ID A1DFS0_NEOFI Unreviewed; 560 AA.
AC A1DFS0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Vacuolar fusion protein MON1 {ECO:0000256|ARBA:ARBA00018132, ECO:0000256|RuleBase:RU367048};
GN ORFNames=NFIA_081730 {ECO:0000313|EMBL:EAW18227.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW18227.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW18227.1; -; Genomic_DNA.
DR RefSeq; XP_001260124.1; XM_001260123.1.
DR AlphaFoldDB; A1DFS0; -.
DR STRING; 331117.A1DFS0; -.
DR EnsemblFungi; EAW18227; EAW18227; NFIA_081730.
DR GeneID; 4586680; -.
DR KEGG; nfi:NFIA_081730; -.
DR VEuPathDB; FungiDB:NFIA_081730; -.
DR eggNOG; KOG0997; Eukaryota.
DR HOGENOM; CLU_014574_5_0_1; -.
DR OMA; EYSAKEP; -.
DR OrthoDB; 73361at2759; -.
DR Proteomes; UP000006702; 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|ARBA:ARBA00022753, ECO:0000256|RuleBase:RU367048};
KW Membrane {ECO:0000256|RuleBase:RU367048};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU367048};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Transport {ECO:0000256|RuleBase:RU367048};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554, ECO:0000256|RuleBase:RU367048}.
FT DOMAIN 216..338
FT /note="FUZ/MON1/HPS1 first Longin"
FT /evidence="ECO:0000259|Pfam:PF19036"
FT DOMAIN 378..491
FT /note="FUZ/MON1/HPS1 second Longin"
FT /evidence="ECO:0000259|Pfam:PF19037"
FT DOMAIN 523..554
FT /note="FUZ/MON1/HPS1 third Longin"
FT /evidence="ECO:0000259|Pfam:PF19038"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 60922 MW; B103669E1203AE38 CRC64;
MNSNALEQPQ VSPGDDGAGG NNYGTPEYSA KEPSNTGSDD SSARLEERPP PLPPRPNTLS
LLDEGFISSR STRQSSSASL QAKATTAVSI PDISLLQLND GGKENHPTRG PFGALRAKAS
LTQLTASRGS DAGDSASIRS TAPNTELGEA ENVFSDFLAQ ESGDFQQDSS GLLQFPEFRA
DDVEDDFTSE FEPIGELDDE GRNEELLLEK WKSKRKHYLI LSAAGKPIWT RHGDGGLISG
YIGVIQTIIS FYEDANDRLS SFCAGNTKFV IVTKGPLYLV AISRLLESDT QLKLQLEALY
MQILSTLTLP SLTHLFSVRP STDLKRPLQG SETLLSTLAD SFTKGSPSTF LSALECLKIR
KSHRQAINNA LLKTKVSSLL YGLVVAGGRL VSVVRPKKHS LHPGDLQLLF NMIFEAEGIK
AGGGESWIPV CLPGFNSSGY LYMYVSFLDL RENSGNTASE TTTTEQSVAI ILISPNKEGF
FEMQEMRNSL VEQLEKNNSI NIIKEAIDGG RPTTTDIVPG TVLHHFLYKS RANVQFTMSS
YDPEFTSISR RRSLGASSSD
//
