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PRM5_YEAS8
ID   PRM5_YEAS8              Reviewed;         318 AA.
AC   C8ZAC7;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Pheromone-regulated membrane protein 5;
GN   Name=PRM5; ORFNames=EC1118_1I12_0606g;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PRM5 family. {ECO:0000305}.
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DR   EMBL; FN393074; CAY80390.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8ZAC7; -.
DR   EnsemblFungi; CAY80390; CAY80390; EC1118_1I12_0606g.
DR   HOGENOM; CLU_061224_0_0_1; -.
DR   Proteomes; UP000000286; Chromosome IX, Scaffold EC1118_1I12.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Isopeptide bond; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..318
FT                   /note="Pheromone-regulated membrane protein 5"
FT                   /id="PRO_0000409313"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          238..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40476"
FT   MOD_RES         279
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40476"
FT   MOD_RES         282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40476"
FT   MOD_RES         288
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40476"
FT   CROSSLNK        314
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P40476"
SQ   SEQUENCE   318 AA;  34589 MW;  AAC557518D4830E1 CRC64;
     MTVITIAKRG LPKLTTSTSS TTTASSSSTI TSVASSSSSL PLLSNSTSSS IIPSITPPSR
     NGNPYILDSG DMPNGTVFIV VGGIAGVIFL AILLWWVITT YSSHRLTRSV QDYESKMFSA
     QHTQFYGDSP YMDYPAKENF QDQVHISESD ISPGNKDESV KDALVSHTNN EKPFLSNFER
     PLSSLVSESN RNSLFISPTG DILYKTRLSK LYQESPRLLQ KPVIMTSDNV STNSLVSTIS
     SSSASSLDNG NEKEVGEDIR KPAKIASSPS RKLLNSPESD GSVNRNHSKG NLLVVQSKRK
     PTPSTYLEHM LEGKEQDE
 
 
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