MLP3B_HUMAN
ID MLP3B_HUMAN Reviewed; 125 AA.
AC Q9GZQ8; Q6NW02;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Microtubule-associated proteins 1A/1B light chain 3B {ECO:0000305};
DE AltName: Full=Autophagy-related protein LC3 B;
DE AltName: Full=Autophagy-related ubiquitin-like modifier LC3 B;
DE AltName: Full=MAP1 light chain 3-like protein 2;
DE AltName: Full=MAP1A/MAP1B light chain 3 B;
DE Short=MAP1A/MAP1B LC3 B;
DE AltName: Full=Microtubule-associated protein 1 light chain 3 beta;
DE Flags: Precursor;
GN Name=MAP1LC3B {ECO:0000312|HGNC:HGNC:13352}; Synonyms=MAP1ALC3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung carcinoma;
RX PubMed=12932674; DOI=10.1016/s0959-8049(03)00419-2;
RA Difilippantonio S., Chen Y., Pietas A., Schluens K., Pacyna-Gengelbach M.,
RA Deutschmann N., Padilla-Nash H.M., Ried T., Petersen I.;
RT "Gene expression profiles in human non-small and small-cell lung cancers.";
RL Eur. J. Cancer 39:1936-1947(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pheochromocytoma;
RX PubMed=14713272; DOI=10.1677/erc.0.0100621;
RA Yang Y.-S., Song H.-D., Peng Y.-D., Huang Q.-H., Li R.-Y., Zhu Z.-D.,
RA Hu R.-M., Han Z.-G., Chen J.-L.;
RT "The gene expression profiling of sporadic pheochromocytoma and novel full-
RT length cDNAs cloning.";
RL Endocr. Relat. Cancer 10:621-627(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CLEAVAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=12740394; DOI=10.1074/jbc.m303800200;
RA He H., Dang Y., Dai F., Guo Z., Wu J., She X., Pei Y., Chen Y., Ling W.,
RA Wu C., Zhao S., Liu J.O., Yu L.;
RT "Post-translational modifications of three members of the human MAP1LC3
RT family and detection of a novel type of modification for MAP1LC3B.";
RL J. Biol. Chem. 278:29278-29287(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Pancreas, and Testis;
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 [6]
RP LIPIDATION AT GLY-120, AND CLEAVAGE BY ATG4B.
RX PubMed=15187094; DOI=10.1074/jbc.m401461200;
RA Tanida I., Sou Y.-S., Ezaki J., Minematsu-Ikeguchi N., Ueno T.,
RA Kominami E.;
RT "HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human
RT Atg8 homologues and delipidates microtubule-associated protein light chain
RT 3- and GABAA receptor-associated protein-phospholipid conjugates.";
RL J. Biol. Chem. 279:36268-36276(2004).
RN [7]
RP CLEAVAGE, AND MUTAGENESIS OF GLY-120 AND LYS-122.
RX PubMed=15355958; DOI=10.1074/jbc.m407016200;
RA Tanida I., Ueno T., Kominami E.;
RT "Human light chain 3/MAP1LC3B is cleaved at its carboxyl-terminal Met121 to
RT expose Gly120 for lipidation and targeting to autophagosomal membranes.";
RL J. Biol. Chem. 279:47704-47710(2004).
RN [8]
RP REVIEW.
RX PubMed=15325588; DOI=10.1016/j.biocel.2004.05.009;
RA Tanida I., Ueno T., Kominami E.;
RT "LC3 conjugation system in mammalian autophagy.";
RL Int. J. Biochem. Cell Biol. 36:2503-2518(2004).
RN [9]
RP INTERACTION WITH CABP1.
RX PubMed=15095872; DOI=10.1016/j.jmb.2003.12.054;
RA Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M., Dieterich D.C.,
RA Zuschratter W., Reissner C., Hammarback J.A., Bockers T.M.,
RA Gundelfinger E.D., Kreutz M.R.;
RT "Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an
RT association with the microtubule cytoskeleton highlighting exclusive
RT binding partners for neuronal Ca(2+)-sensor proteins.";
RL J. Mol. Biol. 336:957-970(2004).
RN [10]
RP INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
RX PubMed=17580304; DOI=10.1074/jbc.m702824200;
RA Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H.,
RA Overvatn A., Bjorkoy G., Johansen T.;
RT "p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of
RT ubiquitinated protein aggregates by autophagy.";
RL J. Biol. Chem. 282:24131-24145(2007).
RN [11]
RP CLEAVAGE BY ATG4B.
RX PubMed=20818167; DOI=10.4161/auto.6.7.13075;
RA Shu C.W., Drag M., Bekes M., Zhai D., Salvesen G.S., Reed J.C.;
RT "Synthetic substrates for measuring activity of autophagy proteases:
RT autophagins (Atg4).";
RL Autophagy 6:936-947(2010).
RN [12]
RP FUNCTION.
RX PubMed=20418806; DOI=10.1038/emboj.2010.74;
RA Weidberg H., Shvets E., Shpilka T., Shimron F., Shinder V., Elazar Z.;
RT "LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently
RT in autophagosome biogenesis.";
RL EMBO J. 29:1792-1802(2010).
RN [13]
RP IDENTIFICATION IN A COMPLEX WITH UBQLN1 AND UBQLN2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20529957; DOI=10.1093/hmg/ddq231;
RA Rothenberg C., Srinivasan D., Mah L., Kaushik S., Peterhoff C.M.,
RA Ugolino J., Fang S., Cuervo A.M., Nixon R.A., Monteiro M.J.;
RT "Ubiquilin functions in autophagy and is degraded by chaperone-mediated
RT autophagy.";
RL Hum. Mol. Genet. 19:3219-3232(2010).
RN [14]
RP INTERACTION WITH FYCO1.
RX PubMed=20100911; DOI=10.1083/jcb.200907015;
RA Pankiv S., Alemu E.A., Brech A., Bruun J.A., Lamark T., Overvatn A.,
RA Bjorkoy G., Johansen T.;
RT "FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule
RT plus end-directed vesicle transport.";
RL J. Cell Biol. 188:253-269(2010).
RN [15]
RP INTERACTION WITH TECPR2, AND MUTAGENESIS OF 52-PHE-LYS-53 AND ARG-70.
RX PubMed=20562859; DOI=10.1038/nature09204;
RA Behrends C., Sowa M.E., Gygi S.P., Harper J.W.;
RT "Network organization of the human autophagy system.";
RL Nature 466:68-76(2010).
RN [16]
RP INTERACTION WITH TBC1D25.
RX PubMed=21383079; DOI=10.1083/jcb.201008107;
RA Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.;
RT "OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal
RT maturation.";
RL J. Cell Biol. 192:839-853(2011).
RN [17]
RP INTERACTION WITH MAPK15, AND PHOSPHORYLATION.
RX PubMed=22948227; DOI=10.4161/auto.21857;
RA Colecchia D., Strambi A., Sanzone S., Iavarone C., Rossi M., Dall'Armi C.,
RA Piccioni F., Verrotti di Pianella A., Chiariello M.;
RT "MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP
RT proteins.";
RL Autophagy 8:1724-1740(2012).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=22311637; DOI=10.1074/mcp.m111.014035;
RA Dengjel J., Hoyer-Hansen M., Nielsen M.O., Eisenberg T., Harder L.M.,
RA Schandorff S., Farkas T., Kirkegaard T., Becker A.C., Schroeder S.,
RA Vanselow K., Lundberg E., Nielsen M.M., Kristensen A.R., Akimov V.,
RA Bunkenborg J., Madeo F., Jaattela M., Andersen J.S.;
RT "Identification of autophagosome-associated proteins and regulators by
RT quantitative proteomic analysis and genetic screens.";
RL Mol. Cell. Proteomics 11:M111.014035.1-M111.014035.17(2012).
RN [19]
RP INTERACTION WITH TBC1D5.
RX PubMed=22354992; DOI=10.1128/mcb.06717-11;
RA Popovic D., Akutsu M., Novak I., Harper J.W., Behrends C., Dikic I.;
RT "Rab GTPase-activating proteins in autophagy: regulation of endocytic and
RT autophagy pathways by direct binding to human ATG8 modifiers.";
RL Mol. Cell. Biol. 32:1733-1744(2012).
RN [20]
RP FUNCTION, AND MUTAGENESIS OF ILE-35; PHE-52 AND GLY-120.
RX PubMed=22922758; DOI=10.1038/nchembio.1059;
RA Sentelle R.D., Senkal C.E., Jiang W., Ponnusamy S., Gencer S., Selvam S.P.,
RA Ramshesh V.K., Peterson Y.K., Lemasters J.J., Szulc Z.M., Bielawski J.,
RA Ogretmen B.;
RT "Ceramide targets autophagosomes to mitochondria and induces lethal
RT mitophagy.";
RL Nat. Chem. Biol. 8:831-838(2012).
RN [21]
RP INTERACTION WITH TP53INP1 AND TP53INP2.
RX PubMed=22470510; DOI=10.1371/journal.pone.0034034;
RA Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T.,
RA Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M.,
RA Johansen T., Zorzano A.;
RT "DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual
RT regulators of autophagy and transcription.";
RL PLoS ONE 7:E34034-E34034(2012).
RN [22]
RP DECONJUGATION BY LEGIONELLA RAVZ (MICROBIAL INFECTION).
RX PubMed=23112293; DOI=10.1126/science.1227026;
RA Choy A., Dancourt J., Mugo B., O'Connor T.J., Isberg R.R., Melia T.J.,
RA Roy C.R.;
RT "The Legionella effector RavZ inhibits host autophagy through irreversible
RT Atg8 deconjugation.";
RL Science 338:1072-1076(2012).
RN [23]
RP MUTAGENESIS OF ARG-68, AND CLEAVAGE BY ATG4B.
RX PubMed=23721406; DOI=10.1186/1471-2121-14-27;
RA Liu C., Ma H., Wu J., Huang Q., Liu J.O., Yu L.;
RT "Arginine68 is an essential residue for the C-terminal cleavage of human
RT Atg8 family proteins.";
RL BMC Cell Biol. 14:27-27(2013).
RN [24]
RP INTERACTION WITH UBQLN1 AND UBQLN4, AND SUBCELLULAR LOCATION.
RX PubMed=23459205; DOI=10.1038/embor.2013.22;
RA Lee D.Y., Arnott D., Brown E.J.;
RT "Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy
RT machinery.";
RL EMBO Rep. 14:373-381(2013).
RN [25]
RP INTERACTION WITH BNIP3, AND FUNCTION.
RX PubMed=23209295; DOI=10.1074/jbc.m112.399345;
RA Zhu Y., Massen S., Terenzio M., Lang V., Chen-Lindner S., Eils R.,
RA Novak I., Dikic I., Hamacher-Brady A., Brady N.R.;
RT "Modulation of serines 17 and 24 in the LC3-interacting region of Bnip3
RT determines pro-survival mitophagy versus apoptosis.";
RL J. Biol. Chem. 288:1099-1113(2013).
RN [26]
RP INTERACTION WITH MAPB1; FYCO1; SQSTM1; KEAP1; PCM1; OFD1 AND CEP131, AND
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 [27]
RP INTERACTION WITH SQSTM1, LACK OF INTERACTION WITH WDFY3, AND MUTAGENESIS OF
RP GLN-26; HIS-27 AND HIS-57.
RX PubMed=24668264; DOI=10.1002/embr.201338003;
RA Lystad A.H., Ichimura Y., Takagi K., Yang Y., Pankiv S., Kanegae Y.,
RA Kageyama S., Suzuki M., Saito I., Mizushima T., Komatsu M., Simonsen A.;
RT "Structural determinants in GABARAP required for the selective binding and
RT recruitment of ALFY to LC3B-positive structures.";
RL EMBO Rep. 15:557-565(2014).
RN [28]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AMBRA1.
RX PubMed=25215947; DOI=10.1038/cdd.2014.139;
RA Strappazzon F., Nazio F., Corrado M., Cianfanelli V., Romagnoli A.,
RA Fimia G.M., Campello S., Nardacci R., Piacentini M., Campanella M.,
RA Cecconi F.;
RT "AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN
RT and p62/SQSTM1.";
RL Cell Death Differ. 22:419-432(2015).
RN [29]
RP INTERACTION WITH KBTBD6 AND KBTBD7.
RX PubMed=25684205; DOI=10.1016/j.molcel.2014.12.040;
RA Genau H.M., Huber J., Baschieri F., Akutsu M., Doetsch V., Farhan H.,
RA Rogov V., Behrends C.;
RT "CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to
RT spatially restrict TIAM1-RAC1 signaling.";
RL Mol. Cell 57:995-1010(2015).
RN [30]
RP INTERACTION WITH RETREG1; RETREG2 AND RETREG3.
RX PubMed=26040720; DOI=10.1038/nature14498;
RA Khaminets A., Heinrich T., Mari M., Grumati P., Huebner A.K., Akutsu M.,
RA Liebmann L., Stolz A., Nietzsche S., Koch N., Mauthe M., Katona I.,
RA Qualmann B., Weis J., Reggiori F., Kurth I., Huebner C.A., Dikic I.;
RT "Regulation of endoplasmic reticulum turnover by selective autophagy.";
RL Nature 522:354-358(2015).
RN [31]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PHB AND PHB2.
RX PubMed=28017329; DOI=10.1016/j.cell.2016.11.042;
RA Wei Y., Chiang W.C., Sumpter R. Jr., Mishra P., Levine B.;
RT "Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor.";
RL Cell 168:224.e10-238.e10(2017).
RN [32]
RP PROTEOLYTIC CLEAVAGE, DELIPIDATION, AND LIPIDATION AT GLY-120.
RX PubMed=29458288; DOI=10.1080/15548627.2018.1437341;
RA Kauffman K.J., Yu S., Jin J., Mugo B., Nguyen N., O'Brien A., Nag S.,
RA Lystad A.H., Melia T.J.;
RT "Delipidation of mammalian Atg8-family proteins by each of the four ATG4
RT proteases.";
RL Autophagy 14:992-1010(2018).
RN [33]
RP INTERACTION WITH TRIM16.
RX PubMed=30143514; DOI=10.15252/embj.201798358;
RA Jena K.K., Kolapalli S.P., Mehto S., Nath P., Das B., Sahoo P.K., Ahad A.,
RA Syed G.H., Raghav S.K., Senapati S., Chauhan S., Chauhan S.;
RT "TRIM16 controls assembly and degradation of protein aggregates by
RT modulating the p62-NRF2 axis and autophagy.";
RL EMBO J. 37:0-0(2018).
RN [34]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=30661429; DOI=10.1080/15548627.2019.1569925;
RA Agrotis A., Pengo N., Burden J.J., Ketteler R.;
RT "Redundancy of human ATG4 protease isoforms in autophagy and LC3/GABARAP
RT processing revealed in cells.";
RL Autophagy 15:976-997(2019).
RN [35]
RP SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF
RP 80-PHE--LEU-82; GLN-116 AND PHE-119.
RX PubMed=31315929; DOI=10.1074/jbc.ac119.009977;
RA Agrotis A., von Chamier L., Oliver H., Kiso K., Singh T., Ketteler R.;
RT "Human ATG4 autophagy proteases counteract attachment of ubiquitin-like
RT LC3/GABARAP proteins to other cellular proteins.";
RL J. Biol. Chem. 294:12610-12621(2019).
RN [36]
RP FUNCTION, INTERACTION WITH JMY, AND SUBCELLULAR LOCATION.
RX PubMed=30420355; DOI=10.1083/jcb.201802157;
RA Hu X., Mullins R.D.;
RT "LC3 and STRAP regulate actin filament assembly by JMY during autophagosome
RT formation.";
RL J. Cell Biol. 218:251-266(2019).
RN [37]
RP INTERACTION WITH TEX264; FUNCTION.
RX PubMed=31006538; DOI=10.1016/j.molcel.2019.03.033;
RA Chino H., Hatta T., Natsume T., Mizushima N.;
RT "Intrinsically disordered protein TEX264 mediates ER-phagy.";
RL Mol. Cell 0:0-0(2019).
RN [38]
RP INTERACTION WITH TEX264; FUNCTION.
RX PubMed=31006537; DOI=10.1016/j.molcel.2019.03.034;
RA An H., Ordureau A., Paulo J.A., Shoemaker C.J., Denic V., Harper J.W.;
RT "TEX264 is an endoplasmic reticulum-resident ATG8-interacting protein
RT critical for ER remodeling during nutrient stress.";
RL Mol. Cell 0:0-0(2019).
RN [39]
RP SUBCELLULAR LOCATION.
RX PubMed=33499712; DOI=10.1080/15548627.2021.1874133;
RA Kojima W., Yamano K., Kosako H., Imai K., Kikuchi R., Tanaka K.,
RA Matsuda N.;
RT "Mammalian BCAS3 and C16orf70 associate with the phagophore assembly site
RT in response to selective and non-selective autophagy.";
RL Autophagy 1:1-26(2021).
RN [40]
RP DECONJUGATION BY LEGIONELLA RAVZ (MICROBIAL INFECTION).
RX PubMed=31722778; DOI=10.5483/bmbrep.2019.52.12.211;
RA Park S.W., Jun Y.W., Jeon P., Lee Y.K., Park J.H., Lee S.H., Lee J.A.,
RA Jang D.J.;
RT "LIR motifs and the membrane-targeting domain are complementary in the
RT function of RavZ.";
RL BMB Rep. 52:700-705(2019).
RN [41]
RP INTERACTION WITH HANTAAN HANTAVIRUS GLYCOPROTEIN N (MICROBIAL INFECTION),
RP AND INTERACTION WITH HANTAAN HANTAVIRUS NUCLEOPROTEIN (MICROBIAL
RP INFECTION).
RX PubMed=31091447; DOI=10.1016/j.celrep.2019.04.061;
RA Wang K., Ma H., Liu H., Ye W., Li Z., Cheng L., Zhang L., Lei Y., Shen L.,
RA Zhang F.;
RT "The Glycoprotein and Nucleocapsid Protein of Hantaviruses Manipulate
RT Autophagy Flux to Restrain Host Innate Immune Responses.";
RL Cell Rep. 27:2075-2091.e5(2019).
RN [42]
RP INTERACTION WITH MOAP1.
RX PubMed=33783314; DOI=10.1080/15548627.2021.1896157;
RA Chang H.C., Tao R.N., Tan C.T., Wu Y.J., Bay B.H., Yu V.C.;
RT "The BAX-binding protein MOAP1 associates with LC3 and promotes closure of
RT the phagophore.";
RL Autophagy 17:3725-3739(2021).
RN [43]
RP LIPIDATION AT GLY-120.
RX PubMed=33909989; DOI=10.1016/j.molcel.2021.03.020;
RA Durgan J., Lystad A.H., Sloan K., Carlsson S.R., Wilson M.I., Marcassa E.,
RA Ulferts R., Webster J., Lopez-Clavijo A.F., Wakelam M.J., Beale R.,
RA Simonsen A., Oxley D., Florey O.;
RT "Non-canonical autophagy drives alternative ATG8 conjugation to
RT phosphatidylserine.";
RL Mol. Cell 81:2031-2040(2021).
RN [44]
RP STRUCTURE BY NMR OF 1-120.
RX PubMed=15857831; DOI=10.1074/jbc.m413565200;
RA Kouno T., Mizuguchi M., Tanida I., Ueno T., Kanematsu T., Mori Y.,
RA Shinoda H., Hirata M., Kominami E., Kawano K.;
RT "Solution structure of microtubule-associated protein light chain 3 and
RT identification of its functional subdomains.";
RL J. Biol. Chem. 280:24610-24617(2005).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH SQSTM1 PEPTIDE, AND
RP INTERACTION WITH SQSTM1.
RX PubMed=18524774; DOI=10.1074/jbc.m802182200;
RA Ichimura Y., Kumanomidou T., Sou Y.S., Mizushima T., Ezaki J., Ueno T.,
RA Kominami E., Yamane T., Tanaka K., Komatsu M.;
RT "Structural basis for sorting mechanism of p62 in selective autophagy.";
RL J. Biol. Chem. 283:22847-22857(2008).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-119, AND INTERACTION WITH
RP ATG13.
RX PubMed=24290141; DOI=10.1016/j.str.2013.09.023;
RA Suzuki H., Tabata K., Morita E., Kawasaki M., Kato R., Dobson R.C.,
RA Yoshimori T., Wakatsuki S.;
RT "Structural basis of the autophagy-related LC3/Atg13 LIR complex:
RT recognition and interaction mechanism.";
RL Structure 22:47-58(2014).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-120 IN COMPLEX WITH
RP L.PNEUMOPHILA RAVZ, AND MUTAGENESIS OF HIS-27.
RX PubMed=28668392; DOI=10.1016/j.bbrc.2017.06.173;
RA Kwon D.H., Kim L., Kim B.W., Kim J.H., Roh K.H., Choi E.J., Song H.K.;
RT "A novel conformation of the LC3-interacting region motif revealed by the
RT structure of a complex between LC3B and RavZ.";
RL Biochem. Biophys. Res. Commun. 490:1093-1099(2017).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 3-119 IN COMPLEX WITH
RP L.PNEUMOPHILA RAVZ, AND DECONJUGATION BY LEGIONELLA RAVZ (MICROBIAL
RP INFECTION).
RX PubMed=28395732; DOI=10.7554/elife.23905;
RA Yang A., Pantoom S., Wu Y.W.;
RT "Elucidation of the anti-autophagy mechanism of the Legionella effector
RT RavZ using semisynthetic LC3 proteins.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Ubiquitin-like modifier involved in formation of
CC autophagosomal vacuoles (autophagosomes) (PubMed:20418806,
CC PubMed:23209295, PubMed:28017329). Plays a role in mitophagy which
CC contributes to regulate mitochondrial quantity and quality by
CC eliminating the mitochondria to a basal level to fulfill cellular
CC energy requirements and preventing excess ROS production
CC (PubMed:23209295, PubMed:28017329). In response to cellular stress and
CC upon mitochondria fission, binds C-18 ceramides and anchors
CC autophagolysosomes to outer mitochondrial membranes to eliminate
CC damaged mitochondria (PubMed:22922758). While LC3s are involved in
CC elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is
CC essential for a later stage in autophagosome maturation
CC (PubMed:20418806, PubMed:23209295, PubMed:28017329). Promotes primary
CC ciliogenesis by removing OFD1 from centriolar satellites via the
CC autophagic pathway (PubMed:24089205). Through its interaction with the
CC reticulophagy receptor TEX264, participates in the remodeling of
CC subdomains of the endoplasmic reticulum into autophagosomes upon
CC nutrient stress, which then fuse with lysosomes for endoplasmic
CC reticulum turnover (PubMed:31006537, PubMed:31006538). Upon nutrient
CC stress, directly recruits cofactor JMY to the phagophore membrane
CC surfaces and promotes JMY's actin nucleation activity and autophagosome
CC biogenesis during autophagy (PubMed:30420355).
CC {ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:22922758,
CC ECO:0000269|PubMed:23209295, ECO:0000269|PubMed:24089205,
CC ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:30420355,
CC ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}.
CC -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with
CC MAP1A and MAP1B proteins (By similarity). Interacts at microtubules
CC with CABP1 (via EF-hands 1 and 2) but not with calmodulin
CC (PubMed:15095872). Interacts with FYCO1 (via C-terminus)
CC (PubMed:20100911, PubMed:24089205). Interacts with TP53INP1 and
CC TP53INP2 (PubMed:22470510). Interacts with TBC1D25 (PubMed:21383079).
CC Directly interacts with SQSTM1; this interaction leads to MAP1LC3B
CC recruitment to inclusion bodies containing polyubiquitinated protein
CC aggregates and to inclusion body degradation by autophagy
CC (PubMed:17580304, PubMed:24089205, PubMed:24668264, PubMed:18524774).
CC Interacts with ATG4B, MAPK15 and BNIP3 (PubMed:22948227,
CC PubMed:23209295). Interacts with MAPB1, KEAP1, PCM1, OFD1, CEP131, and
CC TECPR2 (PubMed:20562859, PubMed:24089205). Interacts with TBC1D5
CC (PubMed:22354992). Found in a complex with UBQLN1 and UBQLN2
CC (PubMed:20529957). Interacts with UBQLN4 (via STI1 1 and 2 domains).
CC Interacts with UBQLN1 in the presence of UBQLN4 (PubMed:23459205).
CC Interacts with ATG13 (PubMed:24290141). Interacts with RETREG2, RETREG1
CC and RETREG3 (PubMed:26040720). No interaction, or very weak, with WDFY3
CC (PubMed:24668264). Interacts with PLCL1; the interaction inhibits
CC autophagosome formation (By similarity). Interacts with TRIM16
CC (PubMed:30143514). Interacts with CRY1 and PER2 (By similarity).
CC Interacts with the reticulophagy receptor TEX264 (PubMed:31006538,
CC PubMed:31006537). Membrane-bound form LC3-II interacts with PHB and
CC PHB2; the interaction takes place upon Parkin-mediated mitochondrial
CC damage (PubMed:28017329). Interacts with PJVK; the interaction is
CC direct (By similarity). Interacts with KBTBD6 and KBTBD7; the
CC interaction is direct (PubMed:25684205). Interacts with AMBRA1 (via LIR
CC motif) (PubMed:25215947). Interacts with JMY; the interaction results
CC in the activation of JYM's nucleation activity in the cytoplasm
CC (PubMed:30420355). Interacts with MOAP1 (via LIR motif)
CC (PubMed:33783314). {ECO:0000250|UniProtKB:Q62625,
CC ECO:0000250|UniProtKB:Q9CQV6, ECO:0000269|PubMed:15095872,
CC ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:18524774,
CC ECO:0000269|PubMed:20100911, ECO:0000269|PubMed:20529957,
CC ECO:0000269|PubMed:20562859, ECO:0000269|PubMed:21383079,
CC ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:22470510,
CC ECO:0000269|PubMed:22948227, ECO:0000269|PubMed:23209295,
CC ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:24089205,
CC ECO:0000269|PubMed:24290141, ECO:0000269|PubMed:24668264,
CC ECO:0000269|PubMed:25215947, ECO:0000269|PubMed:25684205,
CC ECO:0000269|PubMed:26040720, ECO:0000269|PubMed:28017329,
CC ECO:0000269|PubMed:30143514, ECO:0000269|PubMed:30420355,
CC ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538,
CC ECO:0000269|PubMed:33783314}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Hantaan hantavirus
CC glycoprotein N; this interaction contributes to the virus-induced
CC degradation of mitochondria by autophagy, which leads to degradation of
CC host MAVS and inhibition of type I interferon (IFN) responses.
CC {ECO:0000269|PubMed:31091447}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Hantaan hantavirus
CC nucleoprotein; this interaction prevents the breakdown of the viral
CC glycoprotein N by virus-triggered autophagy.
CC {ECO:0000269|PubMed:31091447}.
CC -!- INTERACTION:
CC Q9GZQ8; P05067: APP; NbExp=3; IntAct=EBI-373144, EBI-77613;
CC Q9GZQ8; O75143: ATG13; NbExp=5; IntAct=EBI-373144, EBI-2798775;
CC Q9GZQ8; Q676U5: ATG16L1; NbExp=2; IntAct=EBI-373144, EBI-535909;
CC Q9GZQ8; Q2TAZ0: ATG2A; NbExp=2; IntAct=EBI-373144, EBI-2514077;
CC Q9GZQ8; Q9NT62: ATG3; NbExp=7; IntAct=EBI-373144, EBI-988094;
CC Q9GZQ8; Q9Y4P1: ATG4B; NbExp=14; IntAct=EBI-373144, EBI-712014;
CC Q9GZQ8; Q9H1Y0: ATG5; NbExp=2; IntAct=EBI-373144, EBI-1047414;
CC Q9GZQ8; O95352: ATG7; NbExp=7; IntAct=EBI-373144, EBI-987834;
CC Q9GZQ8; Q03135: CAV1; NbExp=2; IntAct=EBI-373144, EBI-603614;
CC Q9GZQ8; P28329-3: CHAT; NbExp=3; IntAct=EBI-373144, EBI-25837549;
CC Q9GZQ8; Q14677: CLINT1; NbExp=2; IntAct=EBI-373144, EBI-1171113;
CC Q9GZQ8; P35222: CTNNB1; NbExp=5; IntAct=EBI-373144, EBI-491549;
CC Q9GZQ8; O14576-2: DYNC1I1; NbExp=3; IntAct=EBI-373144, EBI-25840445;
CC Q9GZQ8; P22607: FGFR3; NbExp=3; IntAct=EBI-373144, EBI-348399;
CC Q9GZQ8; Q8IVP5: FUNDC1; NbExp=8; IntAct=EBI-373144, EBI-3059266;
CC Q9GZQ8; Q9BQS8: FYCO1; NbExp=8; IntAct=EBI-373144, EBI-2869338;
CC Q9GZQ8; Q9H8Y8: GORASP2; NbExp=6; IntAct=EBI-373144, EBI-739467;
CC Q9GZQ8; P28799: GRN; NbExp=3; IntAct=EBI-373144, EBI-747754;
CC Q9GZQ8; P40939: HADHA; NbExp=4; IntAct=EBI-373144, EBI-356720;
CC Q9GZQ8; P0DMV8: HSPA1A; NbExp=3; IntAct=EBI-373144, EBI-11052499;
CC Q9GZQ8; O00410: IPO5; NbExp=2; IntAct=EBI-373144, EBI-356424;
CC Q9GZQ8; Q8WZA9: IRGQ; NbExp=3; IntAct=EBI-373144, EBI-1055331;
CC Q9GZQ8; Q86V97: KBTBD6; NbExp=2; IntAct=EBI-373144, EBI-2514778;
CC Q9GZQ8; Q8WVZ9: KBTBD7; NbExp=4; IntAct=EBI-373144, EBI-473695;
CC Q9GZQ8; Q01546: KRT76; NbExp=2; IntAct=EBI-373144, EBI-2952745;
CC Q9GZQ8; Q9BQD3: KXD1; NbExp=4; IntAct=EBI-373144, EBI-739657;
CC Q9GZQ8; P20700: LMNB1; NbExp=14; IntAct=EBI-373144, EBI-968218;
CC Q9GZQ8; Q9Y383: LUC7L2; NbExp=3; IntAct=EBI-373144, EBI-352851;
CC Q9GZQ8; Q14696: MESD; NbExp=3; IntAct=EBI-373144, EBI-6165891;
CC Q9GZQ8; Q14596: NBR1; NbExp=9; IntAct=EBI-373144, EBI-742698;
CC Q9GZQ8; P46934: NEDD4; NbExp=3; IntAct=EBI-373144, EBI-726944;
CC Q9GZQ8; Q8TD19: NEK9; NbExp=3; IntAct=EBI-373144, EBI-1044009;
CC Q9GZQ8; O75323: NIPSNAP2; NbExp=4; IntAct=EBI-373144, EBI-307133;
CC Q9GZQ8; O75665: OFD1; NbExp=7; IntAct=EBI-373144, EBI-716327;
CC Q9GZQ8; Q9BXM7: PINK1; NbExp=3; IntAct=EBI-373144, EBI-2846068;
CC Q9GZQ8; O60260-5: PRKN; NbExp=3; IntAct=EBI-373144, EBI-21251460;
CC Q9GZQ8; Q9NS23: RASSF1; NbExp=2; IntAct=EBI-373144, EBI-367363;
CC Q9GZQ8; Q8WWW0: RASSF5; NbExp=5; IntAct=EBI-373144, EBI-367390;
CC Q9GZQ8; Q8NC44: RETREG2; NbExp=2; IntAct=EBI-373144, EBI-712899;
CC Q9GZQ8; Q15424: SAFB; NbExp=3; IntAct=EBI-373144, EBI-348298;
CC Q9GZQ8; Q14151: SAFB2; NbExp=3; IntAct=EBI-373144, EBI-352869;
CC Q9GZQ8; Q96EB6: SIRT1; NbExp=2; IntAct=EBI-373144, EBI-1802965;
CC Q9GZQ8; Q13501: SQSTM1; NbExp=26; IntAct=EBI-373144, EBI-307104;
CC Q9GZQ8; O95210: STBD1; NbExp=2; IntAct=EBI-373144, EBI-2947137;
CC Q9GZQ8; Q13188: STK3; NbExp=5; IntAct=EBI-373144, EBI-992580;
CC Q9GZQ8; Q13043: STK4; NbExp=7; IntAct=EBI-373144, EBI-367376;
CC Q9GZQ8; Q8TC07: TBC1D15; NbExp=2; IntAct=EBI-373144, EBI-1048247;
CC Q9GZQ8; Q9UPU7: TBC1D2B; NbExp=3; IntAct=EBI-373144, EBI-2947180;
CC Q9GZQ8; Q15025: TNIP1; NbExp=4; IntAct=EBI-373144, EBI-357849;
CC Q9GZQ8; Q8WZ42: TTN; NbExp=4; IntAct=EBI-373144, EBI-681210;
CC Q9GZQ8; Q9GZZ9: UBA5; NbExp=2; IntAct=EBI-373144, EBI-747805;
CC Q9GZQ8; O75385: ULK1; NbExp=3; IntAct=EBI-373144, EBI-908831;
CC Q9GZQ8; Q8IZQ1: WDFY3; NbExp=6; IntAct=EBI-373144, EBI-1569256;
CC Q9GZQ8; P40344: ATG3; Xeno; NbExp=2; IntAct=EBI-373144, EBI-3381;
CC Q9GZQ8; P38862: ATG7; Xeno; NbExp=2; IntAct=EBI-373144, EBI-2677;
CC Q9GZQ8; Q9Z2F7: Bnip3l; Xeno; NbExp=5; IntAct=EBI-373144, EBI-1774669;
CC Q9GZQ8; P97432: Nbr1; Xeno; NbExp=2; IntAct=EBI-373144, EBI-642554;
CC Q9GZQ8; Q64337: Sqstm1; Xeno; NbExp=6; IntAct=EBI-373144, EBI-645025;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:20529957,
CC ECO:0000269|PubMed:22311637, ECO:0000269|PubMed:23459205,
CC ECO:0000269|PubMed:31315929, ECO:0000269|PubMed:33499712}; Lipid-anchor
CC {ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:29458288}.
CC Endomembrane system {ECO:0000269|PubMed:12740394}; Lipid-anchor
CC {ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:29458288}.
CC Mitochondrion membrane {ECO:0000269|PubMed:25215947,
CC ECO:0000269|PubMed:28017329}; Lipid-anchor
CC {ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:29458288}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q9CQV6}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:30420355}. Note=LC3-II binds to the autophagic
CC membranes. LC3-II localizes with the mitochondrial inner membrane
CC during Parkin-mediated mitophagy (PubMed:28017329). Localizes also to
CC discrete punctae along the ciliary axoneme.
CC {ECO:0000269|PubMed:28017329}.
CC -!- TISSUE SPECIFICITY: Most abundant in heart, brain, skeletal muscle and
CC testis. Little expression observed in liver.
CC {ECO:0000269|PubMed:12740394}.
CC -!- PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or
CC ATG4D) to expose the glycine at the C-terminus and form the cytosolic
CC form, LC3-I (PubMed:15187094, PubMed:15355958, PubMed:20818167,
CC PubMed:29458288, PubMed:30661429, PubMed:31315929). The processed form
CC is then activated by APG7L/ATG7, transferred to ATG3 and conjugated to
CC phosphatidylethanolamine (PE) phospholipid to form the membrane-bound
CC form, LC3-II (PubMed:15187094). During non-canonical autophagy, the
CC processed form is conjugated to phosphatidylserine (PS) phospholipid
CC (PubMed:33909989). ATG4 proteins also mediate the delipidation of PE-
CC conjugated forms (PubMed:29458288, PubMed:33909989). In addition, ATG4B
CC and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during
CC non-canonical autophagy (PubMed:33909989). ATG4B constitutes the major
CC protein for proteolytic activation (PubMed:30661429). ATG4D is the main
CC enzyme for delipidation activity (By similarity).
CC {ECO:0000250|UniProtKB:Q9CQV6, ECO:0000269|PubMed:15187094,
CC ECO:0000269|PubMed:15355958, ECO:0000269|PubMed:20818167,
CC ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:30661429,
CC ECO:0000269|PubMed:31315929, ECO:0000269|PubMed:33909989}.
CC -!- PTM: (Microbial infection) The Legionella effector RavZ is a
CC deconjugating enzyme that hydrolyzes the amide bond between the C-
CC terminal glycine residue and an adjacent aromatic residue in ATG8
CC proteins conjugated to phosphatidylethanolamine (PE), producing an ATG8
CC protein that is resistant to reconjugation by the host machinery due to
CC the cleavage of the reactive C-terminal glycine (PubMed:23112293,
CC PubMed:28395732, PubMed:31722778). RavZ is also able to mediate
CC delipidation of ATG8 proteins conjugated to phosphatidylserine (PS)
CC (PubMed:33909989). {ECO:0000269|PubMed:23112293,
CC ECO:0000269|PubMed:28395732, ECO:0000269|PubMed:31722778,
CC ECO:0000269|PubMed:33909989}.
CC -!- PTM: Phosphorylation by PKA inhibits conjugation of
CC phosphatidylethanolamine (PE) (PubMed:22948227). Interaction with
CC MAPK15 reduces the inhibitory phosphorylation and increases autophagy
CC activity (PubMed:22948227). {ECO:0000269|PubMed:22948227}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
CC -!- CAUTION: PubMed:12740394 has shown that the protein is cleaved at Lys-
CC 122 but PubMed:15355958 has shown that the cleavage site is at Gly-120
CC as in other mammalian orthologs. {ECO:0000269|PubMed:12740394,
CC ECO:0000269|PubMed:22948227}.
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DR EMBL; AF303888; AAG23182.1; -; mRNA.
DR EMBL; AF183417; AAG09686.1; -; mRNA.
DR EMBL; AF087871; AAM10499.1; -; mRNA.
DR EMBL; AK025556; BAB15169.1; -; mRNA.
DR EMBL; BC018634; AAH18634.1; -; mRNA.
DR EMBL; BC041874; AAH41874.1; -; mRNA.
DR EMBL; BC067797; AAH67797.1; -; mRNA.
DR CCDS; CCDS10960.1; -.
DR RefSeq; NP_073729.1; NM_022818.4.
DR PDB; 1V49; NMR; -; A=1-120.
DR PDB; 2LUE; NMR; -; A=5-119.
DR PDB; 2N9X; NMR; -; A=1-120.
DR PDB; 2ZJD; X-ray; 1.56 A; A/C=1-125.
DR PDB; 3VTU; X-ray; 1.60 A; A=2-119.
DR PDB; 3VTV; X-ray; 1.70 A; A=2-119.
DR PDB; 3VTW; X-ray; 2.52 A; A/B/C=2-119.
DR PDB; 3WAO; X-ray; 2.60 A; A/B/C/D=2-119.
DR PDB; 3X0W; X-ray; 2.71 A; A/B=2-119.
DR PDB; 4WAA; X-ray; 2.35 A; A/B=2-119.
DR PDB; 5D94; X-ray; 1.53 A; A=1-125.
DR PDB; 5DCN; X-ray; 2.00 A; A=2-119.
DR PDB; 5GMV; X-ray; 2.25 A; A/B=1-125.
DR PDB; 5MS2; X-ray; 2.47 A; B=1-119.
DR PDB; 5MS5; X-ray; 1.53 A; A/B=2-119.
DR PDB; 5MS6; X-ray; 1.90 A; A/B=2-119.
DR PDB; 5V4K; X-ray; 2.10 A; A/B=2-119.
DR PDB; 5W9A; X-ray; 2.74 A; C/D=4-117.
DR PDB; 5XAC; X-ray; 1.70 A; A/B/C/D=2-120.
DR PDB; 5XAD; X-ray; 1.88 A; A/B=2-120.
DR PDB; 5XAE; X-ray; 2.00 A; A/B/C/D=2-120.
DR PDB; 6J04; X-ray; 1.90 A; A/B/C/D=2-125.
DR PDB; 6LAN; X-ray; 1.41 A; A=2-125.
DR PDB; 7ELG; X-ray; 1.60 A; A=2-119.
DR PDBsum; 1V49; -.
DR PDBsum; 2LUE; -.
DR PDBsum; 2N9X; -.
DR PDBsum; 2ZJD; -.
DR PDBsum; 3VTU; -.
DR PDBsum; 3VTV; -.
DR PDBsum; 3VTW; -.
DR PDBsum; 3WAO; -.
DR PDBsum; 3X0W; -.
DR PDBsum; 4WAA; -.
DR PDBsum; 5D94; -.
DR PDBsum; 5DCN; -.
DR PDBsum; 5GMV; -.
DR PDBsum; 5MS2; -.
DR PDBsum; 5MS5; -.
DR PDBsum; 5MS6; -.
DR PDBsum; 5V4K; -.
DR PDBsum; 5W9A; -.
DR PDBsum; 5XAC; -.
DR PDBsum; 5XAD; -.
DR PDBsum; 5XAE; -.
DR PDBsum; 6J04; -.
DR PDBsum; 6LAN; -.
DR PDBsum; 7ELG; -.
DR AlphaFoldDB; Q9GZQ8; -.
DR BMRB; Q9GZQ8; -.
DR SMR; Q9GZQ8; -.
DR BioGRID; 123565; 499.
DR DIP; DIP-29760N; -.
DR ELM; Q9GZQ8; -.
DR IntAct; Q9GZQ8; 469.
DR MINT; Q9GZQ8; -.
DR STRING; 9606.ENSP00000268607; -.
DR BindingDB; Q9GZQ8; -.
DR iPTMnet; Q9GZQ8; -.
DR PhosphoSitePlus; Q9GZQ8; -.
DR SwissPalm; Q9GZQ8; -.
DR BioMuta; MAP1LC3B; -.
DR DMDM; 17433141; -.
DR EPD; Q9GZQ8; -.
DR jPOST; Q9GZQ8; -.
DR MassIVE; Q9GZQ8; -.
DR MaxQB; Q9GZQ8; -.
DR PaxDb; Q9GZQ8; -.
DR PeptideAtlas; Q9GZQ8; -.
DR PRIDE; Q9GZQ8; -.
DR ProteomicsDB; 80115; -.
DR TopDownProteomics; Q9GZQ8; -.
DR Antibodypedia; 30678; 1212 antibodies from 41 providers.
DR DNASU; 81631; -.
DR Ensembl; ENST00000268607.10; ENSP00000268607.5; ENSG00000140941.14.
DR Ensembl; ENST00000650688.1; ENSP00000498476.1; ENSG00000140941.14.
DR GeneID; 81631; -.
DR KEGG; hsa:81631; -.
DR MANE-Select; ENST00000268607.10; ENSP00000268607.5; NM_022818.5; NP_073729.1.
DR UCSC; uc002fjx.4; human.
DR CTD; 81631; -.
DR DisGeNET; 81631; -.
DR GeneCards; MAP1LC3B; -.
DR HGNC; HGNC:13352; MAP1LC3B.
DR HPA; ENSG00000140941; Low tissue specificity.
DR MIM; 609604; gene.
DR neXtProt; NX_Q9GZQ8; -.
DR OpenTargets; ENSG00000140941; -.
DR PharmGKB; PA134923100; -.
DR VEuPathDB; HostDB:ENSG00000140941; -.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000154158; -.
DR HOGENOM; CLU_119276_1_0_1; -.
DR InParanoid; Q9GZQ8; -.
DR OMA; EFSHDER; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; Q9GZQ8; -.
DR TreeFam; TF312964; -.
DR PathwayCommons; Q9GZQ8; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-HSA-9664873; Pexophagy.
DR Reactome; R-HSA-9679504; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR Reactome; R-HSA-9694676; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR Reactome; R-HSA-9754560; SARS-CoV-2 modulates autophagy.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR SABIO-RK; Q9GZQ8; -.
DR SignaLink; Q9GZQ8; -.
DR SIGNOR; Q9GZQ8; -.
DR BioGRID-ORCS; 81631; 131 hits in 1046 CRISPR screens.
DR ChiTaRS; MAP1LC3B; human.
DR EvolutionaryTrace; Q9GZQ8; -.
DR GeneWiki; MAP1LC3B; -.
DR GenomeRNAi; 81631; -.
DR Pharos; Q9GZQ8; Tbio.
DR PRO; PR:Q9GZQ8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9GZQ8; protein.
DR Bgee; ENSG00000140941; Expressed in paraflocculus and 202 other tissues.
DR ExpressionAtlas; Q9GZQ8; baseline and differential.
DR Genevisible; Q9GZQ8; HS.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031090; C:organelle membrane; ISS:UniProtKB.
DR GO; GO:0097001; F:ceramide binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IDA:UniProtKB.
DR GO; GO:0006914; P:autophagy; IDA:CAFA.
DR GO; GO:0000422; P:autophagy of mitochondrion; IGI:ParkinsonsUK-UCL.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IDA:UniProtKB.
DR GO; GO:0000423; P:mitophagy; IDA:UniProtKB.
DR IDEAL; IID00346; -.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR Pfam; PF02991; ATG8; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Lipoprotein; Membrane; Microtubule; Mitochondrion; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..120
FT /note="Microtubule-associated proteins 1A/1B light chain
FT 3B"
FT /id="PRO_0000017198"
FT PROPEP 121..125
FT /note="Removed in mature form"
FT /id="PRO_0000017199"
FT SITE 120..121
FT /note="Cleavage; by ATG4B"
FT /evidence="ECO:0000269|PubMed:15355958"
FT LIPID 120
FT /note="Phosphatidylethanolamine amidated glycine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:33909989,
FT ECO:0000305|PubMed:15187094, ECO:0000305|PubMed:29458288"
FT LIPID 120
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000269|PubMed:33909989"
FT MUTAGEN 26
FT /note="Q->K: Increased interaction with WDFY3/ALFY, no
FT effect on SQSTM1-binding; when associated with Y-27 and D-
FT 57."
FT /evidence="ECO:0000269|PubMed:24668264"
FT MUTAGEN 27
FT /note="H->A: Decreased interaction with Legionella effector
FT RavZ."
FT /evidence="ECO:0000269|PubMed:28668392"
FT MUTAGEN 27
FT /note="H->Y: Increased interaction with WDFY3/ALFY, no
FT effect on SQSTM1-binding; when associated with K-26 and D-
FT 57."
FT /evidence="ECO:0000269|PubMed:24668264"
FT MUTAGEN 35
FT /note="I->A: Decreases C18 ceramide binding."
FT /evidence="ECO:0000269|PubMed:22922758"
FT MUTAGEN 52..53
FT /note="FL->AA: No effect on interaction with TECPR2."
FT /evidence="ECO:0000269|PubMed:20562859"
FT MUTAGEN 52
FT /note="F->A: Decreases C18 ceramide binding."
FT /evidence="ECO:0000269|PubMed:22922758"
FT MUTAGEN 57
FT /note="H->D: Increased interaction with WDFY3/ALFY, no
FT effect on SQSTM1-binding; when associated with K-26 and Y-
FT 27."
FT /evidence="ECO:0000269|PubMed:24668264"
FT MUTAGEN 68
FT /note="R->A: Impairs cleavage by ATG4B."
FT /evidence="ECO:0000269|PubMed:23721406"
FT MUTAGEN 70
FT /note="R->A: Abolishes interaction with TECPR2."
FT /evidence="ECO:0000269|PubMed:20562859"
FT MUTAGEN 80..82
FT /note="FLL->ALA: Impaired localization to autophagosomes."
FT /evidence="ECO:0000269|PubMed:31315929"
FT MUTAGEN 116
FT /note="Q->P: Abolished delipidation by ATG4 family
FT proteins."
FT /evidence="ECO:0000269|PubMed:31315929"
FT MUTAGEN 119
FT /note="F->A: Impaired localization to autophagosomes."
FT /evidence="ECO:0000269|PubMed:31315929"
FT MUTAGEN 120
FT /note="G->A: No processing of precursor. No lipidation.
FT Decreases C18 ceramide binding."
FT /evidence="ECO:0000269|PubMed:15355958,
FT ECO:0000269|PubMed:22922758"
FT MUTAGEN 122
FT /note="K->A: No effect on processing of precursor."
FT /evidence="ECO:0000269|PubMed:15355958"
FT CONFLICT 61
FT /note="S -> G (in Ref. 5; AAH67797)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:3X0W"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:6LAN"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:6LAN"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:6LAN"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3VTW"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:6LAN"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:6LAN"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5DCN"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6LAN"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:6LAN"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:3VTU"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5MS5"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:6LAN"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5W9A"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:6LAN"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:6LAN"
SQ SEQUENCE 125 AA; 14688 MW; BB141DEC7653E83F CRC64;
MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVYASQETFG
MKLSV
