ID   ATG31_KLUMD             Reviewed;         139 AA.
AC   W0T3G1;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Autophagy-related protein 31 {ECO:0000303|PubMed:26442587};
GN   Name=ATG31 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_10525;
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: Plays a role in starvation-induced autophagy
CC       (PubMed:26442587). Involved in mitophagy (By similarity). Functions
CC       with ATG17 and ATG29 at the preautophagosomal structure (PAS) in order
CC       to form normal autophagosomes under starvation conditions
CC       (PubMed:26442587). {ECO:0000250|UniProtKB:Q12421,
CC       ECO:0000269|PubMed:26442587}.
CC   -!- SUBUNIT: Forms a stable complex with ATG17 and ATG29 (By similarity).
CC       Interacts directly with ATG29 (By similarity). The ATG17-ATG29-ATG31
CC       complex interacts with the ATG1-ATG13 complex (By similarity). Note=The
CC       interaction with the ATG1-ATG13 complex is induced by starvation (By
CC       similarity). {ECO:0000250|UniProtKB:Q12421}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC       {ECO:0000250|UniProtKB:Q12421}.
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 ATG31 family. {ECO:0000305}.
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DR   EMBL; AP012213; BAO38147.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0T3G1; -.
DR   SMR; W0T3G1; -.
DR   EnsemblFungi; BAO38147; BAO38147; KLMA_10525.
DR   OrthoDB; 1605510at2759; -.
DR   Proteomes; UP000065495; Chromosome 1.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR018621; Atg31.
DR   Pfam; PF09795; ATG31; 1.
PE   3: Inferred from homology;
KW   Autophagy; Protein transport; Transport.
FT   CHAIN           1..139
FT                   /note="Autophagy-related protein 31"
FT                   /id="PRO_0000443928"
SQ   SEQUENCE   139 AA;  16224 MW;  62139C6F37788A1C CRC64;
     MDTPMLLVTN VNDAIQNDDL RMDSLTNENA WFLNNISYIF EDDEPIQQED HSNYENLFII
     DSDLNGKISG VELLSEKWQL LSYDQNKPYN CISLRVMDEL RADLSPQDGD VKDLDSLARR
     YHDRNVQIRN LLDSLIQED