ID   PRM1_YEAS7              Reviewed;         661 AA.
AC   A6ZRG6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Plasma membrane fusion protein PRM1;
DE   AltName: Full=Pheromone-regulated membrane protein 1;
GN   Name=PRM1; ORFNames=SCY_4527;
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   -!- FUNCTION: Involved in cell fusion during mating by stabilizing the
CC       plasma membrane fusion event. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Note=Localizes at sites of cell fusion during
CC       mating. {ECO:0000250}.
CC   -!- INDUCTION: By pheromones during mating, through the regulation by the
CC       STE12 transcription factor. Also induced in respiratory-deficient cells
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PRM1 family. {ECO:0000305}.
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DR   EMBL; AAFW02000067; EDN62548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZRG6; -.
DR   EnsemblFungi; EDN62548; EDN62548; SCY_4527.
DR   HOGENOM; CLU_010191_1_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043332; C:mating projection tip; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR026777; PRM1.
DR   PANTHER; PTHR31030; PTHR31030; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Conjugation; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..661
FT                   /note="Plasma membrane fusion protein PRM1"
FT                   /id="PRO_0000337294"
FT   TOPO_DOM        1..16
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..105
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..296
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..424
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        446..629
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        630..650
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        651..661
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        505
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        512
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        531
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        573
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        587
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   661 AA;  73302 MW;  283A48A06CAD5F1E CRC64;
     MSGFKCYLQL GDRLSQIWLN KYTLVLLLAM LKLLFFSKSI QHAIEVSETY ILSNCYSIDS
     LYSKMTDNTP HYLGIMGNYL IEKGMEETVK ATLETLSLIV YASEGLVNFA IDLYLGTYAC
     LIVSAVDGTV DVATNTTEKL ISLVNDTVSS VANELDTGLN DISKIINKVI KAASKVENFF
     TGDDDDSNMT SSIKSVNLTI SALHNLYIPS SINDKLEELS AKTPDFAQVK NTTKNLISVP
     FNEVRKNIKA VNASNIIGDT SVLYVPPVSL DNSTGICSSN QSEILAFYSI LGQVLKIATV
     VCITVLICFA VGAMAPVAWN EIKLWRRLCG MRDHYMLSRQ DSYTSFSSEN THELKDPFRD
     PPIQNGQYDV IASYQQCFQT WNTRIAGWMT NLVTFGKSPE NIDPKTKQKI EWVVAYMTSE
     RALCVLGIGL LGILVCICQF VMIALLKHKI SHSLTSNDGD GVQNLLKSST AVDIENQMSL
     WSVQTNKYIN TTETNINQEV FGWINTTTLS VNNTVATMIS DIDTTLADVF NGTLLYNPMK
     TVVGCAIENK LYTIEKAMTW IHDKAQLHIP RINGTQIKQA LAKQADNSTI PTASSTSAAT
     ENLLENLVND MREGLLKILR AYHRITLGEL TVALVILAVW LVQLPIALVI LRLRLRKATF
     D