ID   MON1_KLULA              Reviewed;         528 AA.
AC   Q6CKL5;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Vacuolar fusion protein MON1;
GN   Name=MON1; OrderedLocusNames=KLLA0F09768g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: In complex with CCZ1, is required for multiple vacuole
CC       delivery pathways including the cytoplasm to vacuole transport (Cvt),
CC       autophagy, pexophagy and endocytosis. The CCZ1-MON1 complex acts at the
CC       fusion of vesicles with the vacuole, through its regulation of the
CC       SNARE complex during the coordinated priming and docking stages of
CC       fusion, and particularly at the stage of tethering/docking.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Prevacuolar
CC       compartment membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Vacuole membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MON1/SAND family. {ECO:0000305}.
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DR   EMBL; CR382126; CAG98232.1; -; Genomic_DNA.
DR   RefSeq; XP_455524.1; XM_455524.1.
DR   AlphaFoldDB; Q6CKL5; -.
DR   STRING; 28985.XP_455524.1; -.
DR   EnsemblFungi; CAG98232; CAG98232; KLLA0_F09768g.
DR   GeneID; 2894962; -.
DR   KEGG; kla:KLLA0_F09768g; -.
DR   eggNOG; KOG0997; Eukaryota.
DR   HOGENOM; CLU_014574_0_0_1; -.
DR   InParanoid; Q6CKL5; -.
DR   OMA; ENENHAM; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0032585; C:multivesicular body 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:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR043972; FUZ/MON1/HPS1_longin_1.
DR   InterPro; IPR043971; FUZ/MON1/HPS1_longin_2.
DR   InterPro; IPR043970; FUZ/MON1/HPS1_longin_3.
DR   InterPro; IPR004353; Mon1.
DR   PANTHER; PTHR13027; PTHR13027; 1.
DR   Pfam; PF19036; Fuz_longin_1; 1.
DR   Pfam; PF19037; Fuz_longin_2; 1.
DR   Pfam; PF19038; Fuz_longin_3; 1.
DR   PRINTS; PR01546; YEAST73DUF.
PE   3: Inferred from homology;
KW   Autophagy; Endosome; Membrane; Protein transport; Reference proteome;
KW   Transport; Vacuole.
FT   CHAIN           1..528
FT                   /note="Vacuolar fusion protein MON1"
FT                   /id="PRO_0000278863"
SQ   SEQUENCE   528 AA;  60856 MW;  270C01FB11B173D6 CRC64;
     MRRSPSFQIS TKNSAKPTTS IDLTNHLSAR GGLFYQDIDT GTTASIKAKN DPNLLAATYD
     HSISADTDLN IDLQSLITSE LNSLYPLTLN QETSNKSANT TKFIDERGGK DKHFFVFTSA
     GKLVFSQWEN ENHAMGLTGI IHTVMNYFNI NDNTAMRQFT MYGKDGIMTR FVFLDKNHIK
     LMVQCNNNYE STAQLQQQLD LVYSYIISSV SQRNLNKLML KRSNFDLQHY LTDLDQQLLK
     SLCESLATQP KLTWFANSLE CLPMSPKKRN AINSILSTTY LDFNISNHNG QILYTLVTSL
     DMRLISILRP SNHTLHTMDL QILFEVVRAQ LTDLLLDKVL WFPICFQKFN DNGFLYALIK
     VLPNNTIMMV ISSQKNAFDI LNEFVRRIED KMIDDNTCNN LELQLLDWHK KFPYINHFIY
     KMKRTVQIYT PSQPTNEMLQ FYYHLKNLCE DDKGTNLNKS SVAMLKWKND ATPGLLSGVY
     WATEKFELYI LLNDINLSNQ SILKSAKLLI QHIREIESYL FISRGVTF