Q9CQV6 · MLP3B_MOUSE
- ProteinMicrotubule-associated proteins 1A/1B light chain 3B
- GeneMap1lc3b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids125 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. In response to cellular stress and upon mitochondria fission, binds C-18 ceramides and anchors autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria. While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. Upon nutrient stress, directly recruits cofactor JMY to the phagophore membrane surfaces and promotes JMY's actin nucleation activity and autophagosome biogenesis during autophagy.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 120-121 | Cleavage; by ATG4B | ||||
Sequence: GT |
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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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMicrotubule-associated proteins 1A/1B light chain 3B
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9CQV6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, autophagosome membrane ; Lipid-anchor
Endomembrane system ; Lipid-anchor
Mitochondrion membrane ; Lipid-anchor
Note: LC3-II binds to the autophagic membranes. LC3-II localizes with the mitochondrial inner membrane during Parkin-mediated mitophagy (By similarity).
Localizes also to discrete punctae along the ciliary axoneme (By similarity).
Localizes also to discrete punctae along the ciliary axoneme (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000017200 | 1-120 | Microtubule-associated proteins 1A/1B light chain 3B | |||
Sequence: MPSEKTFKQRRSFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYESERDEDGFLYMVYASQETFG | ||||||
Lipidation | 120 | Phosphatidylethanolamine amidated glycine; alternate | ||||
Sequence: G | ||||||
Lipidation | 120 | Phosphatidylserine amidated glycine; alternate | ||||
Sequence: G | ||||||
Propeptide | PRO_0000017201 | 121-125 | Removed in mature form | |||
Sequence: TAMAV |
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:12207896, PubMed:14530254).
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 (By similarity).
During non-canonical autophagy, the processed form is conjugated to phosphatidylserine (PS) phospholipid (By similarity).
ATG4 proteins also mediate the delipidation of PE-conjugated forms (PubMed:33795848).
In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (By similarity).
ATG4B constitutes the major protein for proteolytic activation (By similarity).
ATG4D is the main enzyme for delipidation activity (PubMed:33795848).
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 (By similarity).
During non-canonical autophagy, the processed form is conjugated to phosphatidylserine (PS) phospholipid (By similarity).
ATG4 proteins also mediate the delipidation of PE-conjugated forms (PubMed:33795848).
In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (By similarity).
ATG4B constitutes the major protein for proteolytic activation (By similarity).
ATG4D is the main enzyme for delipidation activity (PubMed:33795848).
Phosphorylation by PKA inhibits conjugation of phosphatidylethanolamine (PE). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity.
Ubiquitinated by BIRC6; this activity is inhibited by DIABLO/SMAC.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins (By similarity).
Interacts at microtubules with CABP1 (via EF-hands 1 and 2) but not with calmodulin. Interacts with FYCO1 (via C-terminus). Interacts with TP53INP1 and TP53INP2 (By similarity).
Interacts with TBC1D25 (PubMed:21383079).
Directly interacts with SQSTM1; this interaction leads to MAP1LC3B recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy. Interacts with ATG4B, MAPK15 and BNIP3. Interacts with MAPB1, KEAP1, PCM1, OFD1, CEP131, and TECPR2. Interacts with TBC1D5. Found in a complex with UBQLN1 and UBQLN2. Interacts with UBQLN4 (via STI1 1 and 2 domains). Interacts with UBQLN1 in the presence of UBQLN4. Interacts with ATG13. Interacts with reticulophagy regulators RETREG1, RETREG2 and RETREG3 (PubMed:34338405).
Interacts with PLCL1; the interaction inhibits autophagosome formation (PubMed:23399561).
Interacts with TRIM16. Interacts with CRY1 and PER2 (PubMed:29937374).
Interacts with the reticulophagy receptor TEX264 (By similarity).
Membrane-bound form LC3-II interacts with PHB1 and PHB2; the interaction takes place upon Parkin-mediated mitochondrial damage (By similarity).
Interacts with PJVK; the interaction is direct (PubMed:30936319).
Interacts with KBTBD6 and KBTBD7; the interaction is direct (By similarity).
Interacts with AMBRA1 (via LIR motif) (By similarity).
Interacts with JMY; the interaction results in the activation of JYM's nucleation activity in the cytoplasm (By similarity).
Interacts with MOAP1 (via LIR motif) (By similarity).
Interacts with TAX1BP1 (By similarity).
Interacts with Irgm1 (By similarity).
Interacts with STX17 (By similarity).
Interacts (the lipidate and non-lipidated LC3 form) with DNM2; this interaction mediates recycling endosome scission leading to autophagosome release (By similarity).
Interacts at microtubules with CABP1 (via EF-hands 1 and 2) but not with calmodulin. Interacts with FYCO1 (via C-terminus). Interacts with TP53INP1 and TP53INP2 (By similarity).
Interacts with TBC1D25 (PubMed:21383079).
Directly interacts with SQSTM1; this interaction leads to MAP1LC3B recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy. Interacts with ATG4B, MAPK15 and BNIP3. Interacts with MAPB1, KEAP1, PCM1, OFD1, CEP131, and TECPR2. Interacts with TBC1D5. Found in a complex with UBQLN1 and UBQLN2. Interacts with UBQLN4 (via STI1 1 and 2 domains). Interacts with UBQLN1 in the presence of UBQLN4. Interacts with ATG13. Interacts with reticulophagy regulators RETREG1, RETREG2 and RETREG3 (PubMed:34338405).
Interacts with PLCL1; the interaction inhibits autophagosome formation (PubMed:23399561).
Interacts with TRIM16. Interacts with CRY1 and PER2 (PubMed:29937374).
Interacts with the reticulophagy receptor TEX264 (By similarity).
Membrane-bound form LC3-II interacts with PHB1 and PHB2; the interaction takes place upon Parkin-mediated mitochondrial damage (By similarity).
Interacts with PJVK; the interaction is direct (PubMed:30936319).
Interacts with KBTBD6 and KBTBD7; the interaction is direct (By similarity).
Interacts with AMBRA1 (via LIR motif) (By similarity).
Interacts with JMY; the interaction results in the activation of JYM's nucleation activity in the cytoplasm (By similarity).
Interacts with MOAP1 (via LIR motif) (By similarity).
Interacts with TAX1BP1 (By similarity).
Interacts with Irgm1 (By similarity).
Interacts with STX17 (By similarity).
Interacts (the lipidate and non-lipidated LC3 form) with DNM2; this interaction mediates recycling endosome scission leading to autophagosome release (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length125
- Mass (Da)14,617
- Last updated2007-01-23 v3
- Checksum520E29028163FA8D
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M0QWT8 | M0QWT8_MOUSE | Map1lc3b | 66 | ||
M0QWC2 | M0QWC2_MOUSE | Map1lc3b | 160 | ||
A0A1D5RLG5 | A0A1D5RLG5_MOUSE | Map1lc3b | 173 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 89 | in Ref. 2; BAB22641 | ||||
Sequence: V → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF255953 EMBL· GenBank· DDBJ | AAL83723.1 EMBL· GenBank· DDBJ | mRNA | ||
AK002795 EMBL· GenBank· DDBJ | BAB22364.1 EMBL· GenBank· DDBJ | mRNA | ||
AK003106 EMBL· GenBank· DDBJ | BAB22569.1 EMBL· GenBank· DDBJ | mRNA | ||
AK003205 EMBL· GenBank· DDBJ | BAB22641.1 EMBL· GenBank· DDBJ | mRNA | ||
AK003558 EMBL· GenBank· DDBJ | BAB22855.1 EMBL· GenBank· DDBJ | mRNA | ||
AK012604 EMBL· GenBank· DDBJ | BAB28350.1 EMBL· GenBank· DDBJ | mRNA | ||
AK132329 EMBL· GenBank· DDBJ | BAE21108.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151614 EMBL· GenBank· DDBJ | BAE30551.1 EMBL· GenBank· DDBJ | mRNA | ||
BC068180 EMBL· GenBank· DDBJ | AAH68180.1 EMBL· GenBank· DDBJ | mRNA |