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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
 
 
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