ID A0A165I4E3_XYLHT Unreviewed; 685 AA.
AC A0A165I4E3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Vacuolar fusion protein MON1 {ECO:0000256|ARBA:ARBA00018132, ECO:0000256|RuleBase:RU367048};
GN ORFNames=L228DRAFT_281447 {ECO:0000313|EMBL:KZF24365.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF24365.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF24365.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF24365.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV407456; KZF24365.1; -; Genomic_DNA.
DR RefSeq; XP_018189920.1; XM_018335888.1.
DR AlphaFoldDB; A0A165I4E3; -.
DR STRING; 1328760.A0A165I4E3; -.
DR GeneID; 28901025; -.
DR InParanoid; A0A165I4E3; -.
DR OMA; EYSAKEP; -.
DR OrthoDB; 73361at2759; -.
DR Proteomes; UP000076632; 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:UP000076632};
KW Transport {ECO:0000256|RuleBase:RU367048};
KW Vacuole {ECO:0000256|RuleBase:RU367048}.
FT DOMAIN 262..384
FT /note="FUZ/MON1/HPS1 first Longin"
FT /evidence="ECO:0000259|Pfam:PF19036"
FT DOMAIN 424..543
FT /note="FUZ/MON1/HPS1 second Longin"
FT /evidence="ECO:0000259|Pfam:PF19037"
FT DOMAIN 575..674
FT /note="FUZ/MON1/HPS1 third Longin"
FT /evidence="ECO:0000259|Pfam:PF19038"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 75369 MW; FBEE682A93CA1162 CRC64;
MEESKESQKE SGQAGNGQPS PESSKPRTPE QEARIPGNGG NGSSGTNVEG REEAQDNALV
AETISRTVHS KDSSEIDRES SAETPPPLPP RPVNLESTDA QNTLHLSGKQ ARPKLQSHPT
TAVSLTDIST QVNNEGIRET YPSTTGGLTS PLSVASQFNN RFGSPKSSET EDTASIKSYV
PTLETGGDVE SLLGEVLGNG QQDPAWRFMT AQGENQNAAD ELLPEDAAFE KDFQKEFKEL
EAINAEGTNE EAVLDAWTSR MKHFLILSAA GKPIYSRHGD DNITSGYIGI IQTIISFYQN
ADDTLKSFTA GDVKFVVLSK TSLYLVAISR LGESDGQLRA QLEALYMQIL STLTLPRLQT
IFSNRPSSDL RRPLSGTEPL LSALADTFTR GSPPTLLSAL ECLRLRKSHR QVIDQTLLKT
RTENLLYGLI VAGGRLVSVV RPKKHSLHPS DLQLIFNMLF ETEGVKTAGG ENWIPLCLPG
FNNTGFLYMY VSFLSAKEDE NEDESQRPST SSSFNKEEEV AVLLISPKKE SFYEMQQMRD
DVVEQLQKNG SMDLIKAAVR RGRPHVTDVV PGTVLRHFLY KSKANVQFAM PSFEPHFKGL
VARRKLLSIY HTLHANVHSK ISHLKVHYCV SRDSISLAWT TPLFELYCVA GPSASRGALA
QSANKVVQWA RKEEERIFII GGAVF
//
