UniProt functional annotation for Q9GZQ8



	UniProt functional annotation for Q9GZQ8

UniProt code: Q9GZQ8.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

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 (PubMed:28017329). 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 (PubMed:31006538, PubMed:31006537). {ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:23209295, ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}.

Subunit: 3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins (By similarity). Interacts at microtubules with CABP1 (via EF-hands 1 and 2) but not with calmodulin (PubMed:15095872). Interacts with FYCO1 (via C-terminus) (PubMed:20100911, PubMed:24089205). Interacts with TP53INP1 and TP53INP2 (PubMed:22470510). Interacts with TBC1D25 (PubMed:21383079). Directly interacts with SQSTM1; this interaction leads to MAP1LC3B recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy (PubMed:17580304, PubMed:24089205, PubMed:24668264, PubMed:18524774). Interacts with ATG4B, MAPK15 and BNIP3 (PubMed:22948227, PubMed:23209295). Interacts with MAPB1, KEAP1, PCM1, OFD1, CEP131, and TECPR2 (PubMed:20562859, PubMed:24089205). Interacts with TBC1D5 (PubMed:22354992). Found in a complex with UBQLN1 and UBQLN2 (PubMed:20529957). Interacts with UBQLN4 (via STI1 1 and 2 domains). Interacts with UBQLN1 in the presence of UBQLN4 (PubMed:23459205). Interacts with ATG13 (PubMed:24290141). Interacts with RETREG2, RETREG1 and RETREG3 (PubMed:26040720). No interaction, or very weak, with WDFY3 (PubMed:24668264). Interacts with PLCL1; the interaction inhibits autophagosome formation (By similarity). Interacts with TRIM16 (PubMed:30143514). Interacts with CRY1 and PER2 (By similarity). Interacts with the reticulophagy receptor TEX264 (PubMed:31006538, PubMed:31006537). Membrane-bound form LC3-II interacts with PHB and PHB2; the interaction takes place upon Parkin-mediated mitochondrial damage (PubMed:28017329). Interacts with PJVK; the interaction is direct (By similarity). Interacts with KBTBD6 and KBTBD7; the interaction is direct (PubMed:25684205). {ECO:0000250|UniProtKB:Q9CQV6, ECO:0000269|PubMed:15095872, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:18524774, ECO:0000269|PubMed:20100911, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:20562859, ECO:0000269|PubMed:21383079, ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:22470510, ECO:0000269|PubMed:22948227, ECO:0000269|PubMed:23209295, ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:24290141, ECO:0000269|PubMed:24668264, ECO:0000269|PubMed:25684205, ECO:0000269|PubMed:26040720, ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:30143514, ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}.

Subcellular location: Cytoplasm, cytoskeleton. Endomembrane system; Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:33499712}; Lipid-anchor. Note=LC3-II binds to the autophagic membranes. LC3-II localizes with the mitochondrial inner membrane during Parkin-mediated mitophagy (PubMed:28017329). Localizes also to discrete punctae along the ciliary axoneme. {ECO:0000269|PubMed:28017329}.

Tissue specificity: Most abundant in heart, brain, skeletal muscle and testis. Little expression observed in liver. {ECO:0000269|PubMed:12740394}.

Ptm: The precursor molecule is cleaved by ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II (PubMed:15187094). {ECO:0000269|PubMed:15187094}.

Ptm: The Legionella effector RavZ is a deconjugating enzyme that produces an ATG8 product that would be resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine.

Ptm: Phosphorylation at Thr-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE) (By similarity). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity. {ECO:0000250, ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:22948227}.

Similarity: Belongs to the ATG8 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



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 (PubMed:28017329). 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 (PubMed:31006538, PubMed:31006537). {ECO:0000269\|PubMed:20418806, ECO:0000269\|PubMed:23209295, ECO:0000269\|PubMed:24089205, ECO:0000269\|PubMed:28017329, ECO:0000269\|PubMed:31006537, ECO:0000269\|PubMed:31006538}.


Subunit:		3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins (By similarity). Interacts at microtubules with CABP1 (via EF-hands 1 and 2) but not with calmodulin (PubMed:15095872). Interacts with FYCO1 (via C-terminus) (PubMed:20100911, PubMed:24089205). Interacts with TP53INP1 and TP53INP2 (PubMed:22470510). Interacts with TBC1D25 (PubMed:21383079). Directly interacts with SQSTM1; this interaction leads to MAP1LC3B recruitment to inclusion bodies containing polyubiquitinated protein aggregates and to inclusion body degradation by autophagy (PubMed:17580304, PubMed:24089205, PubMed:24668264, PubMed:18524774). Interacts with ATG4B, MAPK15 and BNIP3 (PubMed:22948227, PubMed:23209295). Interacts with MAPB1, KEAP1, PCM1, OFD1, CEP131, and TECPR2 (PubMed:20562859, PubMed:24089205). Interacts with TBC1D5 (PubMed:22354992). Found in a complex with UBQLN1 and UBQLN2 (PubMed:20529957). Interacts with UBQLN4 (via STI1 1 and 2 domains). Interacts with UBQLN1 in the presence of UBQLN4 (PubMed:23459205). Interacts with ATG13 (PubMed:24290141). Interacts with RETREG2, RETREG1 and RETREG3 (PubMed:26040720). No interaction, or very weak, with WDFY3 (PubMed:24668264). Interacts with PLCL1; the interaction inhibits autophagosome formation (By similarity). Interacts with TRIM16 (PubMed:30143514). Interacts with CRY1 and PER2 (By similarity). Interacts with the reticulophagy receptor TEX264 (PubMed:31006538, PubMed:31006537). Membrane-bound form LC3-II interacts with PHB and PHB2; the interaction takes place upon Parkin-mediated mitochondrial damage (PubMed:28017329). Interacts with PJVK; the interaction is direct (By similarity). Interacts with KBTBD6 and KBTBD7; the interaction is direct (PubMed:25684205). {ECO:0000250\|UniProtKB:Q9CQV6, ECO:0000269\|PubMed:15095872, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:18524774, ECO:0000269\|PubMed:20100911, ECO:0000269\|PubMed:20529957, ECO:0000269\|PubMed:20562859, ECO:0000269\|PubMed:21383079, ECO:0000269\|PubMed:22354992, ECO:0000269\|PubMed:22470510, ECO:0000269\|PubMed:22948227, ECO:0000269\|PubMed:23209295, ECO:0000269\|PubMed:23459205, ECO:0000269\|PubMed:24089205, ECO:0000269\|PubMed:24290141, ECO:0000269\|PubMed:24668264, ECO:0000269\|PubMed:25684205, ECO:0000269\|PubMed:26040720, ECO:0000269\|PubMed:28017329, ECO:0000269\|PubMed:30143514, ECO:0000269\|PubMed:31006537, ECO:0000269\|PubMed:31006538}.
Subcellular location:		Cytoplasm, cytoskeleton. Endomembrane system; Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269\|PubMed:20529957, ECO:0000269\|PubMed:23459205, ECO:0000269\|PubMed:33499712}; Lipid-anchor. Note=LC3-II binds to the autophagic membranes. LC3-II localizes with the mitochondrial inner membrane during Parkin-mediated mitophagy (PubMed:28017329). Localizes also to discrete punctae along the ciliary axoneme. {ECO:0000269\|PubMed:28017329}.
Tissue specificity:		Most abundant in heart, brain, skeletal muscle and testis. Little expression observed in liver. {ECO:0000269\|PubMed:12740394}.
Ptm:		The precursor molecule is cleaved by ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II (PubMed:15187094). {ECO:0000269\|PubMed:15187094}.
Ptm:		The Legionella effector RavZ is a deconjugating enzyme that produces an ATG8 product that would be resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine.
Ptm:		Phosphorylation at Thr-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE) (By similarity). Interaction with MAPK15 reduces the inhibitory phosphorylation and increases autophagy activity. {ECO:0000250, ECO:0000269\|PubMed:15187094, ECO:0000269\|PubMed:22948227}.
Similarity:		Belongs to the ATG8 family. {ECO:0000305}.