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   02-SEP-2026, entry version 187.
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; DOI=10.1038/387s093;
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   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   FUNCTION, SUBUNIT, INTERACTION WITH DOP1, AND SUBCELLULAR LOCATION.
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   FUNCTION, INTERACTION WITH DOP1, AND SUBCELLULAR LOCATION.
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).
RN   [14]
RP   INTERACTION WITH DOP1.
RX   PubMed=28404745; DOI=10.1091/mbc.e16-11-0772;
RA   Dalton L.E., Bean B.D.M., Davey M., Conibear E.;
RT   "Quantitative high-content imaging identifies novel regulators of Neo1
RT   trafficking at endosomes.";
RL   Mol. Biol. Cell 28:1539-1550(2017).
CC   -!- FUNCTION: Required for traffic between late Golgi and early endosomes
CC       (PubMed:16219684, PubMed:16301316). Required for endocytosis and
CC       maintenance of vacuolar structure (PubMed:12052896, PubMed:12134085,
CC       PubMed:16219684). {ECO:0000269|PubMed:12052896,
CC       ECO:0000269|PubMed:12134085, ECO:0000269|PubMed:16219684,
CC       ECO:0000269|PubMed:16301316}.
CC   -!- SUBUNIT: Homodimer (PubMed:16219684). Interacts with DOP1
CC       (PubMed:16219684, PubMed:16301316, PubMed:28404745). Interacts with
CC       ARL1 (PubMed:12052896). Interacts with NEO1 (PubMed:15314152).
CC       {ECO:0000269|PubMed:12052896, ECO:0000269|PubMed:15314152,
CC       ECO:0000269|PubMed:16219684, ECO:0000269|PubMed:16301316,
CC       ECO:0000269|PubMed:28404745}.
CC   -!- INTERACTION:
CC       P48563; Q03921: DOP1; NbExp=6; 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; 457.
DR   ComplexPortal; CPX-1028; NEO1-DOP1-MON2 golgi transporter complex.
DR   FunCoup; P48563; 871.
DR   IntAct; P48563; 9.
DR   MINT; P48563; -.
DR   STRING; 4932.YNL297C; -.
DR   iPTMnet; P48563; -.
DR   PaxDb; 4932-YNL297C; -.
DR   PeptideAtlas; P48563; -.
DR   EnsemblFungi; YNL297C_mRNA; YNL297C; YNL297C.
DR   GeneID; 855420; -.
DR   KEGG; sce:YNL297C; -.
DR   AGR; SGD:S000005241; -.
DR   SGD; S000005241; MON2.
DR   VEuPathDB; FungiDB:YNL297C; -.
DR   eggNOG; KOG1848; Eukaryota.
DR   HOGENOM; CLU_001169_1_0_1; -.
DR   InParanoid; P48563; -.
DR   OMA; AWRLCLN; -.
DR   OrthoDB; 294853at2759; -.
DR   BioCyc; YEAST:G3O-33285-MONOMER; -.
DR   BioGRID-ORCS; 855420; 0 hits in 10 CRISPR screens.
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; NAS:ComplexPortal.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; EXP:UniProtKB.
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; NAS:ComplexPortal.
DR   InterPro; IPR032629; DCB_dom.
DR   InterPro; IPR032691; Mon2/Sec7/BIG1-like_HUS.
DR   InterPro; IPR032817; Mon2_C.
DR   Pfam; PF16213; DCB; 1.
DR   Pfam; PF16206; Mon2_C; 1.
DR   Pfam; PF12783; Sec7-like_HUS; 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..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..576
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..589
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
//