ID   PRM5_YEASL              Reviewed;         318 AA.
AC   E7KPQ3;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   02-JUN-2021, entry version 27.
DE   RecName: Full=Pheromone-regulated membrane protein 5;
GN   Name=PRM5; ORFNames=QA23_2310;
OS   Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin QA23;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ADVV01000043; EGA82450.1; -; Genomic_DNA.
DR   EnsemblFungi; EGA82450; EGA82450; QA23_2310.
DR   HOGENOM; CLU_061224_0_0_1; -.
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_0000409314"
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;  34669 MW;  82D045E94609B016 CRC64;
     MTVITIAKRG LPKLTTSTSS TTTASSSSTI TSVXSSSSSL PLLSNSTSSS IIPSITPPSR
     NGNPYILDSG DMPNGTVFIV VGGIAGVIFL AILLWWVITT YSSHRLTRSV QDYESKMFSX
     QHTQFYGDSP YMDYPAKENF QDQVHISESD ISPGNKDESV KDALVSHTNN EKPFLSNFER
     PLSSLVSESN RNSLFISPTG DILYKTRLSK LYQESPRLLQ KPVIMTSDNV STNSLVSTIS
     SSSASSLDNG NEKEVGEDIR KPAKIASSPS RKLLNSPESD GSVNRNHSKG NLLVVQSKRK
     PTPSTYLEHM LEGKEQDE