Map1lc3b
entrez
64862
canonical
uniprot
Q62625
canonical
ensembl
ENSRNOG00000017905
resolver
ensembl
ENSRNOG00055020808
resolver
ensembl
ENSRNOG00065001119
resolver
ensp
ENSRNOP00000112440
resolver
genesymbol
Map1lc3b
resolver
genesymbol_syn
Map1alc3
resolver
genesymbol_syn
Map1lc3
resolver
uniprot
Q6XVN7
resolver
uniprot_entry
MLP3B_RAT
resolver
uniprot_sec
Q6XVN7
resolver
amino_acid_sequence
MPSEKTFKQRRSFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYESERDEDGFLYMVYASQETFGTALAVTYMSALKATATGREPCL
uniprot
proteins
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. {ECO:0000250|UniProtKB:Q9GZQ8}.
uniprot
proteins
mass_dalton
16394
uniprot
proteins
mutagenesis
MUTAGEN 116; /note="Q->A: No processing of precursor."; /evidence="ECO:0000269|PubMed:16183633"; MUTAGEN 119; /note="F->A: No processing of precursor."; /evidence="ECO:0000269|PubMed:16183633"; MUTAGEN 120; /note="G->A: No processing of precursor."; /evidence="ECO:0000269|PubMed:11060023, ECO:0000269|PubMed:16183633
uniprot
proteins
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:11060023, PubMed:16183633, PubMed:16874114). 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. During non-canonical autophagy, the processed form is conjugated to phosphatidylserine (PS) phospholipid. ATG4 proteins also mediate the delipidation of PE-conjugated forms. In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy. ATG4B constitutes the major protein for proteolytic activation (By similarity). ATG4D is the main enzyme for delipidation activity (By similarity). {ECO:0000250|UniProtKB:Q9CQV6, ECO:0000250|UniProtKB:Q9GZQ8, ECO:0000269|PubMed:11060023, ECO:0000269|PubMed:16183633, ECO:0000269|PubMed:16874114}.; PTM: Phosphorylation by PKA inhibits conjugation of phosphatidylethanolamine (PE). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity. {ECO:0000250|UniProtKB:Q9GZQ8}.; PTM: Ubiquitinated by BIRC6; this activity is inhibited by DIABLO/SMAC. {ECO:0000250|UniProtKB:Q9GZQ8}.
uniprot
proteins
protein_family
ATG8 family
uniprot
proteins
pubmed
11060023
uniprot
proteins
pubmed
15095872
uniprot
proteins
pubmed
15265004
uniprot
proteins
pubmed
15325588
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16183633
uniprot
proteins
pubmed
16874114
uniprot
proteins
pubmed
19322194
uniprot
proteins
pubmed
23399561
uniprot
proteins
pubmed
7908909
uniprot
proteins
sequence_length
142
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:11060023}; Lipid-anchor {ECO:0000269|PubMed:11060023}. Endomembrane system {ECO:0000269|PubMed:11060023}; Lipid-anchor {ECO:0000269|PubMed:11060023}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9GZQ8}; Lipid-anchor {ECO:0000250|UniProtKB:Q9GZQ8}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11060023}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9GZQ8}. Note=LC3-II binds to the autophagic membranes. LC3-II localizes with the mitochondrial inner membrane during Parkin-mediated mitophagy (By similarity). Also localizes to discrete punctae along the ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:Q9GZQ8}.
uniprot
proteins