Autophagy protein Atg8 ubiquitin like; Light chain 3 is proposed to function primarily as a subunit of microtubule associated proteins 1A and 1B and that its expression may regulate microtubule binding activity. Autophagy is generally known as a process involved in the degradation of bulk cytoplasmic components that are non-specifically sequestered into an autophagosome, where they are sequestered into double-membrane vesicles and delivered to the degradative organelle, the lysosome/vacuole, for breakdown and eventual recycling of the resulting macromolecules. The yeast proteins are involved in the autophagosome, and Atg8 binds Atg19, via its N-terminus and the C-terminus of Atg19.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701362    16 RCKEVQQIRDQHPSKIPVIIERYKGEKqLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQhSMVSVSTPI 95
Cdd:pfam02991   2 RQKESEKIREKYPDRIPVIIEKASGSD-LPDIDKKKYLVPADLTVGQFIYIIRKRIQLRPEKAIFLFVNN-TLPPTSATM 79

                          90       100
                  ....*....|....*....|....*
gi 85701362    96 ADIYEQEKDEDGFLYMVYASQETFG 120
Cdd:pfam02991  80 SALYEEEKDEDGFLYMVYSGENTFG 104

ubiquitin-like (Ubl) domain found in microtubule associate protein 1 light chain 3 (MAP1LC3); Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. MAP1LC3 (also known as LC3) has a ubiquitin-like (Ubl) fold and belongs to the ATG8 autophagy protein family. A Ubl conjugation of MAP1LC3 by the phospholipid phosphatidylethanolamine (PE) is an essential process for the formation of autophagosomes. MAP1LC3 is cleaved by the cysteine protease ATG4 and is then conjugated with PE by E1-like enzyme ATG7 and ATG3, an E2-like enzyme. The Ubl conversion of MAP1LC3 is known as a marker of autophagy-induction. This sub-family includes MAP1LC3A, MAP1LC3B, and MAP1LC3C, each encoded by a different MAP1LC3 gene.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701362  15 DRCKEVQQIRDQHPSKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQHSMVSVSTP 94
Cdd:cd16129   1 QRKKDVEEIREKHPNKIPVIIERYKGEKQLPLLDKTKFLVPDHVTMSELVKIIRRRLQLNPTQAFFLLVNQRSMVSVSTP 80

                        90       100
                ....*....|....*....|....*
gi 85701362  95 IADIYEQEKDEDGFLYMVYASQETF 119
Cdd:cd16129  81 MSEVYRREKDEDGFLYMVYASQETF 105

ubiquitin-like (Ubl) domain found in microtubule associate protein 1 light chain 3C (MAPLC3C); Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. MAP1LC3C belongs to the MAP1LC3 (short name LC3) family proteins. MAP1LC3 has a ubiquitin-like (Ubl) fold that belongs to the autophagy-related 8 (ATG8) protein family. A Ubl conjugation of MAP1LC3 by the phospholipid phosphatidylethanolamine (PE) is an essential process for the formation of autophagosomes. MAP1LC3 is cleaved by cysteine protease ATG4 and then conjugated with PE by E1-like enzyme ATG7 and ATG3, a E2-like enzyme. The Ubl conversion of MAP1LC3 is known as a marker of autophagy-induction. ATG8 proteins are ubiquitously expressed, although some subfamily members are expressed at increased levels in certain tissues, e.g. MAP1LC3C is transcribed at lower levels than other members of MAP1LC3 subfamily and expressed predominantly in the lung.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701362   7 FKQRRSFADRCKEVQQIRDQHPSKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQH 86
Cdd:cd17236   1 FKQRKSLASRKEEVAGIRAKFPNKIPVIVERYYKEKNLPILDKTKFLVPQELTMSQFVTIIRNRMSLTATQAFYLLVNNK 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 85701362  87 SMVSVSTPIADIYEQEKDEDGFLYMVYASQETF 119
Cdd:cd17236  81 SLASMSTTMAEVYRDEKDEDGFLYMTYASQEMF 113

ubiquitin-like (Ubl) domain found in autophagy-related ubiquitin-like protein; Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. The autophagy-related ubiquitin-like proteins, such as Saccharomyces cerevisiae Atg8p, undergo a unique ubiquitin-like (Ubl) conjugation, a process essential for autophagosome formation. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. ATG8 family proteins undergo multistep modifications by the E1-like (ubiquitin activating) enzyme ATG7, and the E2-like (ubiquitin conjugating) enzyme ATG3. The mammalian ATG8 family is classified into three subfamilies: i) MAP1LC3 (microtubule associated protein 1 light chain 3) which includes MAP1LC3A, MAP1LC3B, MAP1LC3B2, and MAP1LC3C, ii) GABARAP (GABA type A receptor associated protein) which includes GABARAP, GABARAPL1, and GABARAPL3, and iii) GABARAPL2 (GABA type A receptor associated protein like 2), also known as GATE-16 (golgi-associated adenosine triphosphatase enhancer of 16 kDa).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701362  30 KIPVIIERYKGEKqLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQHSMVSvSTPIADIYEQEKDEDGFL 109
Cdd:cd01611   1 KIPVILEKAGKTK-IPILDKKKYLVPRDLTVGQLIDFIRKRLKLVAEEALFIFVNQFAPPT-SAEMGTLYEEHGDEDGFL 78

                ....*.
gi 85701362 110 YMVYAS 115
Cdd:cd01611  79 YLHYSK 84

ubiquitin-like (Ubl) domain found in GABA type A receptor associated protein like 2 (GABARAPL2, also known as GATE16); Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. GABARAPL2 (GABA type A receptor associated protein like 2), also known as GATE-16 (golgi-associated adenosine triphosphatase enhancer of 16 kDa), has a ubiquitin-like (Ubl) domain and is a sub-family of the autophagy-related 8 (ATG8) protein family. GABARAPL2 participates to the autophagosome maturation, and seems to be involved in constitutive transport under normal conditions and in autophagic processes during stress. GABARAPL2 is characterized as a membrane transport modulator that controls intra-Golgi transport by interacting with NSF and Golgi v-SNARE GOS-28.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701362   7 FKQRRSFADRCKEVQQIRDQHPSKIPVIIERYKGEkQLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQh 86
Cdd:cd17163   1 FKEEHSLEQRCAESAKIRAKYPDRIPVIVEKVPKS-QIPDIDKRKFLVPSDITVAQFMWIIRKRIQLPSEKAIFLFVGK- 78

                        90       100       110
                ....*....|....*....|....*....|....
gi 85701362  87 SMVSVSTPIADIYEQEKDEDGFLYMVYASQETFG 120
Cdd:cd17163  79 VLPQSSATMGQLYEEHKDEDGFLYVAYSGENTFG 112

ubiquitin-like (Ubl) domain found in gamma-aminobutyric acid receptor-associated protein (GABARAP) and similar proteins; sub-family of the autophagy-related 8 (ATG8) protein family; GABARAP (also termed GABA(A) receptor-associated protein, ATG8A, or MM46) has been implicated in intracellular protein trafficking. It is a cytosolic protein, localized to transport vesicles, the Golgi network and the endoplasmic reticulum. It interacts with the intracellular domain of the gamma2 subunit of GABA(A) receptors, and thus, functions as a trafficking modulator implicated in the intracellular trafficking of GABA(A) receptor. GABARAP also acts as a Ubl modifier belonging to the ATG8 (autophagy-related 8) protein family which is essential for autophagosome biogenesis and maturation. GABARAP recruits phosphatidylinositol 4-kinase II alpha (PI4KIIalpha) as a specific downstream effector, and regulates phosphatidylinositol 4-phosphate (PI4P)-dependent autophagosome lysosome fusion. This sub-family also includes GABARAPL1 (also termed GABA(A) receptor-associated protein-like, or GEC1), GABARAPL2/GATE-16, and GABARAPL3. GABARAPL1 has been involved in the intracellular transport of receptors via interactions with tubulin and GABA(A) or kappa opioid receptors. GABARAPL1 is also a Ubl modifier that functions as a mediator involved in androgen-regulated autophagy process. It is transcriptionally modulated by androgen receptor (AR) and has a repressive role in autophagy. In addition, GABARAPL1 is required for increased membrane expression of epidermal growth factor receptor (EGFR) during hypoxia, suggesting a possible role in the trafficking of these membrane proteins. GABARAPL1 may also play a key role in several important biological processes such as cancer or neurodegenerative diseases. Low expression of GABARAPL1 is associated with poor prognosis of patients with hepatocellular carcinoma.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701362   3 SDRPFKQRRSfadrckEVQQIRDQHPSKIPVIIERYKgEKQLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLL 82
Cdd:cd16127   3 EDHPFEKRRS------EGEKIRKKYPDRVPVIVEKAP-KARVADLDKKKYLVPSDLTVGQFYFLIRKRIHLRPEDALFFF 75

                        90       100       110
                ....*....|....*....|....*....|..
gi 85701362  83 VNqHSMVSVSTPIADIYEQEKDEDGFLYMVYA 114
Cdd:cd16127  76 VN-NVIPPTSATMGQLYQEHHEEDFFLYIAYS 106

ubiquitin-like (Ubl) domain found in gamma-aminobutyric acid receptor-associated protein (GABARAP); GABARAP (also termed GABA(A) receptor-associated protein, ATG8A, or MM46) has been implicated in intracellular protein trafficking. It is a cytosolic protein that is localized to transport vesicles, the Golgi network and the endoplasmic reticulum. It interacts with the intracellular domain of the gamma2 subunit of GABA(A) receptors, and thus functions as a trafficking modulator implicated in the intracellular trafficking of GABA(A) receptor. GABARAP also acts as a Ubl modifier belonging to the ATG8 (autophagy-related 8) protein family, which is essential for autophagosome biogenesis and maturation. GABARAP recruits phosphatidylinositol 4-kinase II alpha (PI4KIIalpha) as a specific downstream effector, and regulates phosphatidylinositol 4-phosphate (PI4P)-dependent autophagosome lysosome fusion.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701362   7 FKQRRSFADRCKEVQQIRDQHPSKIPVIIERYKgEKQLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNqH 86
Cdd:cd17232   4 YKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAP-KARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVN-N 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 85701362  87 SMVSVSTPIADIYEQEKDEDGFLYMVYASQETFG 120
Cdd:cd17232  82 VIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYG 115

Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. The Apg12 system is one of the ubiquitin-like protein conjugation systems conserved in eukaryotes. It was first discovered in yeast during systematic analyses of the apg mutants defective in autophagy. Covalent attachment of Apg12-Apg5 is essential for autophagy.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85701362    45 PVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQHSMVSVSTPIADIYEQEKdEDGFLYMVYASQETFG 120
Cdd:pfam04110  13 PILKKSKFKVNPSQTFASVILFLKKFLKLQASDSLFLYVNNSFAPSPDQIVGNLYECFG-TDGKLVLNYCISVAWG 87