ATG8C_SOLTU
ID ATG8C_SOLTU Reviewed; 119 AA.
AC M1C146;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Autophagy-related protein 8C-like {ECO:0000305};
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8CL {ECO:0000305};
DE Flags: Precursor;
GN Name=ATG8CL {ECO:0000303|PubMed:26765567};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2]
RP FUNCTION, INTERACTION WITH JOKA2 AND PHYTOPHTORA INFESTANS EFFECTOR
RP PEXRD54, SUBCELLULAR LOCATION, LIPIDATION AT GLY-117, AND MUTAGENESIS OF
RP GLY-117.
RX PubMed=26765567; DOI=10.7554/elife.10856;
RA Dagdas Y.F., Belhaj K., Maqbool A., Chaparro-Garcia A., Pandey P.,
RA Petre B., Tabassum N., Cruz-Mireles N., Hughes R.K., Sklenar J., Win J.,
RA Menke F., Findlay K., Banfield M.J., Kamoun S., Bozkurt T.O.;
RT "An effector of the Irish potato famine pathogen antagonizes a host
RT autophagy cargo receptor.";
RL Elife 5:0-0(2016).
RN [3]
RP FUNCTION, INTERACTION WITH JOKA2, AND SUBCELLULAR LOCATION.
RX PubMed=29932422; DOI=10.7554/elife.37476;
RA Dagdas Y.F., Pandey P., Tumtas Y., Sanguankiattichai N., Belhaj K.,
RA Duggan C., Leary A.Y., Segretin M.E., Contreras M.P., Savage Z.,
RA Khandare V.S., Kamoun S., Bozkurt T.O.;
RT "Host autophagy machinery is diverted to the pathogen interface to mediate
RT focal defense responses against the Irish potato famine pathogen.";
RL Elife 7:0-0(2018).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 5-114 IN COMPLEX WITH A PEPTIDE
RP FROM PHYTOPHTORA INFESTAHS PATHOGEN EFFECTOR PROTEIN PEXRD54, AND
RP INTERACTION WITH PHYTOPHTORA INFESTANS EFFECTOR PEXRD54.
RX PubMed=27458016; DOI=10.1074/jbc.m116.744995;
RA Maqbool A., Hughes R.K., Dagdas Y.F., Tregidgo N., Zess E., Belhaj K.,
RA Round A., Bozkurt T.O., Kamoun S., Banfield M.J.;
RT "Structural basis of host autophagy-related protein 8 (ATG8) binding by the
RT Irish potato famine pathogen effector protein PexRD54.";
RL J. Biol. Chem. 291:20270-20282(2016).
CC -!- FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation
CC (Probable). May mediate the delivery of the autophagosomes to the
CC vacuole via the microtubule cytoskeleton (Probable). ATG8CL-mediated
CC selective autophagy contributes to defense against the fungal pathogen
CC Phytophtora infestans (PubMed:26765567, PubMed:29932422).
CC {ECO:0000269|PubMed:26765567, ECO:0000269|PubMed:29932422,
CC ECO:0000305|PubMed:26765567, ECO:0000305|PubMed:29932422}.
CC -!- SUBUNIT: Interacts with ATG4 (By similarity). Interacts with the
CC Phytophtora infestans effector PexRD54 (PubMed:26765567,
CC PubMed:27458016). Interacts with JOKA2 (PubMed:26765567,
CC PubMed:29932422). {ECO:0000250|UniProtKB:Q2XPP5,
CC ECO:0000269|PubMed:26765567, ECO:0000269|PubMed:27458016,
CC ECO:0000269|PubMed:29932422}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:26765567, ECO:0000269|PubMed:29932422}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P38182}. Vacuole membrane
CC {ECO:0000269|PubMed:29932422}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P38182}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8LEM4}.
CC -!- PTM: The C-terminal 2 residues are removed by ATG4 to expose Gly-117 at
CC the C-terminus (By similarity). The C-terminal Gly is then amidated
CC with phosphatidylethanolamine by an activating system similar to that
CC for ubiquitin (Probable). The phosphatidylethanolamine amidated glycine
CC is required for autophagosome formation (PubMed:26765567).
CC {ECO:0000250|UniProtKB:P38182, ECO:0000269|PubMed:26765567,
CC ECO:0000305|PubMed:26765567}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR RefSeq; XP_006346207.1; XM_006346145.2.
DR RefSeq; XP_006352510.1; XM_006352448.1.
DR RefSeq; XP_006352511.1; XM_006352449.2.
DR PDB; 5L83; X-ray; 1.90 A; A/B=5-114.
DR PDBsum; 5L83; -.
DR AlphaFoldDB; M1C146; -.
DR SMR; M1C146; -.
DR STRING; 4113.PGSC0003DMT400037386; -.
DR EnsemblPlants; PGSC0003DMT400037386; PGSC0003DMT400037386; PGSC0003DMG400014422.
DR EnsemblPlants; PGSC0003DMT400057469; PGSC0003DMT400057469; PGSC0003DMG402022314.
DR EnsemblPlants; RHC10H1G0274.2.1; RHC10H1G0274.2.1; RHC10H1G0274.2.
DR GeneID; 102578628; -.
DR GeneID; 102593150; -.
DR Gramene; PGSC0003DMT400037386; PGSC0003DMT400037386; PGSC0003DMG400014422.
DR Gramene; PGSC0003DMT400057469; PGSC0003DMT400057469; PGSC0003DMG402022314.
DR Gramene; RHC10H1G0274.2.1; RHC10H1G0274.2.1; RHC10H1G0274.2.
DR KEGG; sot:102578628; -.
DR KEGG; sot:102593150; -.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; M1C146; -.
DR OMA; AVYQEHK; -.
DR OrthoDB; 1508198at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IDA:UniProtKB.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Lipoprotein; Membrane; Reference proteome; Ubl conjugation pathway;
KW Vacuole.
FT CHAIN 1..119
FT /note="Autophagy-related protein 8C-like"
FT /id="PRO_0000447346"
FT PROPEP 118..119
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q2XPP5"
FT /id="PRO_0000447363"
FT SITE 117..118
FT /note="Cleavage; by ATG4"
FT /evidence="ECO:0000250|UniProtKB:Q2XPP5"
FT LIPID 117
FT /note="Phosphatidylethanolamine amidated glycine"
FT /evidence="ECO:0000305|PubMed:26765567"
FT MUTAGEN 117
FT /note="G->A: Loss of localization to autophagosome."
FT /evidence="ECO:0000269|PubMed:26765567"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:5L83"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:5L83"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:5L83"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:5L83"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:5L83"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5L83"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:5L83"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:5L83"
SQ SEQUENCE 119 AA; 13745 MW; CCF13ECBBE9BB2FD CRC64;
MAKSSFKLEH PLERRQAEAA RIREKYPDRI PVIVEKAERS DIPDIDKKKY LVPADLTVGQ
FVYVVRKRIK LSAEKAIFIF VKNILPPTAA MMSAIYEEHK DEDGFLYMTY SGENTFGSF
