ID   ATG11_YEAS7             Reviewed;        1178 AA.
AC   A6ZWU0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Autophagy-related protein 11;
DE   AltName: Full=Cytoplasm to vacuole targeting protein 9;
GN   Name=ATG11; Synonyms=CVT9; ORFNames=SCY_5767;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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, through its
CC       interaction with ATG32. Works as scaffold proteins that recruit ATG
CC       proteins to the pre-autophagosome (PAS), the site of
CC       vesicle/autophagosome formation. Required for ATG9 anterograde
CC       transport from the mitochondria to the PAS. Recruits also the ATG19-
CC       prAPE1 complex to the PAS. Required for the Cvt vesicles completion.
CC       Plays a significant role in life span extension (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and potential homooligomers. Interacts with ATG1
CC       kinase and the ATG19 and ATG34 cargo protein transporters. Interacts
CC       with ATG9, ATG17, ATG20, ATG30, ATG32, ATG36 and YPT1 (By similarity).
CC       {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   -!- PTM: Acetylated by the NuA4 histone acetyltransferase (HAT) complex.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR   EMBL; AAFW02000135; EDN61182.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZWU0; -.
DR   SMR; A6ZWU0; -.
DR   EnsemblFungi; EDN61182; EDN61182; SCY_5767.
DR   HOGENOM; CLU_272501_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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   Acetylation; Autophagy; Coiled coil; Membrane; Protein transport;
KW   Transport; Vacuole.
FT   CHAIN           1..1178
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000317927"
FT   COILED          538..572
FT                   /evidence="ECO:0000255"
FT   COILED          696..846
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1178 AA;  135011 MW;  FE859D440DB490F0 CRC64;
     MADADEYSTA PTQQEITPLQ TTATIINAIS GECITTNVDF FVSLDKFKQF IARKWKIPPD
     QLLILLPYGN KLKPSMFKEL LINRSFTLND FYVYDRRLFS LVSKPTSTNL LTSKDSNPMN
     SPNSNDLTET LEYLIKNSHI SQYQGSDTIM IKPMPSPLED ADVDLSRLNY HSVTSLLTTN
     LGWLSALEID VHYFKSLIPD IIAHIKRIFD GLTVCSQYLK LYCFDVESLY NSNVQFLNQL
     VDNGMTSKWE KCFNDTLSKL TALEGDSLQK FINIESLLEN EKSVKILNHS INGKLNKIKR
     EIDENASFRD IITVNIDRLR QIFTPNESKF ELEDQMAESF EVLVSEMRTR SRNVLDKEEE
     EFNSQEFLKS MNVMLEKDKK ESVKTLFTIS QALYSQIGEL IDLKKSLQKH AVAILGNIAF
     TQMEILGIKR LLLNECNKDL ELYKKYEVEF AQVEDLPLIY GLYLIEKYRR LSWFRQILSF
     ISNFNQDLEL FKQNELRTRN KWVKNFGSIA TVFCEDLLSS SDFKRLNEYH SHTSPPNEDE
     EDENENSIAN YRQDLVKVSQ AIDNYMTQIK ETDVSEPIID LLSKTLFETK RFHIIYSNFK
     NNNNNSSNGN SISPEGSIAL KSDDVVKGYK TRIKKLESLL HEFQYSDIGH WPQGVLNTHL
     KPFRGSATSI NKKKFLGASV LLEPANISEV NIDSVSQANN HQIQELESNV DDLLHQLQLL
     KEENNRKSMQ ISEIGKKISD LEVEKTAYRE TLTNLNQELA RLTNEEQSHR TEIFTLNASF
     KKQLNDIISQ DNEKIEKLTG DYYDVSKSRE RLQMDLDESN KKHEQEVNLL KADIERLGKQ
     IVTSEKSDAE TNSSSMEKGE KFETIPLAED TGRENQISAY TQTLQDRIFD IISTNIFILE
     NIGLLLTFDN NNNIQIRRVK GLKKGTAQSN ILDESTQMLD AHDNSLIKSP VFQKLKDEYE
     LIKSVANGSE KDTQQSIFLG NITQLYDNKL YEVAVIRRFK DIETLAKKLT KENKIKRTLL
     ERFQREKVTL RNFQIGDLAL FLPTRENVNS VGSMSSSTSS LSSSFSSVDL STPPPLDAMS
     IQSSPSVIHS NVINQASISG RDKNKLMRPW AAFTAFEEST RYFLKDEKGL TKGKEWFVGR
     IVTLEHFVAD SPSNNPFRLP KGSVWFQVTA VVVSYQGV