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Database: UniProt
Entry: A0A2J8BWR6_VERDA
LinkDB: A0A2J8BWR6_VERDA
Original site: A0A2J8BWR6_VERDA 
ID   A0A2J8BWR6_VERDA        Unreviewed;       598 AA.
AC   A0A2J8BWR6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Vacuolar fusion protein MON1 {ECO:0000256|ARBA:ARBA00018132, ECO:0000256|RuleBase:RU367048};
GN   ORFNames=BJF96_g7517 {ECO:0000313|EMBL:PNH29211.1};
OS   Verticillium dahliae (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=27337 {ECO:0000313|EMBL:PNH29211.1, ECO:0000313|Proteomes:UP000236305};
RN   [1] {ECO:0000313|EMBL:PNH29211.1, ECO:0000313|Proteomes:UP000236305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12008 {ECO:0000313|EMBL:PNH29211.1,
RC   ECO:0000313|Proteomes:UP000236305};
RA   Fan R., Armitage A.D., Cascant-Lopez E., Sobczyk M., Cockerton H.M.,
RA   Harrison R.J.;
RT   "Comparative genomics yields insights into virulence evolution of
RT   Verticillium dahliae.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 MON1-CCZ1 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:0000256|ARBA:ARBA00043892}.
CC   -!- FUNCTION: Required for multiple vacuole delivery pathways including the
CC       cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and
CC       endocytosis. {ECO:0000256|RuleBase:RU367048}.
CC   -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC       {ECO:0000256|RuleBase:RU367048}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU367048}. Prevacuolar compartment membrane
CC       {ECO:0000256|ARBA:ARBA00004380, ECO:0000256|RuleBase:RU367048};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004380,
CC       ECO:0000256|RuleBase:RU367048}. Vacuole membrane
CC       {ECO:0000256|RuleBase:RU367048}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU367048}.
CC   -!- SIMILARITY: Belongs to the MON1/SAND family.
CC       {ECO:0000256|RuleBase:RU367048}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNH29211.1}.
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DR   EMBL; MPSH01000028; PNH29211.1; -; Genomic_DNA.
DR   Proteomes; UP000236305; Unassembled WGS sequence.
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-UniRule.
DR   GO; GO:0006623; P:protein targeting to vacuole; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; SAND PROTEIN-RELATED; 1.
DR   PANTHER; PTHR13027:SF7; VACUOLAR FUSION PROTEIN MON1 HOMOLOG; 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 {ECO:0000256|RuleBase:RU367048};
KW   Endosome {ECO:0000256|RuleBase:RU367048};
KW   Membrane {ECO:0000256|RuleBase:RU367048};
KW   Protein transport {ECO:0000256|RuleBase:RU367048};
KW   Transport {ECO:0000256|RuleBase:RU367048};
KW   Vacuole {ECO:0000256|RuleBase:RU367048}.
SQ   SEQUENCE   598 AA;  64825 MW;  07E1A5CEF242A4C0 CRC64;
     MGEDPKTQSG DSQEQRPPLP PRPVAFTSAS IDSKLATTAI TPVDIQTLSF PDGTRGTFST
     PGAQNASTPP GSSISGSATP RHDLGEMEDS MSIMSLAPTM RPAGDIASLL TGDFNRRSPA
     WNLLRSQSPA VLPFETLNLD TATHRLAGFE HEFDPLPDDS SPDVKDEDRL ELWKSKLKQF
     MILSSAGKPI WSRHGDLGLI NSYMGIIQTI ISFYQGANNP LTGFTAGDTR FVIATEGPLY
     FVATSRLGES DSQLRGQLEA LYMQILSTLT LPTLRNIFVN RPSTDLRKPL QGTESLLSSL
     ADHFTKGSAS ALLGALECLR LRKSQRHAIN NAFLKQRTDK LLYGLIVADG KLVSVIRPRR
     HSLHPSDLKL IFNMLFESGG ISAGGGENWV PLCLPAFNNN GYLYMYVSFI DGPPSSDASS
     QPADASPASG GQTAIILVSP DKESFFELKQ MRDAVVASLE KNGLLAIIRA AASAGRPAIP
     AIAAGSQVSH FLYKSRANVQ FSMSALDPVF ASPIARRRLM TLYHQLHASV HAKHSAMRVL
     HCVSDEATSL AWVTPIFEFY CVAGPNVSRA TITQGANKII QWAKREEERI FIIGGGVF
//
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