ID   PRM5_YEAS1              Reviewed;         318 AA.
AC   B3LTW4;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Pheromone-regulated membrane protein 5;
GN   Name=PRM5; ORFNames=SCRG_05289;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408055; EDV09595.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LTW4; -.
DR   EnsemblFungi; EDV09595; EDV09595; SCRG_05289.
DR   HOGENOM; CLU_061224_0_0_1; -.
DR   Proteomes; UP000008335; 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..318
FT                   /note="Pheromone-regulated membrane protein 5"
FT                   /id="PRO_0000409310"
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;  34619 MW;  E0DEEDF13C583D8C CRC64;
     MTVITIAKRG LPKLTTSTSS TTTASSSSTI TSVASSSSSL PLLSNSTSSS IIPSITPPSR
     NGNPYILDSG DMPNGTVFIV VGGIAGVIFL AILLWWVITT YSSHRLTRSV QDYESKMFST
     QHTQFYGDSP YMDYPAKENF QDQVHISESD ISPGNKDESV KDALVSHTNN EKPFLSNFER
     PLSSLVSESN RNSLFISPTG DILYKTRLSK LYQESPRLLQ KPVIMTSDNV STNSLVSTIS
     SSSASSLDNG NEKEVGEDIR KPAKIASSPS RKLLNSPESD GSVNRNHSKG NLLVVQSKRK
     PTPSTYLEHM LEGKEQDE