ID   ATG11_KLULA             Reviewed;        1046 AA.
AC   Q6CVG9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Autophagy-related protein 11;
GN   Name=ATG11; OrderedLocusNames=KLLA0B12133g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382122; CAH02463.1; -; Genomic_DNA.
DR   RefSeq; XP_452070.1; XM_452070.1.
DR   AlphaFoldDB; Q6CVG9; -.
DR   SMR; Q6CVG9; -.
DR   STRING; 28985.XP_452070.1; -.
DR   EnsemblFungi; CAH02463; CAH02463; KLLA0_B12133g.
DR   GeneID; 2897251; -.
DR   KEGG; kla:KLLA0_B12133g; -.
DR   eggNOG; ENOG502QVZE; Eukaryota.
DR   HOGENOM; CLU_272501_0_0_1; -.
DR   InParanoid; Q6CVG9; -.
DR   OMA; EIDVHYF; -.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:EnsemblFungi.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0000149; F:SNARE binding; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0030242; P:autophagy of peroxisome; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR   GO; GO:2000786; P:positive regulation of autophagosome assembly; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR   InterPro; IPR040040; ATG11.
DR   InterPro; IPR019460; Atg11_C.
DR   InterPro; IPR045326; ATG17-like_dom.
DR   PANTHER; PTHR13222; PTHR13222; 2.
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..1046
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000124548"
FT   COILED          582..730
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1046 AA;  120702 MW;  469A749025E5DA07 CRC64;
     MPPCKLICAT SGVSHQLSNV YFPSFLDLKQ FASDTFQIPL DDILLLLPYG MILKKAGWDS
     RKLQQEGLEE IYVFDRGIFN EEIEFSPKPR FQLFKPLPSP ISDSLQLDKN VILRNLGWLK
     ALQSDVEFFQ DVIKETYQDV QRLLECGTVM LEYLKNYCYE VEVLYNGNVD FLNKLHEDGA
     SNQWHSFYDN ILGNIKVSNQ LLSSFFNYSE LTEIEDSIHR LDRELNAKLK ELKKSIDECY
     QQRTQLISDL DDVKKNSVVS SDDMDNQMVE RFKEMATEIE LVSNQYKEEA SKDASKEKFE
     TFKSVHVPKL QTISQAMFNK ASTNLDTKAT VQQKLQQLYL SVAKSQMSVI MVKSVLTKDV
     KTNMKFLKNE ELKLSQVLDL PMCYGLYLIE LYREQLWTDR YSQLRQQHES SLQHLLDDEV
     RQRNSWYKDF QWITRFLDVD SLLPSSVYIP SISDHKQVTL SQIKDYINQL ASLNLGEPTI
     NLLKSKVSQA ELTGLHLPTD YALSKDSELI IEGYKARIKK LEHLLLDAQF HQYDSWPAGI
     LNKETAMVQM FRNSTVSTKL QQSSTFDLPS SKQQHESNKT FEEFQNLQKD ISKYSELTKT
     LETELSTLKS QLSHMEVEKN AYRESMTNLN KELSTLLIER ENFYSEMNSR SENFKKHLGS
     LFEQNEELVR ESEESRRKSE DLNKMKEDLL VNMATQEVQA EQERASLQEE VESLKKDLNQ
     LQISKSKTID AEFINFNKQL EKTLYDVFQG SIFILASIGL LLSKDQDGNF QIVRVKGLRK
     DLDSSLADMN SSMAKSVIAQ EIKSTFESIK DQIDYKPHEN FITYIEKLFG NQLFETSVIR
     RFNDIESLAK KLRKENKNKK LLLQKSARDK ITIYNFQPGD LALFLPINDQ ELLLNSSISS
     LNSSFSSIDL NSSTQSVMQR PNVVKSDIAA SILNGSSASI TENIPLSKAN RNPALNANGR
     PDTFNVNTQD SAKKHVVWAI FTATNTDIKY VLRNSTSNYE LLKDREWAMG RISALEKHVV
     GDDSKNPFKF PRNTVWYEVD AFFNLD