MON1_CANGA
ID MON1_CANGA Reviewed; 597 AA.
AC Q6FU19;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Vacuolar fusion protein MON1;
GN Name=MON1; OrderedLocusNames=CAGL0F07051g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380952; CAG59199.1; -; Genomic_DNA.
DR RefSeq; XP_446275.1; XM_446275.1.
DR AlphaFoldDB; Q6FU19; -.
DR SMR; Q6FU19; -.
DR STRING; 5478.XP_446275.1; -.
DR PRIDE; Q6FU19; -.
DR EnsemblFungi; CAG59199; CAG59199; CAGL0F07051g.
DR GeneID; 2887661; -.
DR KEGG; cgr:CAGL0F07051g; -.
DR CGD; CAL0129189; CAGL0F07051g.
DR VEuPathDB; FungiDB:CAGL0F07051g; -.
DR eggNOG; KOG0997; Eukaryota.
DR HOGENOM; CLU_014574_0_0_1; -.
DR InParanoid; Q6FU19; -.
DR OMA; YTHIRNN; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0035658; C:Mon1-Ccz1 complex; IEA:EnsemblFungi.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0001786; F:phosphatidylserine binding; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IEA:EnsemblFungi.
DR GO; GO:0016236; P:macroautophagy; IEA:EnsemblFungi.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:EnsemblFungi.
DR GO; GO:0044395; P:protein targeting to vacuolar membrane; IEA:EnsemblFungi.
DR GO; GO:0048278; P:vesicle docking; IEA:EnsemblFungi.
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..597
FT /note="Vacuolar fusion protein MON1"
FT /id="PRO_0000278857"
FT REGION 33..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 68276 MW; E22263AC3DD4FF6F CRC64;
MLSRKSSNWL LNVPSQSEAT TSVNLQSTEV GSITHTSSDD NIATPQDGID HIDNDRSSSR
AENIDMTASM VSHSRSLASL RPVMSSNFQN ESDHIDDSLE FDLMRSLNES IYSTDGAISK
PFMINEMPQI FDKNSNEDIT KNFFIFTSAG KPVYSMYEND KFSASYIGLL TSIISFFQTS
NEDNIKTFTS KESNITFVFC NKDPIFYVAM SRCRDESRDE LEAQLHFLHS FVLSTLTSKQ
LTKLFQKRDN FDLRSHLEST DFETLSEICS NFTDKLYPEF SLNSLQCLKL KKPIRAKIHS
IMSSQLNKME DFPRGTLLYS FIIASNNRLC NVLRPKSHTL HPVDLQILFL VIATQFHNLE
SDKELWIPIC FPKFNSNGYL YCYIRTIMNP GDKSSSKFLG HPPVLVAISG QKDAFFKMKS
YCDELMVILT RNNEIIRELR TSILQPYSIT DIPAPLVHHF IFKSSKHIQF TMPQLSTSAS
EPEQRALYER KLKFYYKSLQ NSIAQEIASQ SNKSLVNFVQ WSEPAKSNSE ETTDHDSFIE
EPVNMLGMVW CSPRFELLLL FNNGIVTRKQ ALSSARRIVR WCVSNESSLF INEGATF
