MON1_YEAST
ID MON1_YEAST Reviewed; 644 AA.
AC P53129; D6VU24;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Vacuolar fusion protein MON1;
DE AltName: Full=Autophagy-related protein 12;
DE AltName: Full=Monensin sensitivity protein 1;
GN Name=MON1; Synonyms=AUT12; OrderedLocusNames=YGL124C; ORFNames=G2889;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896269;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1047::aid-yea991>3.0.co;2-n;
RA Tizon B., Rodriguez-Torres A.M., Rodriguez-Belmonte E., Cadahia J.L.,
RA Cerdan E.;
RT "Identification of a putative methylenetetrahydrofolate reductase by
RT sequence analysis of a 6.8 kb DNA fragment of yeast chromosome VII.";
RL Yeast 12:1047-1051(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 113.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12387888; DOI=10.1016/s0014-5793(02)03456-7;
RA Meiling-Wesse K., Barth H., Voss C., Barmark G., Muren E., Ronne H.,
RA Thumm M.;
RT "Yeast Mon1p/Aut12p functions in vacuolar fusion of autophagosomes and cvt-
RT vesicles.";
RL FEBS Lett. 530:174-180(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCZ1.
RX PubMed=12364329; DOI=10.1074/jbc.m208191200;
RA Wang C.-W., Stromhaug P.E., Shima J., Klionsky D.J.;
RT "The Ccz1-Mon1 protein complex is required for the late step of multiple
RT vacuole delivery pathways.";
RL J. Biol. Chem. 277:47917-47927(2002).
RN [6]
RP FUNCTION.
RX PubMed=12134085; DOI=10.1091/mbc.02-01-0005;
RA Bonangelino C.J., Chavez E.M., Bonifacino J.S.;
RT "Genomic screen for vacuolar protein sorting genes in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:2486-2501(2002).
RN [7]
RP FUNCTION OF THE CCZ1-MON1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=14662743; DOI=10.1083/jcb.200308071;
RA Wang C.-W., Stromhaug P.E., Kauffman E.J., Weisman L.S., Klionsky D.J.;
RT "Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the
RT tethering/docking stage.";
RL J. Cell Biol. 163:973-985(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP FUNCTION.
RX PubMed=15721293; DOI=10.1016/j.bbrc.2005.01.107;
RA Hoffman-Sommer M., Migdalski A., Rytka J., Kucharczyk R.;
RT "Multiple functions of the vacuolar sorting protein Ccz1p in Saccharomyces
RT cerevisiae.";
RL Biochem. Biophys. Res. Commun. 329:197-204(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-71, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP FUNCTION.
RX PubMed=20797862; DOI=10.1016/j.cub.2010.08.002;
RA Nordmann M., Cabrera M., Perz A., Broecker C., Ostrowicz C.,
RA Engelbrecht-Vandre S., Ungermann C.;
RT "The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog
RT Ypt7.";
RL Curr. Biol. 20:1654-1659(2010).
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 CCZ1-MON1 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 (PubMed:12134085, PubMed:12364329, PubMed:12387888, PubMed:14662743,
CC PubMed:15721293). The CCZ1-MON1 complex acts as a guanine nucleotide-
CC exchange factor (GEF) for Rab-type GTPase YPT7, promoting nucleotide
CC exchange on YPT7 and triggering endosomal maturation by activating YPT7
CC on late endosomes (PubMed:20797862). {ECO:0000269|PubMed:12134085,
CC ECO:0000269|PubMed:12364329, ECO:0000269|PubMed:12387888,
CC ECO:0000269|PubMed:14662743, ECO:0000269|PubMed:15721293,
CC ECO:0000269|PubMed:20797862}.
CC -!- SUBUNIT: Forms a complex with CCZ1.
CC -!- INTERACTION:
CC P53129; P38273: CCZ1; NbExp=4; IntAct=EBI-23945, EBI-21608;
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000305|PubMed:12387888}; Peripheral membrane protein. Prevacuolar
CC compartment membrane {ECO:0000269|PubMed:12364329}; Peripheral membrane
CC protein. Vacuole membrane {ECO:0000269|PubMed:12364329,
CC ECO:0000269|PubMed:14662743}; Peripheral membrane protein. Note=The
CC association of the CCZ1-MON1 complex with the vacuole is regulated by
CC the C-Vps/HOPS complex. {ECO:0000269|PubMed:14662743}.
CC -!- SIMILARITY: Belongs to the MON1/SAND family. {ECO:0000305}.
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DR EMBL; X94106; CAA63834.1; -; Genomic_DNA.
DR EMBL; Z72646; CAA96832.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07985.2; -; Genomic_DNA.
DR PIR; S64135; S64135.
DR RefSeq; NP_011391.2; NM_001180989.2.
DR AlphaFoldDB; P53129; -.
DR SMR; P53129; -.
DR BioGRID; 33127; 438.
DR ComplexPortal; CPX-1674; MON1-CCZ1 complex.
DR DIP; DIP-5483N; -.
DR IntAct; P53129; 4.
DR MINT; P53129; -.
DR STRING; 4932.YGL124C; -.
DR iPTMnet; P53129; -.
DR MaxQB; P53129; -.
DR PaxDb; P53129; -.
DR PRIDE; P53129; -.
DR EnsemblFungi; YGL124C_mRNA; YGL124C; YGL124C.
DR GeneID; 852753; -.
DR KEGG; sce:YGL124C; -.
DR SGD; S000003092; MON1.
DR VEuPathDB; FungiDB:YGL124C; -.
DR eggNOG; KOG0997; Eukaryota.
DR GeneTree; ENSGT00390000006665; -.
DR HOGENOM; CLU_014574_0_0_1; -.
DR InParanoid; P53129; -.
DR OMA; TNSTCEY; -.
DR BioCyc; YEAST:G3O-30621-MON; -.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P53129; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53129; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0035658; C:Mon1-Ccz1 complex; IDA:SGD.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:SGD.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:SGD.
DR GO; GO:0097352; P:autophagosome maturation; IC:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IMP:ComplexPortal.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:SGD.
DR GO; GO:0044395; P:protein targeting to vacuolar membrane; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; HMP:SGD.
DR GO; GO:0048278; P:vesicle docking; IMP:SGD.
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 1: Evidence at protein level;
KW Autophagy; Endosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Vacuole.
FT CHAIN 1..644
FT /note="Vacuolar fusion protein MON1"
FT /id="PRO_0000202744"
FT REGION 64..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 113
FT /note="S -> C (in Ref. 1; CAA63834 and 2; CAA96832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 73478 MW; B5F36B87346C97F3 CRC64;
MNLNESYLDA EIPKGQLKHS KSGNFEGIPI VATTSEPTTS VNLDETFFKK APIAMPICDD
HSVSKSTSVN SLNTTSLASR RSPLQTKKLQ AKNNLLSADL AKSNDDTTRA LNSPKKDFGP
YLDSENDIRS RLAESIYSME TSIRGSELQR RPYVSNEIPN VFKFSKFNSN CKLNESQTLC
DKNFFIFTSA GKPIYCMHGK DEQIMSYTGL VNTVISYFQV NGPSELKTIS TLTSGKRLTF
LDKSPILLMA QSERGESSNE LLNQLDFLYS YILSSLSERQ LLRLFSKREN FDLRNYLEST
DFENLDEICS LICNRMFPDL LLNSLQCLPF NHSSRLKLQN VVLQQLEKRQ DIPRGTLLYG
LIIAPQNKLC CVLRPRGHTL HTTDLHLLFC LISHQFQNLD ETQELWVPIC FPKFNSSGFL
YCYIKFLPND THSNEKSALV LISAQKDAFF SLKSFSDELI IKLEEEKLLK KINTSKGFKL
SDIPAPMVHH FIYKSKQNVQ YVMPHFEVNS NIALDSSQGL EYELKLKTYY QQLHGTVVRD
NGNLLSRSML NFVRWSSKDN EDLAMDETQM DFSELDEYII GNSSFKQESV NMVGMAWVTP
TFELYLIGNN GIVDKRVLFK SARKVANWCQ KHESRLFISD GAVF
