ID   PRM5_YEASO              Reviewed;         318 AA.
AC   E7NIY5;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   29-SEP-2021, entry version 26.
DE   RecName: Full=Pheromone-regulated membrane protein 5;
GN   Name=PRM5; ORFNames=FOSTERSO_2274;
OS   Saccharomyces cerevisiae (strain FostersO) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FostersO;
RX   PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "Whole-genome comparison reveals novel genetic elements that characterize
RT   the genome of industrial strains of Saccharomyces cerevisiae.";
RL   PLoS Genet. 7:E1001287-E1001287(2011).
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; AEEZ01000053; EGA61897.1; -; Genomic_DNA.
DR   EnsemblFungi; EGA61897; EGA61897; FOSTERSO_2274.
DR   HOGENOM; CLU_061224_0_0_1; -.
DR   OMA; VSHTNNE; -.
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_0000409315"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          240..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;  34631 MW;  4A7443F13C583EEC CRC64;
     MTVITIAKRG LPKLTTSTSS TTTASSSSTI TSVASSSSSL PLLSNSTSSS IIPSITPPSR
     NGNPYILDSG DMPNGTVFIX VGGIAGVIFL AILLWWVITT YSSHRLTRSV QDYESKMFST
     QHTQFYGDSP YMDYPAKENF QDQVHISESD ISPGNKDESV KDALVSHTNN EKPFLSNFER
     PLSSLVSESN RNSLFISPTG DILYKTRLSK LYQESPRLLQ KPVIMTSDNV STNSLVSTIS
     SSSASSLDNG NEKEVGEDIR KPAKIASSPS RKLLNSPESD GSVNRNHSKG NLLVVQSKRK
     PTPSTYLEHM LEGKEQDE