ID   ATG11_DEBHA             Reviewed;        1282 AA.
AC   Q6BRA6; B5RTK6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Autophagy-related protein 11;
GN   Name=ATG11; OrderedLocusNames=DEHA2D17886g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAR65691.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR382136; CAR65691.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002770337.1; XM_002770291.1.
DR   AlphaFoldDB; Q6BRA6; -.
DR   SMR; Q6BRA6; -.
DR   STRING; 4959.XP_002770337.1; -.
DR   EnsemblFungi; CAR65691; CAR65691; DEHA2D17886g.
DR   GeneID; 8998557; -.
DR   KEGG; dha:DEHA2D17886g; -.
DR   eggNOG; ENOG502QVZE; Eukaryota.
DR   HOGENOM; CLU_249394_0_0_1; -.
DR   InParanoid; Q6BRA6; -.
DR   OrthoDB; 287492at2759; -.
DR   Proteomes; UP000000599; Chromosome D.
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:0000045; P:autophagosome assembly; IEA:InterPro.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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..1282
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000124546"
FT   REGION          586..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          579..641
FT                   /evidence="ECO:0000255"
FT   COILED          722..799
FT                   /evidence="ECO:0000255"
FT   COILED          834..917
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        588..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1282 AA;  146453 MW;  5FDE280171F1B300 CRC64;
     MVAPISYLTL YNAHNGDSVK IPKPIRFHSL NGLKSFIHES FTDYIISDIE NIFLLTSFGM
     KVKFNIINEL NDIYVFDKRL FSGARDETII NAYVNQNEGG YKEMIKPTPS SLVKLEKTNI
     KQMTSSLKVN DGWSKALFQD CLGVVGQMKA YVKQINTIFK CLNIIFQFGS NFINGIEKSF
     NNYLNYIKLL NLKTLHRSWN GYYNNLRKFP SFQLKNGTGN IKISDHLNTS ELEKSSSFVS
     KTLPLVINKF NEMSASINSV NDDKVNVDKL IESLRNESIE NFKDYDTGSE DIIKDVSRLS
     QLISHDIDKL STNVSISLDW VYRIHKDEIS PKIFDKATGL YKILQNLYLF KNKIVDESLS
     IFGKIANLQM RMVNIKNDLR ILTNADDNND IANENEISIH VINNIKSAED YLSLTIDLPL
     LFGFMLIEKR RQFEWHEFYS KGIVNNVSEQ LSVIIDHEKI FRKLWLKKFG NFLSILNSKD
     ENDALRTVLP SIDVTLVNGN AESNSTFGII NNIQVERDDI STYINALEEY SNAGTTSSPS
     SKKFSELMKK NFQDLIKCTN NMKRVTKMVS SLSSFTSPVA NEIKNNDKLL ANSKDENNDK
     QAEGGGHMSE LGEVDYDINL VKGLKIRIRK LENLLHQQQY KDLSNWPVTR SNGANATSTS
     ETDGKFSLIL DSNQKTSTSS NSKIDPTNLL QRRQTLPLKL GHEKPTTSQQ SNHLDVSTTI
     DKHLDNIRLK KENNELTNEN LKLSNTNRTN EKLIEALNKQ ISNLKTVNDD QNKHHEEKLR
     KRDAENQQTI TRLETELQAF KPQNNKEVVD LKDKLSLRDA EILDLRKDIT RLHDVNEGFT
     EEVTKLNEKI ATLQSDINDV NAMKKDLLSN MASKETDTIN HRISLEEEIK KLHSKIEELT
     EDYENLMDLT QSKHNNLDIM VNYLNNMIIH LLSSIKCLVE QQFETFIEFC FILESMGLLL
     IKEHNNNKNL DEYKITRVKG LKSKRNDKIV PTSANGNVLD ETPIVSTMGN MPTSKVVDDI
     NKIIGWVDDI QSFKNISTKS SEDGDEKSCS ANTAGSVSSS VIDDLPEEIT NLSVEETNKF
     NRQSLELVKL FRDIFKSSNG SISKFEDFIN TIRFKENICI NQNQDDSGVS NKFFLGAITK
     RFKDVEGFAK KLTKENKSKA HELSQLIGKL NCKISMNSFE MDDLVLFLPT RIDRAEEIDE
     NFQPWAAFNI GAPHYFLRVQ KNEGNKTGIT HSIKDKEWMV GRVTYIEEHT VTDANFNDKD
     ANPFHLSTGV VWYVVDAKEE IF