MAP1LC3C
entrez
440738
canonical
uniprot
Q9BXW4
canonical
ensembl
ENSG00000197769
resolver
ensp
ENSP00000349785
resolver
ensp
ENSP00000613129
resolver
enst
ENST00000357246
resolver
enst
ENST00000943070
resolver
genesymbol
MAP1LC3C
resolver
hgnc
HGNC:13353
resolver
uniprot
A0PJY8
resolver
uniprot
A2RUP0
resolver
uniprot_entry
MLP3C_HUMAN
resolver
uniprot_sec
A0PJY8
resolver
uniprot_sec
A2RUP0
resolver
amino_acid_sequence
MPPPQKIPSVRPFKQRKSLAIRQEEVAGIRAKFPNKIPVVVERYPRETFLPPLDKTKFLVPQELTMTQFLSIIRSRMVLRATEAFYLLVNNKSLVSMSATMAEIYRDYKDEDGFVYMTYASQETFGCLESAAPRDGSSLEDRPCNPL
uniprot
proteins
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}.
uniprot
proteins
mass_dalton
16852
uniprot
proteins
mutagenesis
MUTAGEN 93..96; /note="SLVS->ALVA: Impaired phosphorylation by TBK1."; /evidence="ECO:0000269|PubMed:31709703"; MUTAGEN 93..96; /note="SLVS->DLVD: Phospho-mimetic mutant; impaired interaction with ATG4 proteins, preventing cleavage at the C-terminus, conjugation to phosphatidylethanolamine and localization to autophagosomes."; /evidence="ECO:0000269|PubMed:31709703"; MUTAGEN 126; /note="G->A: No processing of precursor."; /evidence="ECO:0000269|PubMed:12740394
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: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). {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}.
uniprot
proteins
protein_family
ATG8 family
uniprot
proteins
pubmed
12740394
uniprot
proteins
pubmed
15187094
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
20529957
uniprot
proteins
pubmed
20562859
uniprot
proteins
pubmed
20818167
uniprot
proteins
pubmed
22354992
uniprot
proteins
pubmed
22470510
uniprot
proteins
pubmed
23022382
uniprot
proteins
pubmed
23112293
uniprot
proteins
pubmed
23459205
uniprot
proteins
pubmed
24290141
uniprot
proteins
pubmed
25127057
uniprot
proteins
pubmed
26347139
uniprot
proteins
pubmed
26451915
uniprot
proteins
pubmed
28404643
uniprot
proteins
pubmed
29420192
uniprot
proteins
pubmed
30661429
uniprot
proteins
pubmed
31709703
uniprot
proteins
pubmed
31722778
uniprot
proteins
pubmed
33783314
uniprot
proteins
pubmed
33909989
uniprot
proteins
pubmed
34338405
uniprot
proteins
pubmed
37443287
uniprot
proteins
pubmed
39284914
uniprot
proteins
sequence_length
147
uniprot
proteins
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}.
uniprot
proteins