MAP1LC3A
entrez
84557
canonical
uniprot
Q9H492
canonical
ensembl
ENSG00000101460
resolver
ensp
ENSP00000353886
resolver
ensp
ENSP00000363970
resolver
ensp
ENSP00000380821
resolver
ensp
ENSP00000611422
resolver
genesymbol
MAP1LC3A
resolver
hgnc
HGNC:6838
resolver
uniprot
E1P5P4
resolver
uniprot
E1P5P5
resolver
uniprot
Q9BXW5
resolver
uniprot_entry
MLP3A_HUMAN
resolver
uniprot_sec
E1P5P4
resolver
uniprot_sec
E1P5P5
resolver
uniprot_sec
Q9BXW5
resolver
amino_acid_sequence
MPSDRPFKQRRSFADRCKEVQQIRDQHPSKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQHSMVSVSTPIADIYEQEKDEDGFLYMVYASQETFGF
uniprot
proteins
function
FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes) (PubMed:20713600, PubMed:24290141). 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:20713600). 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). {ECO:0000269|PubMed:20713600, ECO:0000269|PubMed:24290141, ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}.
uniprot
proteins
mass_dalton
14272
uniprot
proteins
mutagenesis
MUTAGEN 27; /note="H->Y: Enhances binding to RETREG1."; /evidence="ECO:0000269|PubMed:34854256"; MUTAGEN 30; /note="K->R: Enhances binding to RETREG1."; /evidence="ECO:0000269|PubMed:34854256"; MUTAGEN 49; /note="K->A: Increases interaction with ATG13 and strongly reduces autophagosome formation."; /evidence="ECO:0000269|PubMed:24290141"; MUTAGEN 51; /note="K->A: Decreases interaction with ATG13 and strongly reduces autophagosome formation."; /evidence="ECO:0000269|PubMed:24290141"; MUTAGEN 53; /note="L->A: Decreases interaction with ATG13."; /evidence="ECO:0000269|PubMed:24290141"; MUTAGEN 57; /note="H->D: Enhances binding to RETREG1."; /evidence="ECO:0000269|PubMed:34854256"; MUTAGEN 65; /note="K->F: Enhances binding to RETREG1."; /evidence="ECO:0000269|PubMed:34854256"; MUTAGEN 116..119; /note="QETF->AAAA: Abolished deconjugation of phosphatidylethanolamine (PE) by both Legionella RavZ and ATG4B."; /evidence="ECO:0000269|PubMed:32686895"; MUTAGEN 116..118; /note="QET->AAA: Abolished deconjugation of phosphatidylethanolamine (PE) by both Legionella RavZ and ATG4B."; /evidence="ECO:0000269|PubMed:32686895"; MUTAGEN 116..117; /note="QE->AA: Abolished deconjugation of phosphatidylethanolamine (PE) by ATG4B, without affecting deconjugation by Legionella RavZ."; /evidence="ECO:0000269|PubMed:32686895"; MUTAGEN 116; /note="Q->A: Abolished deconjugation of phosphatidylethanolamine (PE) by ATG4B, without affecting deconjugation by Legionella RavZ."; /evidence="ECO:0000269|PubMed:32686895"; MUTAGEN 117; /note="E->A: Abolished deconjugation of phosphatidylethanolamine (PE) by Legionella RavZ, without affecting deconjugation by ATG4B."; /evidence="ECO:0000269|PubMed:32686895"; MUTAGEN 118; /note="T->A: Does not affect deconjugation of phosphatidylethanolamine (PE)."; /evidence="ECO:0000269|PubMed:32686895"; MUTAGEN 119; /note="F->A: Abolished deconjugation of phosphatidylethanolamine (PE) by both Legionella RavZ and ATG4B."; /evidence="ECO:0000269|PubMed:32686895"; MUTAGEN 120; /note="G->A: No processing of precursor."; /evidence="ECO:0000269|PubMed:12740394"; MUTAGEN 120; /note="Missing: Abolished deconjugation of phosphatidylethanolamine (PE) by both Legionella RavZ and ATG4B."; /evidence="ECO:0000269|PubMed:32686895
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:30661429). 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:32686895, 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, PubMed:33909989). ATG4D is the main enzyme for delipidation activity (By similarity). {ECO:0000250|UniProtKB:Q91VR7, ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:30661429, ECO:0000269|PubMed:32686895, 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, PubMed:32686895). 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:32686895, ECO:0000269|PubMed:33909989}.; PTM: Phosphorylation at Ser-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE). {ECO:0000269|PubMed:20713600}.
uniprot
proteins
protein_family
ATG8 family
uniprot
proteins
pubmed
11096062
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
11825910
uniprot
proteins
pubmed
12740394
uniprot
proteins
pubmed
15187094
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17580304
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19056683
uniprot
proteins
pubmed
20529957
uniprot
proteins
pubmed
20713600
uniprot
proteins
pubmed
22354992
uniprot
proteins
pubmed
22421968
uniprot
proteins
pubmed
22470510
uniprot
proteins
pubmed
23043107
uniprot
proteins
pubmed
23112293
uniprot
proteins
pubmed
23459205
uniprot
proteins
pubmed
24067654
uniprot
proteins
pubmed
24290141
uniprot
proteins
pubmed
25127057
uniprot
proteins
pubmed
26040720
uniprot
proteins
pubmed
26347139
uniprot
proteins
pubmed
29420192
uniprot
proteins
pubmed
30661429
uniprot
proteins
pubmed
31006537
uniprot
proteins
pubmed
31006538
uniprot
proteins
pubmed
31722778
uniprot
proteins
pubmed
32686895
uniprot
proteins
pubmed
33783314
uniprot
proteins
pubmed
33909989
uniprot
proteins
pubmed
34338405
uniprot
proteins
pubmed
34854256
uniprot
proteins
pubmed
36992520
uniprot
proteins
pubmed
37443287
uniprot
proteins
pubmed
39284914
uniprot
proteins
sequence_length
121
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:12740394, ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:22421968, ECO:0000269|PubMed:23459205}; Lipid-anchor {ECO:0000269|PubMed:15187094}. Endomembrane system {ECO:0000269|PubMed:12740394}; Lipid-anchor {ECO:0000269|PubMed:15187094}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91VR7}. Note=LC3-II binds to the autophagic membranes. {ECO:0000269|PubMed:15187094}.
uniprot
proteins