ID   ATG14_MAGO7             Reviewed;         428 AA.
AC   G4N6P7;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Autophagy-related protein 14 {ECO:0000303|PubMed:28067330};
GN   Name=ATG14 {ECO:0000303|PubMed:28067330}; ORFNames=MGG_03698;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   IDENTIFICATION, INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP   LOCATION, AND DOMAIN.
RX   PubMed=28067330; DOI=10.1038/srep40018;
RA   Liu X.H., Zhao Y.H., Zhu X.M., Zeng X.Q., Huang L.Y., Dong B., Su Z.Z.,
RA   Wang Y., Lu J.P., Lin F.C.;
RT   "Autophagy-related protein MoAtg14 is involved in differentiation,
RT   development and pathogenicity in the rice blast fungus Magnaporthe
RT   oryzae.";
RL   Sci. Rep. 7:40018-40018(2017).
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 (PubMed:28067330). 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). Plays a crucial role in hyphal
CC       development, conidiogenesis and pathogenicity (PubMed:28067330). Also
CC       required for glycogen mobilization, quantity of lipid bodies, and the
CC       turgor pressure of appressoria (PubMed:28067330).
CC       {ECO:0000250|UniProtKB:P38270, ECO:0000269|PubMed:28067330}.
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:0000269|PubMed:28067330}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P38270}. Vacuole membrane
CC       {ECO:0000250|UniProtKB:P38270}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P38270}.
CC   -!- INDUCTION: Expression is hihghly increased in nitrogen starved hyphae,
CC       as well as in invasive hyphae (PubMed:28067330).
CC       {ECO:0000269|PubMed:28067330}.
CC   -!- DOMAIN: The coiled-Coil domain is essential for autophagy
CC       (PubMed:28067330). {ECO:0000269|PubMed:28067330}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the formation of sparse hyphae with
CC       necrotic centrality, and a reduced number of condia (PubMed:28067330).
CC       Fails to penetrate both hosts in infection assays with the two
CC       susceptible hosts rice and barley (PubMed:28067330). Leads also to
CC       delayed mobilization, reduced lipid bodies and lower turgor pressure of
CC       the appressoria (PubMed:28067330). Impairs the delivery of ATG8 to the
CC       vacuoles upon nitrogen starvation (PubMed:28067330).
CC       {ECO:0000269|PubMed:28067330}.
CC   -!- SIMILARITY: Belongs to the ATG14 family. {ECO:0000305}.
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DR   EMBL; CM001234; EHA49864.1; -; Genomic_DNA.
DR   RefSeq; XP_003716183.1; XM_003716135.1.
DR   AlphaFoldDB; G4N6P7; -.
DR   SMR; G4N6P7; -.
DR   EnsemblFungi; MGG_03698T0; MGG_03698T0; MGG_03698.
DR   GeneID; 2676764; -.
DR   KEGG; mgr:MGG_03698; -.
DR   VEuPathDB; FungiDB:MGG_03698; -.
DR   eggNOG; ENOG502S2VB; Eukaryota.
DR   HOGENOM; CLU_021590_1_0_1; -.
DR   InParanoid; G4N6P7; -.
DR   OMA; HYLSIRL; -.
DR   OrthoDB; 975832at2759; -.
DR   PHI-base; PHI:6902; -.
DR   Proteomes; UP000009058; Chromosome 4.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR018791; UV_resistance/autophagy_Atg14.
DR   Pfam; PF10186; ATG14; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Coiled coil; Membrane; Protein transport; Reference proteome;
KW   Transport; Vacuole.
FT   CHAIN           1..428
FT                   /note="Autophagy-related protein 14"
FT                   /id="PRO_0000443912"
FT   COILED          82..143
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   428 AA;  47470 MW;  BF278612E46DEA0D CRC64;
     MSCYICGRGH HAQRLPFLCP IDARNRLYEG RLAQAHTLID SDRLKQQTNA LIEQPPPTAA
     KASRSSPAAR KAAIDDWASK HQEAIDRTAE IIAQADRLKA EVEAARQEIR QRKKTLARRK
     SDLAEAADGI EEKRKKQLDK VKDNIAATRA DWDLVHESTA SNRAFLCMEA ARLYGLRRLK
     KGSSVKYELG GAEVVDLHAL TGASPQAITI SFSHIVHILN RACQYLAIRL PAEIILPHAD
     YPRPAILSIT SSYSYNHDDI PYPGTSDQQS ELNTLPQDDL FYQRLPRARP LFIDRPLPVL
     AKEDPAMYSL FIEGVALLAH DVAWACCSQG VPVGPEDVLH VGRNLYNLLI GNQLLRGVSS
     NDGGNSTPQM GRYSHGAVHS YLGSAEGSDL VRTFRLPNPI KLADRLKSKL SSDAPNPDWE
     LLEDDAWT