ID   ATG11_ASHGO             Reviewed;        1072 AA.
AC   Q75B79;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Autophagy-related protein 11;
GN   Name=ATG11; OrderedLocusNames=ADL307W;
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: Involved in cytoplasm to vacuole transport (Cvt), pexophagy,
CC       mitophagy and nucleophagy. Recruits mitochondria for their selective
CC       degradation via autophagy (mitophagy) during starvation. Works as
CC       scaffold proteins that recruit ATG proteins to the pre-autophagosome
CC       (PAS), the site of vesicle/autophagosome formation. Required for the
CC       Cvt vesicles completion (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Note=During pexophagy, accumulates in the vacuolar membrane region,
CC       where the peroxisomes contact the vacuole. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR   EMBL; AE016817; AAS51613.1; -; Genomic_DNA.
DR   RefSeq; NP_983789.1; NM_209142.1.
DR   AlphaFoldDB; Q75B79; -.
DR   SMR; Q75B79; -.
DR   STRING; 33169.AAS51613; -.
DR   EnsemblFungi; AAS51613; AAS51613; AGOS_ADL307W.
DR   GeneID; 4619924; -.
DR   KEGG; ago:AGOS_ADL307W; -.
DR   eggNOG; ENOG502QVZE; Eukaryota.
DR   HOGENOM; CLU_272501_0_0_1; -.
DR   InParanoid; Q75B79; -.
DR   OMA; EIDVHYF; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IEA:EnsemblFungi.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:2000786; P:positive regulation of autophagosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IEA:EnsemblFungi.
DR   GO; GO:0031503; P:protein-containing complex localization; IEA:EnsemblFungi.
DR   GO; GO:0140255; P:regulation of cellular response to phosphate starvation; IEA:EnsemblFungi.
DR   GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR   InterPro; IPR040040; ATG11.
DR   InterPro; IPR019460; Atg11_C.
DR   InterPro; IPR045326; ATG17-like_dom.
DR   PANTHER; PTHR13222; PTHR13222; 1.
DR   Pfam; PF10377; ATG11; 1.
DR   Pfam; PF04108; ATG17_like; 1.
PE   3: Inferred from homology;
KW   Autophagy; Coiled coil; Membrane; Protein transport; Reference proteome;
KW   Transport; Vacuole.
FT   CHAIN           1..1072
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000124542"
FT   COILED          615..804
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1072 AA;  121907 MW;  132BF5C8991F6EA4 CRC64;
     MGHVEGNLQL VNAISGRSIG THVQYFMTME DLKRFVIQQW HIPGPEIFIL QPYGGKFKRG
     HFQDMVSEAK KAVARGRVRE TSVLYVFDRR LFDGGEEALA QATRHDSTTL VRPLVSPLED
     AEAEVGERAA ASLLTTNLGW LSALEIDVRY FHACIEGWVQ QLANMKECLS VLLQYLELYS
     FDIEKLYHAS AEAVDGVRQR CASNDWRQKN QELLETIDAV ASRGKLVQFV DLEEMSEAEE
     RLRELERLLS KKLSLFRGAL DENHAIRQEI ANHIKEVGTR YQDNISNYEL EAQILGNFKD
     MVKKVKEDTR TILDLDTTKV SPDLMTSAVS LFKEMKSTAI PALYTVGLSL FTQASKCMET
     KASLQREMLV ILADIAVAQV NIVDAKNSLL QQVNQDISAL HTTEQQLLRV SELPVVYGLY
     LIELYRRQHW ITGLDRYYSE HTKEIQSVLQ RELVFREKWS SDFSSYSEIF QWQDDKPQLA
     KLFSNASPLE VGRPCIDIGT IQTYIEMLAR CDVAEDSQTL LKKTLSEVSR FQFIVKSPLA
     GSVSKDSTDS MNEVIEGYKN RINKLELLLH STQFSNTSSW PTGVLNSNSL NVFHNNIASI
     NEKLLLSDYK SRDSIMSGKS NEKELQSQLV ELQKQLEEAK NEAKRVQQQL KTTKTQLLNG
     EDERTAYKET LSILNAELSK LILNQEEQKQ ELVIAAKDFQ EKLDVSMRQV NDLLKQVNFW
     KSKCGDLDKI KQDLLANMAT KETDFNNRCT DYERNIVELQ RQLSEKCDAT NERSVTSTSA
     DVPGETKEYI ESLKEVNRRL EEDMFAVFAG NIVLLENIGL LLSRGPDNKL QIIRVKGLRK
     NIDDSIIKDS SPVINSHMVK STVFQDVKNL FDELQLSQGV NDQLHFVSEL ERFYEEDLFQ
     TSVIKRFTDV ENLAKKLRKE NKAKKSVIER HNKDKITFRD LKVGDLALFL PTRGVAGSLT
     SSVASSLASS FSSVDLSTPP PPLPTASQSL IKVTPHKPHR NKSTPWAVFT ASELGVRYFL
     KDSEELVKGK DWFVGKIQSM EKYTVNGDSR NPFKLPEGMV WYEVVASCTK EL