMed:17709747}.
CC -!- SUBUNIT: Forms a conjugate with ATG12 (PubMed:11266458,
CC PubMed:12890687, PubMed:12665549, PubMed:18768753, PubMed:19417210).
CC The ATG5-ATG12 conjugate forms a complex with several units of ATG16L1
CC (PubMed:12665549). Forms an 800-kDa complex composed of ATG12-ATG5 and
CC ATG16L2 (PubMed:22082872). Interacts with TECPR1; the interaction is
CC direct and does not take place when ATG16L1 is associated with the
CC ATG5-ATG12 conjugate (By similarity). Interacts with DHX58/RIG-1,
CC IFIH1/MDA5 and MAVS/IPS-1 in monomeric form as well as in ATG12-ATG5
CC conjugate form. The interaction with MAVS is further enhanced upon
CC vesicular stomatitis virus (VSV) infection (PubMed:17709747). Interacts
CC with ATG3 (By similarity). Interacts with ATG7 and ATG10
CC (PubMed:12482611). Interacts with FADD (By similarity). Interacts with
CC Bassoon/BSN; this interaction is important for the regulation of
CC presynaptic autophagy. Interacts with ATG16L2 (PubMed:22082872).
CC {ECO:0000250|UniProtKB:Q9H1Y0, ECO:0000269|PubMed:11266458,
CC ECO:0000269|PubMed:12482611, ECO:0000269|PubMed:12665549,
CC ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:17709747,
CC ECO:0000269|PubMed:18768753, ECO:0000269|PubMed:19417210,
CC ECO:0000269|PubMed:22082872, ECO:0000269|PubMed:28231469}.
CC -!- INTERACTION:
CC Q99J83; Q9CQY1: Atg12; NbExp=4; IntAct=EBI-2911848, EBI-2911788;
CC Q99J83; Q8C0J2: Atg16l1; NbExp=4; IntAct=EBI-2911848, EBI-769195;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24089209}.
CC Preautophagosomal structure membrane {ECO:0000269|PubMed:24089209};
CC Peripheral membrane protein {ECO:0000269|PubMed:24089209}. Note=The
CC conjugate detaches from the membrane immediately before or after
CC autophagosome formation is completed. Localizes also to discrete
CC punctae along the ciliary axoneme and to the base of the ciliary
CC axoneme.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Conjugated to ATG12; which is essential for autophagy, but is not
CC required for association with isolation membrane.
CC -!- PTM: Acetylated by EP300. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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DR EMBL; AB048349; BAB33383.1; -; mRNA.
DR EMBL; AK028315; BAC25874.1; -; mRNA.
DR EMBL; BC002166; AAH02166.1; -; mRNA.
DR CCDS; CCDS23824.1; -.
DR RefSeq; NP_001300942.1; NM_001314013.1.
DR RefSeq; NP_444299.1; NM_053069.6.
DR RefSeq; XP_011241410.1; XM_011243108.2.
DR AlphaFoldDB; Q99J83; -.
DR SMR; Q99J83; -.
DR BioGRID; 198146; 29.
DR ComplexPortal; CPX-328; Atg12-Atg5-Atg16l1 complex.
DR ComplexPortal; CPX-355; Atg12-Atg5-Atg16l2 complex.
DR ComplexPortal; CPX-357; Atg5-Atg12 complex.
DR ComplexPortal; CPX-360; ATG5-ATG12-TECPR1 complex.
DR CORUM; Q99J83; -.
DR DIP; DIP-46420N; -.
DR IntAct; Q99J83; 11.
DR MINT; Q99J83; -.
DR STRING; 10090.ENSMUSP00000044769; -.
DR iPTMnet; Q99J83; -.
DR PhosphoSitePlus; Q99J83; -.
DR EPD; Q99J83; -.
DR MaxQB; Q99J83; -.
DR PaxDb; Q99J83; -.
DR PeptideAtlas; Q99J83; -.
DR PRIDE; Q99J83; -.
DR ProteomicsDB; 277214; -.
DR Antibodypedia; 32129; 1072 antibodies from 43 providers.
DR DNASU; 11793; -.
DR Ensembl; ENSMUST00000039286; ENSMUSP00000044769; ENSMUSG00000038160.
DR GeneID; 11793; -.
DR KEGG; mmu:11793; -.
DR UCSC; uc007ezt.1; mouse.
DR CTD; 9474; -.
DR MGI; MGI:1277186; Atg5.
DR VEuPathDB; HostDB:ENSMUSG00000038160; -.
DR eggNOG; KOG2976; Eukaryota.
DR GeneTree; ENSGT00390000004766; -.
DR HOGENOM; CLU_051894_1_0_1; -.
DR InParanoid; Q99J83; -.
DR OMA; KWHYPLG; -.
DR OrthoDB; 457861at2759; -.
DR PhylomeDB; Q99J83; -.
DR TreeFam; TF314415; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-MMU-8934903; Receptor Mediated Mitophagy.
DR BioGRID-ORCS; 11793; 23 hits in 80 CRISPR screens.
DR ChiTaRS; Atg5; mouse.
DR PRO; PR:Q99J83; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q99J83; protein.
DR Bgee; ENSMUSG00000038160; Expressed in primary oocyte and 249 other tissues.
DR Genevisible; Q99J83; MM.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IDA:ComplexPortal.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990234; C:transferase complex; IDA:ComplexPortal.
DR GO; GO:0035973; P:aggrephagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0019883; P:antigen processing and presentation of endogenous antigen; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IMP:MGI.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IMP:ParkinsonsUK-UCL.
DR GO; GO:0009267; P:cellular response to starvation; IMP:MGI.
DR GO; GO:0061684; P:chaperone-mediated autophagy; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0060047; P:heart contraction; IMP:MGI.
DR GO; GO:0016236; P:macroautophagy; IMP:ComplexPortal.
DR GO; GO:0070254; P:mucus secretion; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IDA:ComplexPortal.
DR GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; IMP:MGI.
DR GO; GO:0045824; P:negative regulation of innate immune response; IDA:ComplexPortal.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:MGI.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032480; P:negative regulation of type I interferon production; IDA:ComplexPortal.
DR GO; GO:0039689; P:negative stranded viral RNA replication; IMP:MGI.
DR GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
DR GO; GO:0048840; P:otolith development; IMP:MGI.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IMP:MGI.
DR GO; GO:1904973; P:positive regulation of viral translation; ISO:MGI.
DR GO; GO:0043687; P:post-translational protein modification; IDA:UniProtKB.
DR GO; GO:0006497; P:protein lipidation; ISO:MGI.
DR GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; IMP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IMP:MGI.
DR GO; GO:1901096; P:regulation of autophagosome maturation; ISO:MGI.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0002718; P:regulation of cytokine production involved in immune response; IMP:MGI.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:MGI.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:1902617; P:response to fluoride; IEA:Ensembl.
DR GO; GO:0009620; P:response to fungus; IMP:MGI.
DR GO; GO:0010040; P:response to iron(II) ion; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0042311; P:vasodilation; IMP:MGI.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IMP:MGI.
DR Gene3D; 1.10.246.190; -; 1.
DR Gene3D; 3.10.20.620; -; 1.
DR InterPro; IPR007239; Atg5.
DR InterPro; IPR042526; Atg5_HR.
DR InterPro; IPR042527; Atg5_UblA_dom.
DR PANTHER; PTHR13040; PTHR13040; 1.
DR Pfam; PF04106; APG5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Autophagy; Cytoplasm; Immunity; Isopeptide bond;
KW Membrane; Reference proteome; Ubl conjugation.
FT CHAIN 1..275
FT /note="Autophagy protein 5"
FT /id="PRO_0000218995"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1Y0"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ATG12)"
FT /evidence="ECO:0000250"
FT MUTAGEN 130
FT /note="K->R: Loss of conjugation."
FT /evidence="ECO:0000269|PubMed:11266458"
SQ SEQUENCE 275 AA; 32402 MW; F3FCE652D627B694 CRC64;
MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLP RVSYLTLVTD KVKKHFQKVM
RQEDVSEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNI TVHFKSFPEK DLLHCPSKDA
VEAHFMSCMK EADALKHKSQ VINEMQKKDH KQLWMGLQND RFDQFWAINR KLMEYPPEEN
GFRYIPFRIY QTTTERPFIQ KLFRPVAADG QLHTLGDLLR EVCPSAVAPE DGEKRSQVMI
HGIEPMLETP LQWLSEHLSY PDNFLHISIV PQPTD
