MAP1LC3B
entrez
81631
canonical
uniprot
Q9GZQ8
canonical
ensembl
ENSG00000140941
resolver
ensp
ENSP00000268607
resolver
ensp
ENSP00000498476
resolver
enst
ENST00000268607
resolver
enst
ENST00000650688
resolver
genesymbol
DKFZp762B153
resolver
genesymbol
MAP1LC3B
resolver
genesymbol_syn
MAP1ALC3
resolver
genesymbol_syn
MAP1LC3B
resolver
hgnc
HGNC:13352
resolver
uniprot
Q658J6
resolver
uniprot
Q6NW02
resolver
uniprot_entry
MLP3B_HUMAN
resolver
uniprot_entry
Q658J6_HUMAN
resolver
uniprot_sec
Q6NW02
resolver
amino_acid_sequence
MPSEKTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYESEKDEDGFLYMVYASQETFGMKLSV
uniprot
proteins
function
FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes) (PubMed:20418806, PubMed:23209295, PubMed:28017329). 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 (PubMed:23209295, PubMed:28017329). In response to cellular stress and upon mitochondria fission, binds C-18 ceramides and anchors autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria (PubMed:22922758). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20418806, PubMed:23209295, PubMed:28017329). Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway (PubMed:24089205). 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 (PubMed:31006537, PubMed:31006538). Upon nutrient stress, directly recruits cofactor JMY to the phagophore membrane surfaces and promotes JMY's actin nucleation activity and autophagosome biogenesis during autophagy (PubMed:30420355). {ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:22922758, ECO:0000269|PubMed:23209295, ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:30420355, ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}.
uniprot
proteins
mass_dalton
14688
uniprot
proteins
mutagenesis
MUTAGEN 26; /note="Q->K: Increased interaction with WDFY3/ALFY, no effect on SQSTM1-binding; when associated with Y-27 and D-57."; /evidence="ECO:0000269|PubMed:24668264"; MUTAGEN 27; /note="H->A: Decreased interaction with Legionella effector RavZ."; /evidence="ECO:0000269|PubMed:28668392"; MUTAGEN 27; /note="H->Y: Increased interaction with WDFY3/ALFY, no effect on SQSTM1-binding; when associated with K-26 and D-57."; /evidence="ECO:0000269|PubMed:24668264"; MUTAGEN 35; /note="I->A: Decreases C18 ceramide binding."; /evidence="ECO:0000269|PubMed:22922758"; MUTAGEN 52..53; /note="FL->AA: No effect on interaction with TECPR2."; /evidence="ECO:0000269|PubMed:20562859"; MUTAGEN 52; /note="F->A: Decreases C18 ceramide binding."; /evidence="ECO:0000269|PubMed:22922758"; MUTAGEN 57; /note="H->D: Increased interaction with WDFY3/ALFY, no effect on SQSTM1-binding; when associated with K-26 and Y-27."; /evidence="ECO:0000269|PubMed:24668264"; MUTAGEN 68; /note="R->A: Impairs cleavage by ATG4B."; /evidence="ECO:0000269|PubMed:23721406"; MUTAGEN 70; /note="R->A: Abolishes interaction with TECPR2."; /evidence="ECO:0000269|PubMed:20562859"; MUTAGEN 80..82; /note="FLL->ALA: Impaired localization to autophagosomes."; /evidence="ECO:0000269|PubMed:31315929"; MUTAGEN 116; /note="Q->P: Abolished delipidation by ATG4 family proteins."; /evidence="ECO:0000269|PubMed:31315929"; MUTAGEN 119; /note="F->A: Impaired localization to autophagosomes."; /evidence="ECO:0000269|PubMed:31315929"; MUTAGEN 120; /note="G->A: No processing of precursor. No lipidation. Decreases C18 ceramide binding."; /evidence="ECO:0000269|PubMed:15355958, ECO:0000269|PubMed:22922758"; MUTAGEN 122; /note="K->A: No effect on processing of precursor."; /evidence="ECO:0000269|PubMed:15355958
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:15187094, PubMed:15355958, PubMed:20818167, PubMed:29458288, PubMed:30661429, PubMed:31315929). 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:29458288, PubMed:33909989). In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (PubMed:33909989). ATG4B constitutes the major protein for proteolytic activation (PubMed:30661429). ATG4D is the main enzyme for delipidation activity (By similarity). {ECO:0000250|UniProtKB:Q9CQV6, ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:15355958, ECO:0000269|PubMed:20818167, ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:30661429, ECO:0000269|PubMed:31315929, 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:28395732, 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:28395732, ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33909989}.; PTM: Phosphorylation by PKA inhibits conjugation of phosphatidylethanolamine (PE) (PubMed:22948227). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity (PubMed:22948227). {ECO:0000269|PubMed:22948227}.; PTM: Ubiquitinated by BIRC6; this activity is inhibited by DIABLO/SMAC. {ECO:0000269|PubMed:36758105}.
uniprot
proteins
protein_family
ATG8 family
uniprot
proteins
pubmed
12740394
uniprot
proteins
pubmed
12932674
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14713272
uniprot
proteins
pubmed
15095872
uniprot
proteins
pubmed
15187094
uniprot
proteins
pubmed
15325588
uniprot
proteins
pubmed
15355958
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15857831
uniprot
proteins
pubmed
17580304
uniprot
proteins
pubmed
18524774
uniprot
proteins
pubmed
20100911
uniprot
proteins
pubmed
20418806
uniprot
proteins
pubmed
20529957
uniprot
proteins
pubmed
20562859
uniprot
proteins
pubmed
20818167
uniprot
proteins
pubmed
21383079
uniprot
proteins
pubmed
22311637
uniprot
proteins
pubmed
22354992
uniprot
proteins
pubmed
22470510
uniprot
proteins
pubmed
22922758
uniprot
proteins
pubmed
22948227
uniprot
proteins
pubmed
23112293
uniprot
proteins
pubmed
23209295
uniprot
proteins
pubmed
23459205
uniprot
proteins
pubmed
23721406
uniprot
proteins
pubmed
24089205
uniprot
proteins
pubmed
24290141
uniprot
proteins
pubmed
24668264
uniprot
proteins
pubmed
25215947
uniprot
proteins
pubmed
25684205
uniprot
proteins
pubmed
26040720
uniprot
proteins
pubmed
26451915
uniprot
proteins
pubmed
28017329
uniprot
proteins
pubmed
28395732
uniprot
proteins
pubmed
28668392
uniprot
proteins
pubmed
29420192
uniprot
proteins
pubmed
29458288
uniprot
proteins
pubmed
30143514
uniprot
proteins
pubmed
30420355
uniprot
proteins
pubmed
30661429
uniprot
proteins
pubmed
31006537
uniprot
proteins
pubmed
31006538
uniprot
proteins
pubmed
31091447
uniprot
proteins
pubmed
31315929
uniprot
proteins
pubmed
31722778
uniprot
proteins
pubmed
32315611
uniprot
proteins
pubmed
33499712
uniprot
proteins
pubmed
33783314
uniprot
proteins
pubmed
33909989
uniprot
proteins
pubmed
34338405
uniprot
proteins
pubmed
36758105
uniprot
proteins
pubmed
39284914
uniprot
proteins
pubmed
39481378
uniprot
proteins
sequence_length
125
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:22311637, ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:31315929, ECO:0000269|PubMed:33499712}; Lipid-anchor {ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:29458288}. Endomembrane system {ECO:0000269|PubMed:12740394}; Lipid-anchor {ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:29458288}. Mitochondrion membrane {ECO:0000269|PubMed:25215947, ECO:0000269|PubMed:28017329}; Lipid-anchor {ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:29458288}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9CQV6}. Cytoplasmic vesicle {ECO:0000269|PubMed:30420355}. Note=LC3-II binds to the autophagic membranes. LC3-II localizes with the mitochondrial inner membrane during Parkin-mediated mitophagy (PubMed:28017329). Also localizes to discrete punctae along the ciliary axoneme. {ECO:0000269|PubMed:28017329}.
uniprot
proteins