ID G1XGC8_ARTOA Unreviewed; 708 AA.
AC G1XGC8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, 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=AOL_s00083g59 {ECO:0000313|EMBL:EGX47551.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX47551.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX47551.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX47551.1}.
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DR EMBL; ADOT01000151; EGX47551.1; -; Genomic_DNA.
DR RefSeq; XP_011123540.1; XM_011125238.1.
DR AlphaFoldDB; G1XGC8; -.
DR STRING; 756982.G1XGC8; -.
DR GeneID; 22894938; -.
DR eggNOG; KOG0997; Eukaryota.
DR HOGENOM; CLU_014574_5_0_1; -.
DR InParanoid; G1XGC8; -.
DR OMA; QITEDYF; -.
DR OrthoDB; 73361at2759; -.
DR Proteomes; UP000008784; 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:UP000008784};
KW Transport {ECO:0000256|RuleBase:RU367048};
KW Vacuole {ECO:0000256|RuleBase:RU367048}.
FT DOMAIN 308..430
FT /note="FUZ/MON1/HPS1 first Longin"
FT /evidence="ECO:0000259|Pfam:PF19036"
FT DOMAIN 470..566
FT /note="FUZ/MON1/HPS1 second Longin"
FT /evidence="ECO:0000259|Pfam:PF19037"
FT DOMAIN 598..697
FT /note="FUZ/MON1/HPS1 third Longin"
FT /evidence="ECO:0000259|Pfam:PF19038"
FT REGION 37..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 77552 MW; 8EDDCC86C8BFF49D CRC64;
MDLYSKTINL VVTPLRDISD TVNSTISNSA ERTWNLVKRD GGDGGKSSAS TVEGSSGDTA
DMAETSEAAK PLATSNEGGT AGDTESSTSE IPGDETGAEA ITSASRGISL TAEPEAVDEA
DQDDTRTPRP QSPSNPPAAE AAASSSEHIQ ITEDYFARPP HLDLSGASTL RGADNGMLGP
GSCPVTPSLE RLQSKPTTAL SLSQVHANNG ITSSGVSVIL PYTESSSIRS LVPTIDSGDN
DVAGMLGEIL NEDNVAFTSG YNQGWALSQQ VEEEEELVED SDEDWDESDN EEELTEDERI
EKWRSRKKHF FILSSAGKPV YSRYGDEAVV SQFMGVIQTI ISFFQEGSDP LKSFSAGKHR
FTILQEGHLY LVGVSSLGET DIQLRTQLDM LYTQVLSTLT LTTVAKVFGE RENFDLRRLL
GGTEVFLDGL SDAMVRGEPN ILLGSLECVK MRKHIREKIN SVLMKCRTNN LLYGLIIADG
RLVSVIRPKR HSLHPPDLQL FISMLFSAST FKGGGEHWTP ICLPKFNAKG FLHAYICFFQ
PEIALVLISP TREAFFDMKE VKDNIIEQLD RAGSIPIIEG AVKRGRYLAS DLIEGTVIQH
FLYKSKANVQ FTMPSFDPHF SSPHARRRLM ILYQRLHAAV HARGAHLKVH HSIRRRSVSL
AWVTPTFELY CVAGAGTPRN VLAKHANMIV GWVKKEEERL FIVGGATF
//
