ID   ATG11_CANGA             Reviewed;        1110 AA.
AC   Q6FRH2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Autophagy-related protein 11;
GN   Name=ATG11; OrderedLocusNames=CAGL0H08558g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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).
RN   [2]
RP   FUNCTION.
RX   PubMed=19811500; DOI=10.1111/j.1462-5822.2009.01391.x;
RA   Roetzer A., Gratz N., Kovarik P., Schuller C.;
RT   "Autophagy supports Candida glabrata survival during phagocytosis.";
RL   Cell. Microbiol. 12:199-216(2010).
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). Contributes through its
CC       regulation of pexophagy to survival during engulfment by host
CC       phagocytic cells during infection. Through its function in autophagy,
CC       acts as an important virulence factor that supports the viability of
CC       C.glabrata in the phagosomal compartment of infected innate immune
CC       cells. {ECO:0000250, ECO:0000269|PubMed:19811500}.
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; CR380954; CAG60105.1; -; Genomic_DNA.
DR   RefSeq; XP_447172.1; XM_447172.1.
DR   AlphaFoldDB; Q6FRH2; -.
DR   SMR; Q6FRH2; -.
DR   STRING; 5478.XP_447172.1; -.
DR   PRIDE; Q6FRH2; -.
DR   EnsemblFungi; CAG60105; CAG60105; CAGL0H08558g.
DR   GeneID; 2888485; -.
DR   KEGG; cgr:CAGL0H08558g; -.
DR   CGD; CAL0130611; ATG11.
DR   VEuPathDB; FungiDB:CAGL0H08558g; -.
DR   eggNOG; ENOG502QVZE; Eukaryota.
DR   HOGENOM; CLU_272501_0_0_1; -.
DR   InParanoid; Q6FRH2; -.
DR   OMA; EIDVHYF; -.
DR   Proteomes; UP000002428; Chromosome H.
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; Virulence.
FT   CHAIN           1..1110
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000124545"
FT   COILED          264..309
FT                   /evidence="ECO:0000255"
FT   COILED          651..803
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1110 AA;  127649 MW;  D5BF8AE34FBABD89 CRC64;
     MEYRCLDCTT GDTIAVDLKV FLDLKEFKSY LSNKWGVPRA QILLLYPFGI KLKDSNFRHA
     SDLESPEIYV YDRRLFSLTN EPHTGADAHA DSDADADADT ADVEQQAAQL LDSLLEQRRH
     PQLQDDLIRP IPSPLEDLKI ADGISHRTAV SMLTTNLGWL SALEIDVNYY SSISDKCKED
     TQSLARCLGT CEQYLGLYCY DVERLYNSNV VFLDQLHENS LQSRWKECYK NTLTKLAGLN
     GYLSQYVDEA KQIEKEVTLK SLDGKVNSKL KQIKKELDSY ADQRKSIQNE IENLKNIKDM
     KNDDNELHEM QKSFDSIADT VRKASRDILD KDDALFTDEY ITQEVVPVMI DIQKKVKTLL
     TVSQALYENM HELLTHKRNF QIQIIVKLGQ IAWIQLQISE LKQYLLNDCN ADLTLYKDLE
     VEFAQIEDYP LIYGLYLVEK YRRQVWKCGM AKNMISISND IKERSAAELT TRKNWYKNFG
     ELSKPFNEDL TKYNDLDEIS KLMNSDSQFL KEKFIQDLRN EQRKLEDVIK SFIKNMHDLG
     LSKETTQVLE QSFKEASNSN ICSQIDVTYD HRRINNENDL IKRYKIRIRK LESLLHEQGY
     SSISKWPSGV LNHTDRPNYF ADNVSPAGRS LLVSSSALLG LEPSASLKTD AEMFDLKKEI
     GDLSEKVTAL EKDNKLKTDQ LKITHSKLID IEVEKAAFRE TLNHLNKELA RLTVNEEDQT
     NLLKEERLRF KKEMTSVTVV NQNLMNNLDA LQKTFEDVEL ENAHLKSKLK ELQQRQDQLI
     EDSANEKLEI KSKYEKLIKE KDENMGQAFA VTNKAISGEQ NKTESDIIHS SPYPEAILHL
     RTELFDIFST NIYILENIGL LLTETSAGKF EIKRVKGLKK GLSQSLLDES AQISPIDGVI
     NSVVYKNIRA QYEQLPNDNN ISNCELFISS VKKIYENKLF ESAVINRFKD IETLAKRLTK
     ENKSKRILID LYQNERLAVK DFRVNDLALF LPTKEALSET KSLSSSMASS FSSVDLSTPI
     SGANNNITAS RKSLHKPNVK HPWAAFTAFN ESSRYFLKDE NMVTDNKEWF IGKITDIQRQ
     VVENISTNNP FKLPKDTVWY LISAEMISID