ID   ATG11_KLUMD             Reviewed;        1084 AA.
AC   W0TFN1;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Autophagy-related protein 11 {ECO:0000303|PubMed:26442587};
GN   Name=ATG11 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_70337;
OS   Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS   (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1003335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275;
RX   PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA   Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA   Matsutani M., Murata M., Fujimoto N., Suprayogi X., Tsuchikane K.,
RA   Limtong S., Fujita N., Yamada M.;
RT   "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT   complete genome sequence and transcriptome analyses.";
RL   Biotechnol. Biofuels 8:47-47(2015).
RN   [2]
RP   IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26442587; DOI=10.1074/jbc.m115.684233;
RA   Yamamoto H., Shima T., Yamaguchi M., Mochizuki Y., Hoshida H., Kakuta S.,
RA   Kondo-Kakuta C., Noda N.N., Inagaki F., Itoh T., Akada R., Ohsumi Y.;
RT   "The thermotolerant yeast Kluyveromyces marxianus is a useful organism for
RT   structural and biochemical studies of autophagy.";
RL   J. Biol. Chem. 290:29506-29518(2015).
CC   -!- FUNCTION: Involved in cytoplasm to vacuole transport (Cvt), pexophagy,
CC       mitophagy and nucleophagy (PubMed:26442587). Recruits mitochondria for
CC       their selective degradation via autophagy (mitophagy) during
CC       starvation, through its interaction with ATG32 (By similarity). Works
CC       as scaffold proteins that recruit ATG proteins to the pre-autophagosome
CC       (PAS), the site of vesicle/autophagosome formation (By similarity).
CC       Required for ATG9 anterograde transport from the mitochondria to the
CC       PAS (By similarity). Recruits also the ATG19-prAPE1 complex to the PAS
CC       (By similarity). Required for the Cvt vesicles completion (By
CC       similarity). {ECO:0000250|UniProtKB:Q12527,
CC       ECO:0000269|PubMed:26442587}.
CC   -!- SUBUNIT: Homodimer and potential homooligomers (By similarity).
CC       Interacts with ATG1 kinase and the ATG19 and ATG34 cargo protein
CC       transporters (By similarity). Interacts with ATG9, ATG17 and ATG20 (By
CC       similarity). {ECO:0000250|UniProtKB:Q12527}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250|UniProtKB:Q12527}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q12527}. Vacuole membrane
CC       {ECO:0000250|UniProtKB:Q12527}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q12527}. Note=During pexophagy, accumulates in
CC       the vacuolar membrane region, where the peroxisomes contact the vacuole
CC       (By similarity). {ECO:0000250|UniProtKB:Q12527}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the cytoplasm to vacuole transport (Cvt)
CC       pathway (PubMed:26442587). Mislocalizes ATG8 in the cytosol, when
CC       ATG17, ATG29 or ATG31 are also deleted (PubMed:26442587).
CC       {ECO:0000269|PubMed:26442587}.
CC   -!- MISCELLANEOUS: Kluyveromyces marxianus proteins are shorter in length
CC       and have a more ordered secondary structure than their S.cerevisiae
CC       counterparts, which might contribute to the superior thermotolerance
CC       and solubility (PubMed:26442587). K.marxianus could be therefore useful
CC       as a new model organism for further elucidation of the molecular
CC       details of autophagy (PubMed:26442587). {ECO:0000269|PubMed:26442587}.
CC   -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR   EMBL; AP012219; BAO42185.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0TFN1; -.
DR   SMR; W0TFN1; -.
DR   EnsemblFungi; BAO42185; BAO42185; KLMA_70337.
DR   OrthoDB; 287492at2759; -.
DR   Proteomes; UP000065495; Chromosome 7.
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; 2.
DR   Pfam; PF10377; ATG11; 1.
DR   Pfam; PF04108; ATG17_like; 1.
PE   3: Inferred from homology;
KW   Autophagy; Coiled coil; Membrane; Protein transport; Transport; Vacuole.
FT   CHAIN           1..1084
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000443903"
FT   REGION          925..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          973..1007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          585..739
FT                   /evidence="ECO:0000255"
FT   COILED          847..879
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        936..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1084 AA;  124697 MW;  2CAF80E1DB0A3902 CRC64;
     MPPCELISAS NGASFQLSDL YFPSFLDLKQ FVGETFHISV DDILLLLSYG IILKRSQWDS
     TKIRSEGLKS IYVFDRKLFN EDIELAVEER FRLFKPLDSP MSDLSEVDRN IVLRNMGWLK
     ALQSDVEFFQ LSIEQTRKEV QNMLDCGVVM LEYLKNYCHE VETLYNSHVG FLNKLHEHSA
     SSQWREVYDS VLEAVKIDQQ RSLASFFQID ELNQIEAKIR HTDHELNMKL KELKKTIDTC
     YQHRKTLVSE LENIKSISVV SPDCMDKQMT DKFNEMAQEL EAASNEWVQN SENNDHISEK
     VKQMKDSHIP NLQTISQSLF NKASKIIETK TDMQRQLRSL YISVAKSQMD IIEVKSTLTK
     DMKSDMKLLQ TYELQLSQVL DLPMCYGLYL IELYRQQLWM DNYTHIKDQH ESALQVMLQE
     EIHQRKMWYR DFQWISKFLK VDQSLPSTVS ITPLKALRRV DLLQINEYFN QLSSAKVSET
     TLNVLKSKLS QAEMDNMLPE LSEQSSNDTG AAIEGYKSRI KKLENLLLDA QFQRYDSWPS
     GILNKEIAMV QMFRNNTLNN KVQRSSTDDI SNSIQQSYSK TLGDVQNLQK AISEYSGLTD
     TLKEELSTLK SQISNMEVEK NAYKESMANL NKELSNLLIN RENFHTEMME RSNDFKKHLA
     LVGEENEQLT KQNQQLSNEI IESQKKYEEL NKIKDDLLLN MANQETQAEQ ERAALQEEIE
     SLKKEVGQLQ MAKSSLTESE ELLGINKQLE KTLYDVFQGS IFLLESIGLL LSKDIDGKFQ
     IVRVKGLRKD LDSSVIDMNG SLVKSVVSHE IKDTFESIKD SLDYKPHENF ISYTEKLFGN
     QLFEMAVIRR FNDIESLAKK LRKENKNKKI LLQKYTNDKI TINNFQLGDL ALFLPINDQE
     LLLNSSVSSL NSSFSSIDLN SSTQSMIPPR VIPNRVEPAS NTNNSNPSSV PEDMGSPNMN
     RVNTMGNVKV NANIGSNNSN NNYVNTGNAN GNNKPETNID TTSSTNAESP KKQIVWAIFT
     ATNTEVKYIL RNTMSNYELL REKEWAVGRI TALEKNIVME GARNPFKFPQ NTVWFEVDAL
     FNLS