ID M7T4Z6_EUTLA Unreviewed; 623 AA.
AC M7T4Z6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Vacuolar fusion protein MON1 {ECO:0000256|ARBA:ARBA00018132, ECO:0000256|RuleBase:RU367048};
GN ORFNames=UCREL1_11363 {ECO:0000313|EMBL:EMR61695.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR61695.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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}.
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DR EMBL; KB707568; EMR61695.1; -; Genomic_DNA.
DR RefSeq; XP_007799198.1; XM_007801007.1.
DR AlphaFoldDB; M7T4Z6; -.
DR STRING; 1287681.M7T4Z6; -.
DR KEGG; ela:UCREL1_11363; -.
DR eggNOG; KOG0997; Eukaryota.
DR HOGENOM; CLU_014574_5_0_1; -.
DR OMA; IHNSSRP; -.
DR OrthoDB; 73361at2759; -.
DR Proteomes; UP000012174; 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 Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Transport {ECO:0000256|RuleBase:RU367048};
KW Vacuole {ECO:0000256|RuleBase:RU367048}.
FT DOMAIN 199..321
FT /note="FUZ/MON1/HPS1 first Longin"
FT /evidence="ECO:0000259|Pfam:PF19036"
FT DOMAIN 361..480
FT /note="FUZ/MON1/HPS1 second Longin"
FT /evidence="ECO:0000259|Pfam:PF19037"
FT DOMAIN 512..612
FT /note="FUZ/MON1/HPS1 third Longin"
FT /evidence="ECO:0000259|Pfam:PF19038"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 68813 MW; 11DDAA160880D0FC CRC64;
MGSEDAGSSS SSVAQRDEQP PPLPPRPSQP ATAASVERER GRPQLQSKPT TALSSMNIQT
LSFPDGSRGT FSTSDDNAAA DASDAGQQVD ISPDRATRRR GFSTIGSDRD ESMSVMSFAP
TLRPPGDLES LLVGDMSKRS PAWALLHAQS SDVQPFETVE VSKISALVDF DREFDDIPDT
SEKDWNDEDR VRVWKSKLKH FMVLSSAGKP IYSRHGDLSL INSSMGVVQT IISFYEGAKN
PLLGFTAGDT RFVITTQGPL YFVAISRLGE SDSQLRAQLD ALYMQILSTL TLPTLTNIFA
NRPSTDLRKP LQGTESLLSS LADSFTKGSP SSLLGALECL KLRKSQRHSI NNAFLKAKSE
KLLYGMIAAG GRLVSVIRPR RHSLHPSDLQ LIFNMLFESG GIKAAGGENW IPICLPAFNN
RGYLYMYVSF LNDHDHDHDH AESPTTPEDS RSTEEQIAII LISTDKEGFF TLQQMRDDVV
TELKRKKHLD IIQEAARRGR PAVHEIAPGA AISHFLFKSK ANVQFCMPSL HPAFDNDMIR
HRRLMSLYQN LHATVHAKHS HLKVLNCVGE DSTSLAWVTP IFEFYCVSGP NTPRAVMAQG
ANKIIQWAKR EEERLFIIGG GVF
//
