Detail Information for IndEnz0002007926
IED ID IndEnz0002007926
Enzyme Type ID protease007926
Protein Name Microtubule-associated proteins 1A/1B light chain 3C
Autophagy-related protein LC3 C
Autophagy-related ubiquitin-like modifier LC3 C
MAP1 light chain 3-like protein 3
MAP1A/MAP1B light chain 3 C
MAP1A/MAP1B LC3 C
Microtubule-associated protein 1 light chain 3 gamma
Gene Name MAP1LC3C
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MPPPQKIPSVRPFKQRKSLAIRQEEVAGIRAKFPNKIPVVVERYPRETFLPPLDKTKFLVPQELTMTQFLSIIRSRMVLRATEAFYLLVNNKSLVSMSATMAEIYRDYKDEDGFVYMTYASQETFGCLESAAPRDGSSLEDRPCNPL
Enzyme Length 147
Uniprot Accession Number Q9BXW4
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Ubiquitin-like modifier that plays a crucial role in antibacterial autophagy (xenophagy) through the selective binding of CALCOCO2 (PubMed:23022382). Recruits all ATG8 family members to infecting bacteria such as S.typhimurium (PubMed:23022382). May also play a role in aggrephagy, the macroautophagic degradation of ubiquitinated and aggregated proteins (PubMed:28404643). {ECO:0000269|PubMed:23022382, ECO:0000269|PubMed:28404643}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (8); Chain (1); Helix (4); Lipidation (2); Modified residue (2); Mutagenesis (3); Propeptide (1); Site (1); Turn (1)
Keywords 3D-structure;Autophagy;Cytoplasm;Cytoplasmic vesicle;Cytoskeleton;Lipoprotein;Membrane;Microtubule;Phosphoprotein;Reference proteome;Ubl conjugation pathway
Interact With Q9BSB4; O75143; Q676U5; Q9Y4P1; Q13137; P20807-4; Q8WXU2; Q9BQS8; Q9UKD1; O00410; Q86V97; Q8WVZ9; O43561-2; Q8IVT2; Q14596; Q8TD19; O75323; P35372-10; Q9NS23; Q8WWW0; Q8NHV9; Q6ZNE9; Q15459; Q13501; Q13188; Q86VP1; Q3MII6; Q9UPU7; O15040; Q15025; Q96A56; Q969E8; Q9GZZ9; O75385; Q8IZQ1; P17028
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:12740394, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:31709703}; Lipid-anchor {ECO:0000269|PubMed:12740394}. Endomembrane system {ECO:0000269|PubMed:12740394}; Lipid-anchor {ECO:0000269|PubMed:12740394}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12740394}. Note=LC3-II binds to the autophagic membranes. {ECO:0000269|PubMed:12740394}.
Modified Residue MOD_RES 93; /note=Phosphoserine; by TBK1; /evidence=ECO:0000269|PubMed:31709703; MOD_RES 96; /note=Phosphoserine; by TBK1; /evidence=ECO:0000269|PubMed:31709703
Post Translational Modification PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) to expose the glycine at the C-terminus and form the cytosolic form, LC3-I (PubMed:15187094, PubMed:20818167, PubMed:30661429, PubMed:31709703). The processed form is then activated by APG7L/ATG7, transferred to ATG3 and conjugated to phosphatidylethanolamine (PE) phospholipid to form the membrane-bound form, LC3-II (PubMed:15187094). During non-canonical autophagy, the processed form is conjugated to phosphatidylserine (PS) phospholipid (PubMed:33909989). ATG4 proteins also mediate the delipidation of PE-conjugated forms (PubMed:33909989, PubMed:31709703). In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (PubMed:33909989). {ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:20818167, ECO:0000269|PubMed:30661429, ECO:0000269|PubMed:31709703, ECO:0000269|PubMed:33909989}.; PTM: (Microbial infection) The Legionella effector RavZ is a deconjugating enzyme that hydrolyzes the amide bond between the C-terminal glycine residue and an adjacent aromatic residue in ATG8 proteins conjugated to phosphatidylethanolamine (PE), producing an ATG8 protein that is resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine (PubMed:23112293, PubMed:31722778). RavZ is also able to mediate delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989). {ECO:0000269|PubMed:23112293, ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33909989}.; PTM: Phosphorylation at Ser-96 and Ser-98 by TBK1 prevents interaction with ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) (PubMed:31709703). Phosphorylation by TBK1 on autophagosomes prevents their delipidation by ATG4 and premature removal from nascent autophagosomes (PubMed:31709703). {ECO:0000269|PubMed:31709703}.
Signal Peptide
Structure 3D NMR spectroscopy (1); X-ray crystallography (4)
Cross Reference PDB 2NCN; 3VVW; 3WAM; 3WAP; 5DPW;
Mapped Pubmed ID 11825910; 18321988; 19250911; 19322194; 21177865; 22170151; 24300435; 24668264; 24747438; 25568151; 26431026; 27880899; 28655748; 29149599; 31578424; 31851933; 32065021; 32532970; 33081014; 33230801; 33932238; 33988680;
Motif
Gene Encoded By
Mass 16,852
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda