ID   PRM5_YEAS7              Reviewed;         321 AA.
AC   A6ZVG0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Pheromone-regulated membrane protein 5;
GN   Name=PRM5; ORFNames=SCY_2676;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000124; EDN61385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZVG0; -.
DR   EnsemblFungi; EDN61385; EDN61385; SCY_2676.
DR   HOGENOM; CLU_061224_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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..321
FT                   /note="Pheromone-regulated membrane protein 5"
FT                   /id="PRO_0000409312"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          35..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         132
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         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40476"
FT   MOD_RES         291
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40476"
FT   CROSSLNK        317
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P40476"
SQ   SEQUENCE   321 AA;  34843 MW;  3E54B2A3216CE2B8 CRC64;
     MTVITIAKRG LPKLTTSTSS TTTASSSSTI TSVVSSSSSS SSLPLLSNST SSSIIPSITP
     PSRNGNPYIL DSGDMPNGTV FIIVGGIAGV IFLAILLWWV ITTYSSHRLT RSVQDYESKM
     FSAQHTQFYG DSPYMDYPAK ENFQDQVHIS ESDISPGNKD ESVKDALVSH TNNEKPFLSN
     FERPLSSLVS ESNRNSLFIS PTGDILNKTR LSKLYQESPR LLQKPVIMTS DNVSTNSLVS
     TISSSSASSL DNGNEKEVGE DIRKPAKIAS SPSRKLLNSP ESDGSVNRNH SKGNLLVVQS
     KRKPTPSTYL EHMLEGKEQD E