MON1_CHAGB
ID MON1_CHAGB Reviewed; 656 AA.
AC Q2HFQ4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Vacuolar fusion protein MON1;
GN Name=MON1; ORFNames=CHGG_00950;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- FUNCTION: Required for multiple vacuole delivery pathways including the
CC cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and
CC endocytosis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Prevacuolar
CC compartment membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Vacuole membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MON1/SAND family. {ECO:0000305}.
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DR EMBL; CH408029; EAQ92715.1; -; Genomic_DNA.
DR RefSeq; XP_001220171.1; XM_001220170.1.
DR AlphaFoldDB; Q2HFQ4; -.
DR SMR; Q2HFQ4; -.
DR STRING; 38033.XP_001220171.1; -.
DR EnsemblFungi; EAQ92715; EAQ92715; CHGG_00950.
DR GeneID; 4387539; -.
DR eggNOG; KOG0997; Eukaryota.
DR HOGENOM; CLU_014574_5_0_1; -.
DR InParanoid; Q2HFQ4; -.
DR OMA; TNSTCEY; -.
DR OrthoDB; 829786at2759; -.
DR Proteomes; UP000001056; 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-KW.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
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; PTHR13027; 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; Endosome; Membrane; Protein transport; Reference proteome;
KW Transport; Vacuole.
FT CHAIN 1..656
FT /note="Vacuolar fusion protein MON1"
FT /id="PRO_0000278858"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 71214 MW; 18736B74D1984D7E CRC64;
MARETEVESS HDGPPKVTET SPSPSPSPPP PPLPPRQMIS SDSPAQVAPA QAKPTTAVSS
IDISTVSFPD GSRGTFSTSA PRVGFTPHTN ASGYGTPGRD ATGGDLADSM SVMSFAPTLR
PHGDLASLVA DGLNKKSRAW NMLRSQSETV QPFESIELGA PGSLAGFERE FDEIPDDKTD
DIRMAIWKSK MKHYMILSSA GKPIYSRHGD LGLVNSYMGV VQTIISFYEG ANNPLLGFTA
GNARFVIAIE GPLYFVAISR LNESDAQLRS QLEALYMQIL STLTLPTLKS IFVHRPSTDL
RKPLEGTESL LSSLADSFTR GSPSTLLGAL ECLKLRKSQR HAINNVFLKN RSEKLLYGLV
VAGGKLVSVI RPRKHSLHPS DLQLIFNMLF ESGGIKSGGG ESWIPLCLPA FNNRGYLYMY
VSFFDGNADP AFSAESTAED TPESSTDTNT TNTTEKEDEI ALILISPDKE SFYDLKEMRD
KLAAQLTKTG HLSLIRSAAR ERRPQIQTIA PGAQIAHFLY KSRANVQFCM SALEPANPNP
TPGTSSTTPT TVATTATVAS TSTSTLEPEK MLTRRRLMTL YHELHASMHA KHAHLKVLHA
VSEDAASLAW ITPVFEFYCV AGPNAPRAAM AQGANRVIQW AKREEERLFI IGGGVF