ID   MDG1_YEAS8              Reviewed;         366 AA.
AC   C8ZG55;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Signal transduction protein MDG1;
DE   AltName: Full=Multicopy suppressor of defective G-protein 1;
GN   Name=MDG1; ORFNames=EC1118_1N9_1761g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: Involved in G-protein mediated signal transduction and in the
CC       regulation of polarized cell growth in pheromone-induced cells.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CRP1/MDG1 family. {ECO:0000305}.
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DR   EMBL; FN393086; CAY82428.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8ZG55; -.
DR   SMR; C8ZG55; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   EnsemblFungi; CAY82428; CAY82428; EC1118_1N9_1761g.
DR   HOGENOM; CLU_765367_0_0_1; -.
DR   Proteomes; UP000000286; Chromosome XIV, Scaffold EC1118_1N9.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Cell membrane; Isopeptide bond; Membrane; Phosphoprotein; Ubl conjugation.
FT   CHAIN           1..366
FT                   /note="Signal transduction protein MDG1"
FT                   /id="PRO_0000409626"
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:0000250|UniProtKB:P53885"
FT   MOD_RES         216
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P53885"
FT   MOD_RES         288
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53885"
FT   CROSSLNK        314
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P53885"
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