ID   ATG14_KLUMD             Reviewed;         305 AA.
AC   W0T6B6;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Autophagy-related protein 14 {ECO:0000303|PubMed:26442587};
GN   Name=ATG14 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_20709;
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, 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: Required for cytoplasm to vacuole transport (Cvt) and
CC       autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex
CC       I (By similarity). This complex is essential to recruit the ATG8-
CC       phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-
CC       autophagosomal structure (By similarity). ATG14 mediates the specific
CC       binding of the VPS34 PI3-kinase complex I to the preautophagosomal
CC       structure (PAS) (By similarity). {ECO:0000250|UniProtKB:P38270}.
CC   -!- SUBUNIT: Component of the autophagy-specific VPS34 PI3-kinase complex I
CC       (By similarity). {ECO:0000250|UniProtKB:P38270}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250|UniProtKB:P38270}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P38270}. Vacuole membrane
CC       {ECO:0000250|UniProtKB:P38270}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P38270}.
CC   -!- DOMAIN: Coiled-Coils at the N-terminal half are essential for autophagy
CC       (By similarity). {ECO:0000250|UniProtKB:P38270}.
CC   -!- DISRUPTION PHENOTYPE: Still forms preautophagosomal structures (PAS) in
CC       proximity to the vacuolar membrane (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 ATG14 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP012214; BAO39167.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0T6B6; -.
DR   SMR; W0T6B6; -.
DR   EnsemblFungi; BAO39167; BAO39167; KLMA_20709.
DR   OrthoDB; 1463349at2759; -.
DR   Proteomes; UP000065495; Chromosome 2.
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:0016236; P:macroautophagy; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR023261; Autophagy-related_protein_14.
DR   InterPro; IPR018791; UV_resistance/autophagy_Atg14.
DR   Pfam; PF10186; ATG14; 1.
DR   PRINTS; PR02030; AUTOPHGYRP14.
PE   3: Inferred from homology;
KW   Autophagy; Coiled coil; Membrane; Protein transport; Transport; Vacuole.
FT   CHAIN           1..305
FT                   /note="Autophagy-related protein 14"
FT                   /id="PRO_0000443911"
FT   COILED          34..147
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   305 AA;  35265 MW;  ED8DAB9EF6EA0B0A CRC64;
     MIHCGICGKA KTADVQFICC HCINGSPAVL LRDKMNLLIL RQEVEQLKTA VEDQLETGFA
     GEGQLGRQLQ KLDIYNEKRR LIKLRQRLQL ARNKVQLKRN KYNELLQIMS TNGYLEESTS
     ATDSIDLEEQ AAEESASLDT LSHILARNQK QLFAELCRWF RIRKSDEDDV FSYTIWGLPM
     VNLKNGSELD PSIMVSSMRY LQQYLQLAFR IWLFKAICDK PIENDRNIIE NFTQLIYDTL
     DILRARKLVS KSVSIRDILI RYDLDGMIYH LSQNKYLSSL DDASNSYPPT MQNIKQLVMS
     MIPSI