Q9BXW4 · MLP3C_HUMAN
- ProteinMicrotubule-associated proteins 1A/1B light chain 3C
- GeneMAP1LC3C
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids147 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 126-127 | Cleavage; by ATG4B | ||||
Sequence: GC |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | autophagosome | |
Cellular Component | autophagosome membrane | |
Cellular Component | cytoplasmic ribonucleoprotein granule | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | cytosol | |
Cellular Component | endomembrane system | |
Cellular Component | microtubule | |
Cellular Component | organelle membrane | |
Molecular Function | phosphatidylethanolamine binding | |
Molecular Function | ubiquitin protein ligase binding | |
Biological Process | aggrephagy | |
Biological Process | autophagosome assembly | |
Biological Process | autophagosome maturation | |
Biological Process | autophagy of mitochondrion | |
Biological Process | cellular response to nitrogen starvation | |
Biological Process | cellular response to starvation | |
Biological Process | macroautophagy | |
Biological Process | protein exit from endoplasmic reticulum |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMicrotubule-associated proteins 1A/1B light chain 3C
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BXW4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, autophagosome membrane ; Lipid-anchor
Endomembrane system ; Lipid-anchor
Note: LC3-II binds to the autophagic membranes.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 93-96 | Impaired phosphorylation by TBK1. | ||||
Sequence: SLVS → ALVA | ||||||
Mutagenesis | 93-96 | Phospho-mimetic mutant; impaired interaction with ATG4 proteins, preventing cleavage at the C-terminus, conjugation to phosphatidylethanolamine and localization to autophagosomes. | ||||
Sequence: SLVS → DLVD | ||||||
Mutagenesis | 126 | No processing of precursor. | ||||
Sequence: G → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 181 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000017204 | 1-126 | Microtubule-associated proteins 1A/1B light chain 3C | |||
Sequence: MPPPQKIPSVRPFKQRKSLAIRQEEVAGIRAKFPNKIPVVVERYPRETFLPPLDKTKFLVPQELTMTQFLSIIRSRMVLRATEAFYLLVNNKSLVSMSATMAEIYRDYKDEDGFVYMTYASQETFG | ||||||
Modified residue | 93 | Phosphoserine; by TBK1 | ||||
Sequence: S | ||||||
Modified residue | 96 | Phosphoserine; by TBK1 | ||||
Sequence: S | ||||||
Lipidation | 126 | Phosphatidylethanolamine amidated glycine; alternate | ||||
Sequence: G | ||||||
Lipidation | 126 | Phosphatidylserine amidated glycine; alternate | ||||
Sequence: G | ||||||
Propeptide | PRO_0000017205 | 127-147 | Removed in mature form | |||
Sequence: CLESAAPRDGSSLEDRPCNPL |
Post-translational modification
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:31709703, PubMed:33909989).
In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (PubMed:33909989).
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:31709703, PubMed:33909989).
In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (PubMed:33909989).
(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).
RavZ is also able to mediate delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989).
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).
Phosphorylation by TBK1 on autophagosomes prevents their delipidation by ATG4 and premature removal from nascent autophagosomes (PubMed:31709703).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins (By similarity).
Interacts with TP53INP1 and TP53INP2 (PubMed:22470510).
Interacts with CALCOCO2 (PubMed:23022382).
Interacts with TECPR2 (PubMed:20562859).
Interacts with TBC1D5 (PubMed:22354992).
Found in a complex with UBQLN1 and UBQLN2 (PubMed:20529957).
Interacts with UBQLN4 (via STI1 1 and 2 domains) (PubMed:23459205).
Interacts with UBQLN1 in the presence of UBQLN4 (PubMed:23459205).
Interacts with TRIM5 (PubMed:25127057).
Interacts with ATG13 (PubMed:24290141).
Interacts with MEFV and TRIM21 (PubMed:26347139).
Interacts with WDR81; recruits MAP1LC3C to ubiquitinated protein aggregates in the aggrephagy process (PubMed:28404643).
Interacts with MOAP1 (via LIR motif) (PubMed:33783314).
Interacts with reticulophagy regulators RETREG1, RETREG2 and RETREG3 (PubMed:34338405).
Interacts with TAX1BP1 (PubMed:26451915).
Interacts with IRGM (PubMed:29420192).
Interacts with SPART (PubMed:37443287).
Interacts with TP53INP1 and TP53INP2 (PubMed:22470510).
Interacts with CALCOCO2 (PubMed:23022382).
Interacts with TECPR2 (PubMed:20562859).
Interacts with TBC1D5 (PubMed:22354992).
Found in a complex with UBQLN1 and UBQLN2 (PubMed:20529957).
Interacts with UBQLN4 (via STI1 1 and 2 domains) (PubMed:23459205).
Interacts with UBQLN1 in the presence of UBQLN4 (PubMed:23459205).
Interacts with TRIM5 (PubMed:25127057).
Interacts with ATG13 (PubMed:24290141).
Interacts with MEFV and TRIM21 (PubMed:26347139).
Interacts with WDR81; recruits MAP1LC3C to ubiquitinated protein aggregates in the aggrephagy process (PubMed:28404643).
Interacts with MOAP1 (via LIR motif) (PubMed:33783314).
Interacts with reticulophagy regulators RETREG1, RETREG2 and RETREG3 (PubMed:34338405).
Interacts with TAX1BP1 (PubMed:26451915).
Interacts with IRGM (PubMed:29420192).
Interacts with SPART (PubMed:37443287).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length147
- Mass (Da)16,852
- Last updated2001-06-01 v1
- ChecksumD3DFA8EE5985C3AA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF276659 EMBL· GenBank· DDBJ | AAK35152.1 EMBL· GenBank· DDBJ | mRNA | ||
BX571673 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC127722 EMBL· GenBank· DDBJ | AAI27723.1 EMBL· GenBank· DDBJ | mRNA | ||
BC132986 EMBL· GenBank· DDBJ | AAI32987.1 EMBL· GenBank· DDBJ | mRNA | ||
BC132988 EMBL· GenBank· DDBJ | AAI32989.1 EMBL· GenBank· DDBJ | mRNA |