MLP3C_HUMAN
ID MLP3C_HUMAN Reviewed; 147 AA.
AC Q9BXW4; A0PJY8; A2RUP0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Microtubule-associated proteins 1A/1B light chain 3C;
DE AltName: Full=Autophagy-related protein LC3 C;
DE AltName: Full=Autophagy-related ubiquitin-like modifier LC3 C;
DE AltName: Full=MAP1 light chain 3-like protein 3;
DE AltName: Full=MAP1A/MAP1B light chain 3 C;
DE Short=MAP1A/MAP1B LC3 C;
DE AltName: Full=Microtubule-associated protein 1 light chain 3 gamma;
DE Flags: Precursor;
GN Name=MAP1LC3C;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF GLY-126.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 LIPIDATION AT GLY-126, AND CLEAVAGE BY APG4B.
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 [5]
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 [6]
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 [7]
RP INTERACTION WITH TECPR2.
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
RP INTERACTION WITH TRIM5.
RX PubMed=25127057; DOI=10.1016/j.devcel.2014.06.013;
RA Mandell M.A., Jain A., Arko-Mensah J., Chauhan S., Kimura T., Dinkins C.,
RA Silvestri G., Munch J., Kirchhoff F., Simonsen A., Wei Y., Levine B.,
RA Johansen T., Deretic V.;
RT "TRIM proteins regulate autophagy and can target autophagic substrates by
RT direct recognition.";
RL Dev. Cell 30:394-409(2014).
RN [13]
RP INTERACTION WITH MEFV AND TRIM21.
RX PubMed=26347139; DOI=10.1083/jcb.201503023;
RA Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T.,
RA Deretic V.;
RT "TRIM-mediated precision autophagy targets cytoplasmic regulators of innate
RT immunity.";
RL J. Cell Biol. 210:973-989(2015).
RN [14]
RP FUNCTION, AND INTERACTION WITH WDR81.
RX PubMed=28404643; DOI=10.1083/jcb.201608039;
RA Liu X., Li Y., Wang X., Xing R., Liu K., Gan Q., Tang C., Gao Z., Jian Y.,
RA Luo S., Guo W., Yang C.;
RT "The BEACH-containing protein WDR81 coordinates p62 and LC3C to promote
RT aggrephagy.";
RL J. Cell Biol. 216:1301-1320(2017).
RN [15]
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 [16]
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 [17]
RP PHOSPHORYLATION AT SER-93 AND SER-96, LIPIDATION AT GLY-126, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 93-SER--SER-96.
RX PubMed=31709703; DOI=10.15252/embr.201948317;
RA Herhaus L., Bhaskara R.M., Lystad A.H., Gestal-Mato U.,
RA Covarrubias-Pinto A., Bonn F., Simonsen A., Hummer G., Dikic I.;
RT "TBK1-mediated phosphorylation of LC3C and GABARAP-L2 controls
RT autophagosome shedding by ATG4 protease.";
RL EMBO Rep. 21:e48317-e48317(2020).
RN [18]
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 [19]
RP LIPIDATION AT GLY-126.
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 [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-126 IN COMPLEX WITH CALCOCO2,
RP INTERACTION WITH CALCOCO2, AND FUNCTION.
RX PubMed=23022382; DOI=10.1016/j.molcel.2012.08.024;
RA von Muhlinen N., Akutsu M., Ravenhill B.J., Foeglein A., Bloor S.,
RA Rutherford T.J., Freund S.M., Komander D., Randow F.;
RT "LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required
RT for antibacterial autophagy.";
RL Mol. Cell 48:329-342(2012).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 8-125, 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).
CC -!- FUNCTION: Ubiquitin-like modifier that plays a crucial role in
CC antibacterial autophagy (xenophagy) through the selective binding of
CC CALCOCO2 (PubMed:23022382). Recruits all ATG8 family members to
CC infecting bacteria such as S.typhimurium (PubMed:23022382). May also
CC play a role in aggrephagy, the macroautophagic degradation of
CC ubiquitinated and aggregated proteins (PubMed:28404643).
CC {ECO:0000269|PubMed:23022382, ECO:0000269|PubMed:28404643}.
CC -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with
CC MAP1A and MAP1B proteins (By similarity). Interacts with TP53INP1 and
CC TP53INP2 (PubMed:22470510). Interacts with CALCOCO2 (PubMed:23022382).
CC Interacts with TECPR2 (PubMed:20562859). 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 (PubMed:23459205). Interacts with UBQLN1 in the presence of UBQLN4
CC (PubMed:23459205). Interacts with TRIM5 (PubMed:25127057). Interacts
CC with ATG13 (PubMed:24290141). Interacts with MEFV and TRIM21
CC (PubMed:26347139). Interacts with WDR81; recruits MAP1LC3C to
CC ubiquitinated protein aggregates in the aggrephagy process
CC (PubMed:28404643). Interacts with MOAP1 (via LIR motif)
CC (PubMed:33783314). {ECO:0000250|UniProtKB:Q62625,
CC ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:20562859,
CC ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:22470510,
CC ECO:0000269|PubMed:23022382, ECO:0000269|PubMed:23459205,
CC ECO:0000269|PubMed:24290141, ECO:0000269|PubMed:25127057,
CC ECO:0000269|PubMed:26347139, ECO:0000269|PubMed:28404643,
CC ECO:0000269|PubMed:33783314}.
CC -!- INTERACTION:
CC Q9BXW4; Q9BSB4: ATG101; NbExp=3; IntAct=EBI-2603996, EBI-2946739;
CC Q9BXW4; O75143: ATG13; NbExp=8; IntAct=EBI-2603996, EBI-2798775;
CC Q9BXW4; Q676U5: ATG16L1; NbExp=4; IntAct=EBI-2603996, EBI-535909;
CC Q9BXW4; Q9Y4P1: ATG4B; NbExp=4; IntAct=EBI-2603996, EBI-712014;
CC Q9BXW4; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-2603996, EBI-739580;
CC Q9BXW4; P20807-4: CAPN3; NbExp=3; IntAct=EBI-2603996, EBI-11532021;
CC Q9BXW4; Q8WXU2: DNAAF4; NbExp=2; IntAct=EBI-2603996, EBI-2946907;
CC Q9BXW4; Q9BQS8: FYCO1; NbExp=2; IntAct=EBI-2603996, EBI-2869338;
CC Q9BXW4; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-2603996, EBI-948296;
CC Q9BXW4; O00410: IPO5; NbExp=2; IntAct=EBI-2603996, EBI-356424;
CC Q9BXW4; Q86V97: KBTBD6; NbExp=2; IntAct=EBI-2603996, EBI-2514778;
CC Q9BXW4; Q8WVZ9: KBTBD7; NbExp=2; IntAct=EBI-2603996, EBI-473695;
CC Q9BXW4; O43561-2: LAT; NbExp=3; IntAct=EBI-2603996, EBI-8070286;
CC Q9BXW4; Q8IVT2: MISP; NbExp=3; IntAct=EBI-2603996, EBI-2555085;
CC Q9BXW4; Q14596: NBR1; NbExp=3; IntAct=EBI-2603996, EBI-742698;
CC Q9BXW4; Q8TD19: NEK9; NbExp=2; IntAct=EBI-2603996, EBI-1044009;
CC Q9BXW4; O75323: NIPSNAP2; NbExp=2; IntAct=EBI-2603996, EBI-307133;
CC Q9BXW4; P35372-10: OPRM1; NbExp=3; IntAct=EBI-2603996, EBI-12807478;
CC Q9BXW4; Q9NS23: RASSF1; NbExp=2; IntAct=EBI-2603996, EBI-367363;
CC Q9BXW4; Q8WWW0: RASSF5; NbExp=2; IntAct=EBI-2603996, EBI-367390;
CC Q9BXW4; Q8NHV9: RHOXF1; NbExp=3; IntAct=EBI-2603996, EBI-3923409;
CC Q9BXW4; Q6ZNE9: RUFY4; NbExp=3; IntAct=EBI-2603996, EBI-10181525;
CC Q9BXW4; Q15459: SF3A1; NbExp=3; IntAct=EBI-2603996, EBI-1054743;
CC Q9BXW4; Q13501: SQSTM1; NbExp=7; IntAct=EBI-2603996, EBI-307104;
CC Q9BXW4; Q13188: STK3; NbExp=2; IntAct=EBI-2603996, EBI-992580;
CC Q9BXW4; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-2603996, EBI-529518;
CC Q9BXW4; Q3MII6: TBC1D25; NbExp=3; IntAct=EBI-2603996, EBI-11899977;
CC Q9BXW4; Q9UPU7: TBC1D2B; NbExp=2; IntAct=EBI-2603996, EBI-2947180;
CC Q9BXW4; O15040: TECPR2; NbExp=2; IntAct=EBI-2603996, EBI-2946991;
CC Q9BXW4; Q15025: TNIP1; NbExp=3; IntAct=EBI-2603996, EBI-357849;
CC Q9BXW4; Q96A56: TP53INP1; NbExp=3; IntAct=EBI-2603996, EBI-9986117;
CC Q9BXW4; Q969E8: TSR2; NbExp=3; IntAct=EBI-2603996, EBI-746981;
CC Q9BXW4; Q9GZZ9: UBA5; NbExp=2; IntAct=EBI-2603996, EBI-747805;
CC Q9BXW4; O75385: ULK1; NbExp=3; IntAct=EBI-2603996, EBI-908831;
CC Q9BXW4; Q8IZQ1: WDFY3; NbExp=7; IntAct=EBI-2603996, EBI-1569256;
CC Q9BXW4; P17028: ZNF24; NbExp=3; IntAct=EBI-2603996, EBI-707773;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:12740394, ECO:0000269|PubMed:20529957,
CC ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:31709703}; Lipid-anchor
CC {ECO:0000269|PubMed:12740394}. Endomembrane system
CC {ECO:0000269|PubMed:12740394}; Lipid-anchor
CC {ECO:0000269|PubMed:12740394}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12740394}. Note=LC3-II binds to the autophagic
CC membranes. {ECO:0000269|PubMed:12740394}.
CC -!- TISSUE SPECIFICITY: Most abundant in placenta, lung and ovary.
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:20818167, PubMed:30661429,
CC PubMed:31709703). The processed form is then activated by APG7L/ATG7,
CC transferred to ATG3 and conjugated to phosphatidylethanolamine (PE)
CC phospholipid to form the membrane-bound form, LC3-II (PubMed:15187094).
CC During non-canonical autophagy, the processed form is conjugated to
CC phosphatidylserine (PS) phospholipid (PubMed:33909989). ATG4 proteins
CC also mediate the delipidation of PE-conjugated forms (PubMed:33909989,
CC PubMed:31709703). In addition, ATG4B and ATG4D mediate delipidation of
CC ATG8 proteins conjugated to PS during non-canonical autophagy
CC (PubMed:33909989). {ECO:0000269|PubMed:15187094,
CC ECO:0000269|PubMed:20818167, ECO:0000269|PubMed:30661429,
CC ECO:0000269|PubMed:31709703, 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:31722778). RavZ is also able to mediate delipidation of ATG8
CC proteins conjugated to phosphatidylserine (PS) (PubMed:33909989).
CC {ECO:0000269|PubMed:23112293, ECO:0000269|PubMed:31722778,
CC ECO:0000269|PubMed:33909989}.
CC -!- PTM: Phosphorylation at Ser-96 and Ser-98 by TBK1 prevents interaction
CC with ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) (PubMed:31709703).
CC Phosphorylation by TBK1 on autophagosomes prevents their delipidation
CC by ATG4 and premature removal from nascent autophagosomes
CC (PubMed:31709703). {ECO:0000269|PubMed:31709703}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF276659; AAK35152.1; -; mRNA.
DR EMBL; BX571673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC127722; AAI27723.1; -; mRNA.
DR EMBL; BC132986; AAI32987.1; -; mRNA.
DR EMBL; BC132988; AAI32989.1; -; mRNA.
DR CCDS; CCDS31074.1; -.
DR RefSeq; NP_001004343.1; NM_001004343.2.
DR RefSeq; XP_005273196.1; XM_005273139.3.
DR PDB; 2NCN; NMR; -; A=1-126.
DR PDB; 3VVW; X-ray; 2.50 A; B=1-126.
DR PDB; 3WAM; X-ray; 1.75 A; A=8-125.
DR PDB; 3WAP; X-ray; 3.10 A; A=8-125.
DR PDB; 5DPW; X-ray; 2.19 A; A/C/E/G/I/K/M/O=8-125.
DR PDBsum; 2NCN; -.
DR PDBsum; 3VVW; -.
DR PDBsum; 3WAM; -.
DR PDBsum; 3WAP; -.
DR PDBsum; 5DPW; -.
DR AlphaFoldDB; Q9BXW4; -.
DR SMR; Q9BXW4; -.
DR BioGRID; 136855; 61.
DR DIP; DIP-57020N; -.
DR ELM; Q9BXW4; -.
DR IntAct; Q9BXW4; 73.
DR MINT; Q9BXW4; -.
DR STRING; 9606.ENSP00000349785; -.
DR PhosphoSitePlus; Q9BXW4; -.
DR BioMuta; MAP1LC3C; -.
DR DMDM; 84028113; -.
DR PaxDb; Q9BXW4; -.
DR PeptideAtlas; Q9BXW4; -.
DR PRIDE; Q9BXW4; -.
DR Antibodypedia; 34706; 252 antibodies from 36 providers.
DR DNASU; 440738; -.
DR Ensembl; ENST00000357246.4; ENSP00000349785.3; ENSG00000197769.6.
DR GeneID; 440738; -.
DR KEGG; hsa:440738; -.
DR MANE-Select; ENST00000357246.4; ENSP00000349785.3; NM_001004343.3; NP_001004343.1.
DR UCSC; uc001hzk.3; human.
DR CTD; 440738; -.
DR DisGeNET; 440738; -.
DR GeneCards; MAP1LC3C; -.
DR HGNC; HGNC:13353; MAP1LC3C.
DR HPA; ENSG00000197769; Tissue enhanced (adipose tissue, breast).
DR MIM; 609605; gene.
DR neXtProt; NX_Q9BXW4; -.
DR OpenTargets; ENSG00000197769; -.
DR PharmGKB; PA142671482; -.
DR VEuPathDB; HostDB:ENSG00000197769; -.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000161852; -.
DR HOGENOM; CLU_119276_1_1_1; -.
DR InParanoid; Q9BXW4; -.
DR OMA; RNRMTLM; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; Q9BXW4; -.
DR TreeFam; TF312964; -.
DR PathwayCommons; Q9BXW4; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR SignaLink; Q9BXW4; -.
DR SIGNOR; Q9BXW4; -.
DR BioGRID-ORCS; 440738; 8 hits in 1072 CRISPR screens.
DR GenomeRNAi; 440738; -.
DR Pharos; Q9BXW4; Tbio.
DR PRO; PR:Q9BXW4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BXW4; protein.
DR Bgee; ENSG00000197769; Expressed in secondary oocyte and 120 other tissues.
DR Genevisible; Q9BXW4; HS.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031090; C:organelle membrane; ISS: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:0035973; P:aggrephagy; IMP:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IDA:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
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:0032527; P:protein exit from endoplasmic reticulum; IMP:CACAO.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR027731; MAP1A/MAP1B_LC3C.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR PANTHER; PTHR10969:SF50; PTHR10969:SF50; 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; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..126
FT /note="Microtubule-associated proteins 1A/1B light chain
FT 3C"
FT /id="PRO_0000017204"
FT PROPEP 127..147
FT /note="Removed in mature form"
FT /id="PRO_0000017205"
FT SITE 126..127
FT /note="Cleavage; by ATG4B"
FT /evidence="ECO:0000305|PubMed:15187094"
FT MOD_RES 93
FT /note="Phosphoserine; by TBK1"
FT /evidence="ECO:0000269|PubMed:31709703"
FT MOD_RES 96
FT /note="Phosphoserine; by TBK1"
FT /evidence="ECO:0000269|PubMed:31709703"
FT LIPID 126
FT /note="Phosphatidylethanolamine amidated glycine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:33909989,
FT ECO:0000305|PubMed:15187094"
FT LIPID 126
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000269|PubMed:33909989"
FT MUTAGEN 93..96
FT /note="SLVS->ALVA: Impaired phosphorylation by TBK1."
FT /evidence="ECO:0000269|PubMed:31709703"
FT MUTAGEN 93..96
FT /note="SLVS->DLVD: Phospho-mimetic mutant; impaired
FT interaction with ATG4 proteins, preventing cleavage at the
FT C-terminus, conjugation to phosphatidylethanolamine and
FT localization to autophagosomes."
FT /evidence="ECO:0000269|PubMed:31709703"
FT MUTAGEN 126
FT /note="G->A: No processing of precursor."
FT /evidence="ECO:0000269|PubMed:12740394"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:3WAM"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:3WAM"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:3WAM"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3WAM"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3WAM"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:3WAM"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3WAM"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3WAP"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3WAM"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3WAM"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:3WAM"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3WAP"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:3WAM"
SQ SEQUENCE 147 AA; 16852 MW; D3DFA8EE5985C3AA CRC64;
MPPPQKIPSV RPFKQRKSLA IRQEEVAGIR AKFPNKIPVV VERYPRETFL PPLDKTKFLV
PQELTMTQFL SIIRSRMVLR ATEAFYLLVN NKSLVSMSAT MAEIYRDYKD EDGFVYMTYA
SQETFGCLES AAPRDGSSLE DRPCNPL
