ID A0A074YYY8_AURSE Unreviewed; 652 AA.
AC A0A074YYY8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Vacuolar fusion protein MON1 {ECO:0000256|ARBA:ARBA00018132, ECO:0000256|RuleBase:RU367048};
GN ORFNames=AUEXF2481DRAFT_43452 {ECO:0000313|EMBL:KEQ92046.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ92046.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ92046.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ92046.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584773; KEQ92046.1; -; Genomic_DNA.
DR RefSeq; XP_013340521.1; XM_013485067.1.
DR AlphaFoldDB; A0A074YYY8; -.
DR STRING; 1043005.A0A074YYY8; -.
DR GeneID; 25367417; -.
DR HOGENOM; CLU_014574_5_0_1; -.
DR InParanoid; A0A074YYY8; -.
DR OMA; IHNSSRP; -.
DR OrthoDB; 73361at2759; -.
DR Proteomes; UP000030641; 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:UP000030641};
KW Transport {ECO:0000256|RuleBase:RU367048};
KW Vacuole {ECO:0000256|RuleBase:RU367048}.
FT DOMAIN 229..350
FT /note="FUZ/MON1/HPS1 first Longin"
FT /evidence="ECO:0000259|Pfam:PF19036"
FT DOMAIN 391..509
FT /note="FUZ/MON1/HPS1 second Longin"
FT /evidence="ECO:0000259|Pfam:PF19037"
FT DOMAIN 542..641
FT /note="FUZ/MON1/HPS1 third Longin"
FT /evidence="ECO:0000259|Pfam:PF19038"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 72498 MW; 18EBF4477AF6EEC5 CRC64;
MPDEHDQSSP GAAVIADQAA LDQTTSQTRT TSPGPKDKQH GEEVMEDSRE IRPPLPPRPT
NLDLLEERGS GGSIRLPKRM ASRPNLQARP TTAVSLTDVH TSNNFQDHAS RTLSPPSRPV
SRKQSTANMD RFRSRVGSDA AETSSVRSYA NTLGTNAEME SLLGDPFPTS PAWKSLSAQL
EKENPMDHVF DEDDIFSLRM HHEFDELEEF RANGTNEEFL MNSWTSKLKH FFILSSAGKP
IWSRHGDDQV IANHIGILQT LISFYQDVND NLRGFTAGNA RFVILSKGHL NLAAISRLGE
SDLQLKTQLE SLYMQILSTL TLPSMERMFS NRPSTDLRRP LQGTEVLLGA LADGFTRGSL
PTLLSALECL KIRKSHRQVI NNTLLKVKSP NLLYGLLVAG GRLVSVVRPR KHSLHPGDLQ
LIFNMLFEAG SVKAGGGENW IPLCLPGFNN TGFLYMYVSF LDIGEDHAKV SEERPQPSAS
PRDDDQLAII LISADKEAFY ELRQMRDDLI DQLNQNNSMS ILRTAIHHGR PSIPSILPSS
PLLHFIYKSR PHVQFFTPSF SPNFTSLVPH RRLVSLYSSL HTAVHNKTAS LKVHYACAKD
AVALGWVGRE YEFYGVAGAG ASREGMAKAA QDVVRYLRRE EERVFIIGGA VF
//
