| IED ID | IndEnz0002009600 |
| Enzyme Type ID | protease009600 |
| Protein Name |
Microtubule-associated proteins 1A/1B light chain 3A Autophagy-related protein LC3 A Autophagy-related ubiquitin-like modifier LC3 A MAP1 light chain 3-like protein 1 MAP1A/MAP1B light chain 3 A MAP1A/MAP1B LC3 A Microtubule-associated protein 1 light chain 3 alpha |
| Gene Name | MAP1LC3A |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MPSDRPFKQRRSFADRCKEVQQIRDQHPSKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQHSMVSVSTPIADIYEQEKDEDGFLYMVYASQETFGF |
| Enzyme Length | 121 |
| Uniprot Accession Number | Q9H492 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme 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:31006538, PubMed:31006537). {ECO:0000269|PubMed:20713600, ECO:0000269|PubMed:24290141, ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (6); Chain (1); Helix (5); Lipidation (2); Modified residue (1); Mutagenesis (12); Propeptide (1); Region (1); Site (1); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Autophagy;Cytoplasm;Cytoplasmic vesicle;Cytoskeleton;Lipoprotein;Membrane;Microtubule;Phosphoprotein;Reference proteome;Ubl conjugation pathway |
| Interact With | Q9Y4P1; Q8IVP5; Q8WZA9; Q9BQD3; Q14596; P35372-10; Q86VR2; Q13501; Q15025; Q9H0E2; Q9NRR5; Q9Y2B5; Q9Z2F7; O75143; Q9H6L5-1 |
| Induction | |
| 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}. |
| Modified Residue | MOD_RES 12; /note=Phosphoserine; by PKA; /evidence=ECO:0000269|PubMed:20713600 |
| 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:32686895, 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:32686895, ECO:0000269|PubMed:33909989}.; PTM: Phosphorylation at Ser-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE). {ECO:0000269|PubMed:20713600}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 3ECI; 3WAL; 3WAN; 4ZDV; 5CX3; 5DPR; 6TBE; |
| Mapped Pubmed ID | 15213446; 15383276; 15857831; 16169070; 16303767; 17102583; 17438365; 17804493; 18321988; 18653543; 18688877; 18695874; 19250911; 19322194; 19427866; 19623642; 19696020; 19812190; 20004946; 20010802; 20023420; 20061800; 20352102; 20382705; 20398630; 20479004; 20505359; 20562859; 20639871; 20712405; 21045561; 21048031; 21177865; 21316776; 21412173; 21415575; 21497758; 21507968; 21537144; 21556768; 21628531; 21674156; 21684337; 21709020; 21729531; 21812771; 21845828; 21943220; 21988832; 22011618; 22170151; 22237724; 22249245; 22267086; 22281431; 22286270; 22328508; 22505714; 22648564; 22728060; 22959883; 22974335; 23089287; 23209295; 23219390; 23333394; 23345115; 23376921; 23449484; 23602568; 23624503; 23632916; 23681079; 23752596; 23787295; 23956998; 24023838; 24070620; 24186908; 24282606; 24404161; 24528869; 24532538; 24690104; 24747438; 24806912; 24886140; 24899049; 25005847; 25042851; 25046114; 25132643; 25136588; 25311841; 25416956; 25419843; 25466963; 25483962; 25484071; 25498145; 25503391; 25544559; 25568151; 25601754; 25609649; 25661375; 25824726; 25871810; 25955014; 25996575; 26015503; 26090585; 26097572; 26150155; 26237084; 26350055; 26395023; 26452236; 26468287; 26563373; 26676801; 26722036; 26984766; 27021405; 27246247; 27250032; 27256984; 27328773; 27338037; 27442348; 27444698; 27540684; 27748808; 28069524; 28085066; 28214334; 28296541; 28320742; 28348069; 28381481; 28395732; 28655748; 28740232; 28755428; 28760651; 28800922; 28808307; 28929922; 29022195; 29022200; 29317426; 29416008; 29545906; 29752949; 29844234; 29945702; 30109811; 30349077; 30375512; 30420355; 30429217; 30504397; 30633346; 30729279; 30767704; 30797498; 30811270; 30842153; 30982432; 31029766; 31094090; 31114135; 31226352; 31315929; 31476975; 31597778; 31727942; 31932738; 32073448; 32160093; 32434445; 32437499; 32802187; 33081014; 33095129; 33172148; 33226137; 33362215; 33438275; 33526872; 33769048; 33921398; 34816823; 34943907; |
| Motif | |
| Gene Encoded By | |
| Mass | 14,272 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |