ATG8_PICAN
ID ATG8_PICAN Reviewed; 125 AA.
AC Q5QFG1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Autophagy-related protein 8;
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8;
DE Flags: Precursor;
GN Name=ATG8;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=15569246; DOI=10.1111/j.1600-0854.2004.00252.x;
RA Monastyrska I., van der Heide M., Krikken A.M., Kiel J.A.K.W.,
RA van der Klei I.J., Veenhuis M.;
RT "Atg8 is essential for macropexophagy in Hansenula polymorpha.";
RL Traffic 6:66-74(2005).
RN [2]
RP INDUCTION.
RX PubMed=20044946; DOI=10.1186/1471-2164-11-1;
RA van Zutphen T., Baerends R.J., Susanna K.A., de Jong A., Kuipers O.P.,
RA Veenhuis M., van der Klei I.J.;
RT "Adaptation of Hansenula polymorpha to methanol: a transcriptome
RT analysis.";
RL BMC Genomics 11:1-1(2010).
CC -!- FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation.
CC With ATG4, mediates the delivery of the autophagosomes to the vacuole
CC via the microtubule cytoskeleton. Required for selective autophagic
CC degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC contributes to regulate mitochondrial quantity and quality by
CC eliminating the mitochondria to a basal level to fulfill cellular
CC energy requirements and preventing excess ROS production. Participates
CC also in membrane fusion events that take place in the early secretory
CC pathway. Also involved in endoplasmic reticulum-specific autophagic
CC process and is essential for the survival of cells subjected to severe
CC ER stress. The ATG8-PE conjugate mediates tethering between adjacent
CC membranes and stimulates membrane hemifusion, leading to expansion of
CC the autophagosomal membrane during autophagy.
CC {ECO:0000250|UniProtKB:P38182, ECO:0000269|PubMed:15569246}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:15569246}; Lipid-anchor
CC {ECO:0000269|PubMed:15569246}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P38182}.
CC -!- INDUCTION: Expression is increased after the shift of cells from
CC glucose to methanol. {ECO:0000269|PubMed:20044946}.
CC -!- PTM: The last C-terminal 9 residues are removed to expose Gly-116 at
CC the C-terminus. The C-terminal Gly is then amidated with
CC phosphatidylethanolamine by an activating system similar to that for
CC ubiquitine. {ECO:0000250|UniProtKB:P38182}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; AY619720; AAU04437.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5QFG1; -.
DR SMR; Q5QFG1; -.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR Pfam; PF02991; ATG8; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasmic vesicle; Lipoprotein; Membrane; Protein transport;
KW Transport; Ubl conjugation pathway; Vacuole.
FT CHAIN 1..116
FT /note="Autophagy-related protein 8"
FT /id="PRO_0000017230"
FT PROPEP 117..125
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P38182"
FT /id="PRO_0000017231"
FT SITE 116..117
FT /note="Cleavage; by ATG4"
FT /evidence="ECO:0000250|UniProtKB:P38182"
FT LIPID 116
FT /note="Phosphatidylethanolamine amidated glycine"
FT /evidence="ECO:0000250|UniProtKB:P38182"
SQ SEQUENCE 125 AA; 14625 MW; A8F7B7587E58EFFB CRC64;
MRSQFKDEHP FERRKAEASR IRGKFLDRIP VICEKVEESD IPEIDKRKYL VPSDLTVGQF
VYVIRKRIQL PSEKAIFIFV NDILPPTASL MSTIYEQYKD EDGFLYILYS GENTFGQLEG
VEETL