ATG16_ASHGO
ID ATG16_ASHGO Reviewed; 124 AA.
AC Q755K3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Autophagy protein 16;
GN Name=ATG16; OrderedLocusNames=AFL186W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Stabilizes the ATG5-ATG12 conjugate which is necessary for
CC autophagy. The ATG5-ATG12/ATG16 complex is required for efficient
CC promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8
CC localization to the pre-autophagosomal structure (PAS). Recruits also
CC ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic
CC process and is essential for the survival of cells subjected to severe
CC ER stress (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Part of the ATG5-ATG12/ATG16
CC complex. Several units of each may be present in this complex (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q03818}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q03818}.
CC -!- SIMILARITY: Belongs to the ATG16 family. {ECO:0000305}.
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DR EMBL; AE016819; AAS53188.1; -; Genomic_DNA.
DR RefSeq; NP_985364.1; NM_210718.1.
DR PDB; 6RGO; X-ray; 3.70 A; C/D=70-124.
DR PDBsum; 6RGO; -.
DR AlphaFoldDB; Q755K3; -.
DR SMR; Q755K3; -.
DR STRING; 33169.AAS53188; -.
DR PRIDE; Q755K3; -.
DR EnsemblFungi; AAS53188; AAS53188; AGOS_AFL186W.
DR GeneID; 4621589; -.
DR KEGG; ago:AGOS_AFL186W; -.
DR eggNOG; ENOG502S6TV; Eukaryota.
DR HOGENOM; CLU_158825_0_0_1; -.
DR InParanoid; Q755K3; -.
DR OMA; QLRNKDY; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IEA:EnsemblFungi.
DR GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
DR GO; GO:0019776; F:Atg8 ligase activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:EnsemblFungi.
DR GO; GO:1905037; P:autophagosome organization; IEA:EnsemblFungi.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0006501; P:C-terminal protein lipidation; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR InterPro; IPR013923; Autophagy-rel_prot_16_dom.
DR Pfam; PF08614; ATG16; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Coiled coil; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..124
FT /note="Autophagy protein 16"
FT /id="PRO_0000218587"
FT COILED 42..107
FT /evidence="ECO:0000255"
SQ SEQUENCE 124 AA; 14390 MW; C5A88752FB1B2A5F CRC64;
MDLHQLYLDR LRQRDRIEGN FCYLFEAAVV LETAQPPQDS RDLVAKSLRE ELHAHEQEIH
KLKDIVHLRS KDAEKLNDEI ISLNIENSLL QDKLTALQAE YDKLIQRWLA KAQSEADAMN
QGLA