ID   ATG17_KLUMD             Reviewed;         421 AA.
AC   W0T3R8;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Autophagy-related protein 17 {ECO:0000303|PubMed:26442587};
GN   Name=ATG17 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_10625;
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: Autophagy-specific protein that functions with ATG13, ATG29,
CC       and CIS1/ATG31 in response to autophagy-inducing signals as a scaffold
CC       to recruit other ATG proteins to organize pre-autophagosomal structure
CC       (PAS) formation (PubMed:26442587). Modulates the timing and magnitude
CC       of the autophagy response, such as the size of the sequestering
CC       vesicles, through interacting with and regulating ATG1 kinase activity
CC       (By similarity). Plays particularly a role in pexophagy and nucleophagy
CC       (By similarity). With ATG13, is required for ATG1 activation by
CC       autophosphorylation (By similarity). Recruits ATG9 to the pre-
CC       autophagosomal structure (By similarity).
CC       {ECO:0000250|UniProtKB:Q06410, ECO:0000269|PubMed:26442587}.
CC   -!- SUBUNIT: Forms a complex with ATG13, ATG29 and CIS1/ATG31 (By
CC       similarity). The ATG17-ATG29-ATG31 complex interacts with the ATG1-
CC       ATG13 complex (By similarity). Forms a complex with SNX4 and ATG20 (By
CC       similarity). Interacts with ATG11 (By similarity).
CC       {ECO:0000250|UniProtKB:Q06410}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06410}.
CC       Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q06410};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q06410}.
CC   -!- DISRUPTION PHENOTYPE: Mislocalizes ATG8 in the cytosol, when ATG11 is
CC       also deleted (PubMed:26442587). {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 ATG17 family. {ECO:0000305}.
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DR   EMBL; AP012213; BAO38247.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0T3R8; -.
DR   SMR; W0T3R8; -.
DR   EnsemblFungi; BAO38247; BAO38247; KLMA_10625.
DR   OrthoDB; 1496047at2759; -.
DR   Proteomes; UP000065495; Chromosome 1.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:EnsemblFungi.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0030295; F:protein kinase activator 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:0044805; P:late nucleophagy; 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:0045772; P:positive regulation of autophagosome size; IEA:EnsemblFungi.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IEA:EnsemblFungi.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007240; Atg17.
DR   InterPro; IPR045326; ATG17-like_dom.
DR   PANTHER; PTHR28005; PTHR28005; 1.
DR   Pfam; PF04108; ATG17_like; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Membrane; Protein transport; Transport.
FT   CHAIN           1..421
FT                   /note="Autophagy-related protein 17"
FT                   /id="PRO_0000443917"
SQ   SEQUENCE   421 AA;  49638 MW;  A7BF68CC6A152EC0 CRC64;
     MSYHYDGIPD IEIDLYWNKA RNHLLKAQVE CEESLKLLST IRSEMDSCQK SRLKLQFILN
     CLVNQVEFFS SVILEKCIAV ELLDNEWSKV VLVGVVKDLN YWQDEITNKI NALKNTKYDL
     NAEYKSLADF ICEDHVEILQ QKLDEVPFIK KQVSNIRQHY KSIKEGVQYQ LKAGKVKKLK
     KYYETHFSRD NHLFELLEGE YLTKLNSYES ELTDYIRSIT DHFDKCSILK ADGLPPQDLK
     DLFEVVKNDD AELEHIRELI YESDAEITQF YKNVEGTITS IKENVADFYG LSTKIMVELE
     KCEEYVSIFQ DIAKLVSVYK ESCIRKIEQV QELCEVYDKF KKAYFNLLKE RERRKSVAIQ
     MKSILDECKG KLMALNEDDL DHRQQFLHEN GDYLPENIWP GKIDDMTPLY SLEYTIYNEQ
     K