MON2_YEAST
ID MON2_YEAST Reviewed; 1636 AA.
AC P48563; D6W0P7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein MON2;
GN Name=MON2; Synonyms=YSL2; OrderedLocusNames=YNL297C; ORFNames=N0453;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553702; DOI=10.1002/yea.320111311;
RA Maurer K.C.T., Urbanus J.H.M., Planta R.J.;
RT "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV
RT carrying a ribosomal protein gene cluster, the genes encoding a plasma
RT membrane protein and a subunit of replication factor C, and a novel
RT putative serine/threonine protein kinase gene.";
RL Yeast 11:1303-1310(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
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, SUBCELLULAR LOCATION, AND INTERACTION WITH ARL1.
RX PubMed=12052896; DOI=10.1128/mcb.22.13.4914-4928.2002;
RA Jochum A., Jackson D., Schwarz H., Pipkorn R., Singer-Krueger B.;
RT "Yeast Ysl2p, homologous to Sec7 domain guanine nucleotide exchange
RT factors, functions in endocytosis and maintenance of vacuole integrity and
RT interacts with the Arf-Like small GTPase Arl1p.";
RL Mol. Cell. Biol. 22:4914-4928(2002).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION, AND 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 INTERACTION WITH NEO1.
RX PubMed=15314152; DOI=10.1128/mcb.24.17.7402-7418.2004;
RA Wicky S., Schwarz H., Singer-Krueger B.;
RT "Molecular interactions of yeast Neo1p, an essential member of the Drs2
RT family of aminophospholipid translocases, and its role in membrane
RT trafficking within the endomembrane system.";
RL Mol. Cell. Biol. 24:7402-7418(2004).
RN [8]
RP SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH DOP1, AND FUNCTION.
RX PubMed=16219684; DOI=10.1242/jcs.02599;
RA Efe J.A., Plattner F., Hulo N., Kressler D., Emr S.D., Deloche O.;
RT "Yeast Mon2p is a highly conserved protein that functions in the cytoplasm-
RT to-vacuole transport pathway and is required for Golgi homeostasis.";
RL J. Cell Sci. 118:4751-4764(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP INTERACTION WITH DOP1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16301316; DOI=10.1074/jbc.m510176200;
RA Gillingham A.K., Whyte J.R.C., Panic B., Munro S.;
RT "Mon2, a relative of large Arf exchange factors, recruits Dop1 to the Golgi
RT apparatus.";
RL J. Biol. Chem. 281:2273-2280(2006).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564; SER-567 AND SER-571, 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for traffic between late Golgi and early endosomes.
CC Required for endocytosis and maintenance of vacuolar structure.
CC {ECO:0000269|PubMed:12052896, ECO:0000269|PubMed:12134085,
CC ECO:0000269|PubMed:16219684, ECO:0000269|PubMed:16301316}.
CC -!- SUBUNIT: Homodimer. Interacts with DOP1, ARL1 and NEO1.
CC {ECO:0000269|PubMed:12052896, ECO:0000269|PubMed:15314152,
CC ECO:0000269|PubMed:16219684, ECO:0000269|PubMed:16301316}.
CC -!- INTERACTION:
CC P48563; Q03921: DOP1; NbExp=5; IntAct=EBI-28333, EBI-34442;
CC P48563; P38817: GGA2; NbExp=3; IntAct=EBI-28333, EBI-7569;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12052896, ECO:0000269|PubMed:16219684,
CC ECO:0000269|PubMed:16301316}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12052896, ECO:0000269|PubMed:16219684,
CC ECO:0000269|PubMed:16301316}. Note=Late Golgi.
CC -!- MISCELLANEOUS: Present with 2410 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MON2 family. {ECO:0000305}.
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DR EMBL; U23084; AAC49101.1; -; Genomic_DNA.
DR EMBL; Z71573; CAA96214.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10263.1; -; Genomic_DNA.
DR PIR; S60403; S60403.
DR RefSeq; NP_014102.1; NM_001183135.1.
DR AlphaFoldDB; P48563; -.
DR SMR; P48563; -.
DR BioGRID; 35541; 449.
DR ComplexPortal; CPX-1028; NEO1-MON2-ARL1-DOP1 membrane remodeling complex.
DR IntAct; P48563; 8.
DR MINT; P48563; -.
DR STRING; 4932.YNL297C; -.
DR iPTMnet; P48563; -.
DR MaxQB; P48563; -.
DR PaxDb; P48563; -.
DR PRIDE; P48563; -.
DR EnsemblFungi; YNL297C_mRNA; YNL297C; YNL297C.
DR GeneID; 855420; -.
DR KEGG; sce:YNL297C; -.
DR SGD; S000005241; MON2.
DR VEuPathDB; FungiDB:YNL297C; -.
DR eggNOG; KOG1848; Eukaryota.
DR GeneTree; ENSGT00940000174858; -.
DR HOGENOM; CLU_001169_1_0_1; -.
DR InParanoid; P48563; -.
DR OMA; DETIDCQ; -.
DR BioCyc; YEAST:G3O-33285-MON; -.
DR PRO; PR:P48563; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P48563; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0006895; P:Golgi to endosome transport; IMP:HGNC-UCL.
DR GO; GO:0006623; P:protein targeting to vacuole; IDA:SGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
DR GO; GO:0098629; P:trans-Golgi network membrane organization; IC:ComplexPortal.
DR InterPro; IPR032629; DCB_dom.
DR InterPro; IPR026829; Mon2-like.
DR InterPro; IPR032817; Mon2_C.
DR InterPro; IPR032691; Sec7_N.
DR PANTHER; PTHR10663:SF333; PTHR10663:SF333; 1.
DR Pfam; PF16213; DCB; 1.
DR Pfam; PF16206; Mon2_C; 1.
DR Pfam; PF12783; Sec7_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1636
FT /note="Protein MON2"
FT /id="PRO_0000203372"
FT REGION 60..410
FT /note="Golgi membrane targeting and interaction with ARL1"
FT /evidence="ECO:0000269|PubMed:12052896"
FT REGION 547..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1636
FT /note="Required for function in membrane trafficking"
FT COMPBIAS 547..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1636 AA; 186836 MW; F0B3D8E6B0D994D6 CRC64;
MAMNTGGFDS MQRQLEAELR SLSSESKRRN STIRHASDKS IEILKRVHSF EELERHPDFA
LPFVLACQSR NAKMTTLAMQ CLQGLSTVPS IPRSRLSEIL DAFIEATHLA MEIQLKVLQV
VPIFFKTYGK FIYGPLCKKL LLCCSNLLHV PNKAPVVVGT ASATLQQLID EIFDRLSIES
VVDDKQYEVL ISNSESIKVN VYRYDANKLF DNICSLNEIS SNGAVSDEEM LLDIGDIPID
YGLEILESIL KNSQKNLLEC QDLQYLLRVK AIPLLLRCIS SSRHFSTAVR SCRCLKLLIR
KEYLSILELE LEVILSLLIH GISVESNLSG WQRVLSLELF KDLSQDPEIV NTLYMDYDNY
PDKKHVFKYL LKECIVLLNS PEYITFLAPS KVVEKMDSPL ITTENSTVKT KFMHLLDKSN
APSINITYII SLILTICNHL CEGLNKSALE SSPLEKKIED KEREEGTGND STVVKVYSGL
FSGLFELNKL FLYSTSLETS IFHLVVRAFQ KLAHSAGVLS LKDKLRACMK LFSILITNNV
TSSNQYSFND TSKSAKNQHT RNISTSSVTT SPVESTKNPS RSIADSAQNK EMKRRLHPRN
ISSRQVSLLR ALISLSISLG PIFDSESWRY TFLTWQWITY YIYGPSADFK ESFYSEDIPP
PPILTKSDVT SIESSLTKFF ESTSSYSCST FHLVLTRLIL DSKNTLTLEQ TNLNLNNDIG
YHPLDAKDEI IPCIYNKAFF VNKIGELATY NCKKFLFGKN GKELWSLIST YMIKLISNRE
MDNDSLRLYT VRVFTDIIKK ATNEVGNSDE QDNKVKQFGT LENLVIDSLM ATINSIKQLD
IGKQEIYNGT INVESDILFQ LLLTLKEILN EFGELLMNSW TNIFNIINSP FEWTVEDTDF
SVNEDIDDSS LFEGIVQKHK NMIQVSYDVF KLISDDFLQS LPMSVIKFVI DTLVNFVSQK
RNLNISFSSI SQFWLVGDYL RVRFNPETLN LSDEKRRSLS EKINNQKLIE IITSSSSHDW
ELYNGLWIYL LKNLINCTND DRVEVKNGAV QTFFRIIDSH SVCFPPWDLI FLEVIEPLLT
KEWSTEELEN ETDFINVTLQ GLIKLYPEHF KDFKNNTTCA KEWSMLLDFL KRLLSSTSNN
TKNAVILNYQ TLLKEIITIE DVPSDILKKC CEIFTDYNIT YSDLSTNASS KTEYDCIYEL
ITGFPPLYQL ISKYDAMTDE FVEKVLLLFN SAIKYPLLPE FVQDKTKPSS MQKAILSGLD
IFMTNDSKDT EILILLQLST ISILAFDTRE KITKKLGPKL PKASLNRLPT FEAISYMSCS
NLRNRIAKID QFGISTLKAK HILRILKNLA EIIKRKSLIT GSESDEIPIW VLASNCFCDL
SNKIFKSLQE DAENPLKDNF CDLFINVIVV TLQRINPELD NLTEIDDLNE YSKYREILLE
NRIIDLFNER QLDTFIYAVW DCSFLYEFDE LENALMQDCG TFSELSQKLS SFDFSCIFGS
TTNPRFQTKY KCSLECLQDL VNFMLNTNEK LRKLTAPYLS ARIALALRRY ISDEYLIGRA
PIPKLRKTEL ATLLNGLCVI LRGVLDQNST LGNKQIGVEN LQTLSPLILR TIPVSHKMDG
LQDKVLELSL GFTKLD
