MDG1_YEAS2
ID MDG1_YEAS2 Reviewed; 366 AA.
AC C7GTE8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Signal transduction protein MDG1;
DE AltName: Full=Multicopy suppressor of defective G-protein 1;
GN Name=MDG1; ORFNames=C1Q_03692;
OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=574961;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAY291;
RX PubMed=19812109; DOI=10.1101/gr.091777.109;
RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA Pereira G.A.G.;
RT "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT bioethanol production.";
RL Genome Res. 19:2258-2270(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; ACFL01000260; EEU05905.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GTE8; -.
DR SMR; C7GTE8; -.
DR Proteomes; UP000008073; Unassembled WGS sequence.
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_0000409624"
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; 40327 MW; 6C29D0D6D0A5C974 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 ETPYKGVQKN PAKNGGFFKK
LAQLLK