ID   ATG16_KLUMD             Reviewed;         126 AA.
AC   W0T661;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Autophagy-related protein 16 {ECO:0000303|PubMed:26442587};
GN   Name=ATG16 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_20649;
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: Stabilizes the ATG5-ATG12 conjugate (By similarity). The
CC       ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-
CC       conjugation to phosphatidylethanolamine and ATG8 localization to the
CC       pre-autophagosomal structure (PAS) (PubMed:26442587). Recruits also
CC       ATG3 to the PAS (By similarity). Involved in endoplasmic reticulum-
CC       specific autophagic process and is essential for the survival of cells
CC       subjected to severe ER stress (By similarity).
CC       {ECO:0000250|UniProtKB:Q03818, ECO:0000269|PubMed:26442587}.
CC   -!- SUBUNIT: Homodimer (By similarity). Part of the ATG5-ATG12/ATG16
CC       complex (By similarity). Several units of each may be present in this
CC       complex (By similarity). Interacts directly with ATG12 (By similarity).
CC       {ECO:0000250|UniProtKB:Q03818}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250|UniProtKB:Q03818}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q03818}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the formation of preautophagosomal
CC       structures (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 ATG16 family. {ECO:0000305}.
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DR   EMBL; AP012214; BAO39107.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0T661; -.
DR   SMR; W0T661; -.
DR   EnsemblFungi; BAO39107; BAO39107; KLMA_20649.
DR   OrthoDB; 1616621at2759; -.
DR   Proteomes; UP000065495; Chromosome 2.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IEA:EnsemblFungi.
DR   GO; GO:0061908; C:phagophore; 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:0019776; F:Atg8 ligase activity; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:1905037; P:autophagosome organization; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IEA:EnsemblFungi.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR   GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   InterPro; IPR013923; Autophagy-rel_prot_16_dom.
DR   Pfam; PF08614; ATG16; 1.
PE   3: Inferred from homology;
KW   Autophagy; Coiled coil; Membrane; Protein transport; Transport.
FT   CHAIN           1..126
FT                   /note="Autophagy-related protein 16"
FT                   /id="PRO_0000443915"
FT   COILED          76..113
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   126 AA;  15068 MW;  B77D09E1D3B538E4 CRC64;
     MEYELLESIR ARDLVDKRFS QLFEEVPLVP KLEKAGEGDT NVKESSIKNL KDYLKLRDEE
     VYKLKDILKL KNRDTERLND ELLSANIESN LLQERLEKLQ QEYDRLIERW LLKAQKEADT
     MNSHFK