MDG1_YEAST
ID MDG1_YEAST Reviewed; 366 AA.
AC P53885; D6W111;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Signal transduction protein MDG1;
DE AltName: Full=Multicopy suppressor of defective G-protein 1;
GN Name=MDG1; OrderedLocusNames=YNL173C; ORFNames=N1673;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8914522; DOI=10.1007/bf02172407;
RA Leberer E., Chenevert J., Leeuw T., Harcus D., Herskowitz I., Thomas D.Y.;
RT "Genetic interactions indicate a role for Mdg1p and the SH3 domain protein
RT Bem1p in linking the G-protein mediated yeast pheromone signalling pathway
RT to regulators of cell polarity.";
RL Mol. Gen. Genet. 252:608-621(1996).
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 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-216 AND SER-288, 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 [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-314, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Involved in G-protein mediated signal transduction and in the
CC regulation of polarized cell growth in pheromone-induced cells.
CC {ECO:0000269|PubMed:8914522}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8914522};
CC Peripheral membrane protein {ECO:0000269|PubMed:8914522}.
CC -!- MISCELLANEOUS: Present with 1240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CRP1/MDG1 family. {ECO:0000305}.
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DR EMBL; L02783; AAA63785.1; -; Genomic_DNA.
DR EMBL; Z71449; CAA96064.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10377.1; -; Genomic_DNA.
DR PIR; S56040; S56040.
DR RefSeq; NP_014226.1; NM_001183011.1.
DR AlphaFoldDB; P53885; -.
DR SMR; P53885; -.
DR BioGRID; 35657; 27.
DR DIP; DIP-2777N; -.
DR IntAct; P53885; 8.
DR MINT; P53885; -.
DR STRING; 4932.YNL173C; -.
DR iPTMnet; P53885; -.
DR MaxQB; P53885; -.
DR PaxDb; P53885; -.
DR PRIDE; P53885; -.
DR EnsemblFungi; YNL173C_mRNA; YNL173C; YNL173C.
DR GeneID; 855548; -.
DR KEGG; sce:YNL173C; -.
DR SGD; S000005117; MDG1.
DR VEuPathDB; FungiDB:YNL173C; -.
DR eggNOG; KOG1616; Eukaryota.
DR GeneTree; ENSGT00940000176749; -.
DR HOGENOM; CLU_765367_0_0_1; -.
DR InParanoid; P53885; -.
DR OMA; ETQTYET; -.
DR BioCyc; YEAST:G3O-33186-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-SCE-200425; Carnitine metabolism.
DR Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR PRO; PR:P53885; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53885; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..366
FT /note="Signal transduction protein MDG1"
FT /id="PRO_0000096326"
FT REGION 159..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 314
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 366 AA; 40278 MW; 1B29D0D6D0A5D1C3 CRC64;
MQSSLPQFTF KWPKGPEAII LTGTFDDWKG TLPMVKDPSG AFEITLPVTF DSPSSKFYFK
FIVDGQWLPS KDYKVNIDEG VENNFITEED VIKQRENGSS TLVPESAGLA VSKNAPLIEP
EAEKRAKKLR KFKIKRVIKT NKQTGERSIF SQEVVELPDS EDETQQVNKT GKNADGLSGT
TTIIENNVGV NEEKAIKPYE ENHPKVNLVK SEGYVTDGLG KTQSSESRLY ELSAEDLEKE
EEEEDEDKGG GKDTSTSADA EASEDQNKEP LSKSAKFEKP EEKVPVSSIT SHAKETSVKP
TGKVATETQT YETKQGAPTA AAKKIEAKKA TRPSKPKGTK ETPNKGVQKN PAKNGGFFKK
LAQLLK
