ID   ATG11_CANAL             Reviewed;        1165 AA.
AC   Q5AMN3; A0A1D8PLD3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Autophagy-related protein 11;
GN   Name=ATG11; OrderedLocusNames=CAALFM_C401790WA;
GN   ORFNames=CaO19.12084, CaO19.4614;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017626; AOW28951.1; -; Genomic_DNA.
DR   RefSeq; XP_722686.1; XM_717593.2.
DR   AlphaFoldDB; Q5AMN3; -.
DR   SMR; Q5AMN3; -.
DR   STRING; 237561.Q5AMN3; -.
DR   PRIDE; Q5AMN3; -.
DR   GeneID; 3635597; -.
DR   KEGG; cal:CAALFM_C401790WA; -.
DR   CGD; CAL0000186587; ATG11.
DR   VEuPathDB; FungiDB:C4_01790W_A; -.
DR   eggNOG; ENOG502QVZE; Eukaryota.
DR   HOGENOM; CLU_002803_1_0_1; -.
DR   InParanoid; Q5AMN3; -.
DR   OMA; PHYFLKN; -.
DR   OrthoDB; 287492at2759; -.
DR   PRO; PR:Q5AMN3; -.
DR   Proteomes; UP000000559; Chromosome 4.
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:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IMP:CGD.
DR   GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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..1165
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000124544"
FT   COILED          239..304
FT                   /evidence="ECO:0000255"
FT   COILED          670..853
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1165 AA;  135262 MW;  E4A86AF7A32AAB68 CRC64;
     MSEISYLSIN NAHNGIIIKI PKPVRFHTLS EFKKYIQQSY SIDSVDNLFL LTTFGIKLNY
     NLINEIGEVF VYDKRLFTNI VDQSLIDQYT QSTFRVSEPT HSPLLKSNVG FLKQNLSSNL
     KINQGWARII TQDGELMDQY CRELIQQINV IFKCLNTIFQ FATNFTNEIE KNFSNFFNYV
     KLINYKTLHK SWITNYKNLK TFPTFKIDNE NIKLSDFLEV DRLQSSADYI EKFLPLIVNK
     LNELKQVIET VNEEKLTVDK FIETSRNESI SNFKNVNISN VLSQLQTESQ QLTDDIENLH
     YKNMDEIYRL HRDKLSISIY NNAKDIYKNL NDLQQFKNKL TKASLKAFNT IANLQMKMVG
     VKTEMKKITT EDETATEDSK VGDVNYKTIS NVKKYEDYLS LTIDLPLIFG FSLIEKRRQF
     EWYDFYSKGI VNNVSEQLST IIEHEKVFRG IWLKKFGTLL SLINDDPLTP SLPNIDVTLV
     GNRQNNFSIL YDLKIERDDI INYISLIEAT NMSKNFVTLL NKNFKDLIAS TNNMKKVTKV
     ISSLSTYTTN SADDKSKSSH EEGTEEEIDF DLNLIKGLKS RIKKLENLLH QQQFKNLNNW
     PVIRNVPSMT NDNRQSTIIQ PTVVSPARTN PTQLLSRNPS TTKENTTTNI HNNHQQSEVL
     DSSVIDKHLD NIRLKKLNNE LQTKNTELTN QINSKNETIT QQQKEMEHMK LKTEKRVDEL
     MKKLQEKDEE CQSLKQENKI KCDEVENLTK KLELSDNHNK ELEAKITEYT QKATSKTKEI
     ADLNKTVSNL RSELGDAMHM KNDLLSNLSS KEAEFTKERN QFNNDLKALQ LKLDEINEDY
     ENLMELTQAK QKKHDLIIND LNNVIINLMN DIKKTLLSVF EYFLEYCLVL ESMGLLLVKE
     DEIYKIKRVK GLKSKKSIGD GDMSIISNGT PSSKVIEEIE NEINIVNNIP PISSILPDSY
     SSGTESDSVV DRYNDQSMKL ISTFNQLFKF NNENENENRI DHILNTLAFK NNVQLQEDSI
     NDTRFFLNAI SKRFRDVEGF AKRQAKDNKL KEQEHRKLVH RLNSKISVNG FQEKDLVLFL
     PTRIDRPNGE NIPSNDKIQP WAAFNIGAPH YFLKTEQTKN KEWIIGRVKK ITEYKVTEEN
     VQSLESNPFQ LSVNVTWYLV EADEE