PRM1_YEAST
ID PRM1_YEAST Reviewed; 661 AA.
AC P53835; D6W0R5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Plasma membrane fusion protein PRM1;
DE AltName: Full=Pheromone-regulated membrane protein 1;
GN Name=PRM1; OrderedLocusNames=YNL279W; ORFNames=N0605;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND INDUCTION.
RX PubMed=11062271; DOI=10.1083/jcb.151.3.719;
RA Heiman M.G., Walter P.;
RT "Prm1p, a pheromone-regulated multispanning membrane protein, facilitates
RT plasma membrane fusion during yeast mating.";
RL J. Cell Biol. 151:719-730(2000).
RN [4]
RP INDUCTION.
RX PubMed=11179416; DOI=10.1091/mbc.12.2.297;
RA Epstein C.B., Waddle J.A., Hale W. IV, Dave V., Thornton J., Macatee T.L.,
RA Garner H.R., Butow R.A.;
RT "Genome-wide responses to mitochondrial dysfunction.";
RL Mol. Biol. Cell 12:297-308(2001).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12374868; DOI=10.1073/pnas.172517799;
RA Bagnat M., Simons K.;
RT "Cell surface polarization during yeast mating.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14183-14188(2002).
RN [6]
RP INDUCTION.
RX PubMed=12732146; DOI=10.1016/s0092-8674(03)00301-5;
RA Zeitlinger J., Simon I., Harbison C.T., Hannett N.M., Volkert T.L.,
RA Fink G.R., Young R.A.;
RT "Program-specific distribution of a transcription factor dependent on
RT partner transcription factor and MAPK signaling.";
RL Cell 113:395-404(2003).
RN [7]
RP FUNCTION.
RX PubMed=15590839; DOI=10.1128/ec.3.6.1664-1673.2004;
RA Jin H., Carlile C., Nolan S., Grote E.;
RT "Prm1 prevents contact-dependent lysis of yeast mating pairs.";
RL Eukaryot. Cell 3:1664-1673(2004).
RN [8]
RP FUNCTION.
RX PubMed=17210951; DOI=10.1083/jcb.200609182;
RA Heiman M.G., Engel A., Walter P.;
RT "The Golgi-resident protease Kex2 acts in conjunction with Prm1 to
RT facilitate cell fusion during yeast mating.";
RL J. Cell Biol. 176:209-222(2007).
RN [9]
RP FUNCTION.
RX PubMed=17151357; DOI=10.1091/mbc.e06-09-0776;
RA Aguilar P.S., Engel A., Walter P.;
RT "The plasma membrane proteins Prm1 and Fig1 ascertain fidelity of membrane
RT fusion during yeast mating.";
RL Mol. Biol. Cell 18:547-556(2007).
RN [10]
RP FUNCTION.
RX PubMed=18299351; DOI=10.1083/jcb.200705076;
RA Jin H., McCaffery J.M., Grote E.;
RT "Ergosterol promotes pheromone signaling and plasma membrane fusion in
RT mating yeast.";
RL J. Cell Biol. 180:813-826(2008).
CC -!- FUNCTION: Involved in cell fusion during mating by stabilizing the
CC plasma membrane fusion event. {ECO:0000269|PubMed:11062271,
CC ECO:0000269|PubMed:15590839, ECO:0000269|PubMed:17151357,
CC ECO:0000269|PubMed:17210951, ECO:0000269|PubMed:18299351}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11062271,
CC ECO:0000269|PubMed:12374868}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11062271, ECO:0000269|PubMed:12374868}.
CC Note=Localizes at sites of cell fusion during mating.
CC -!- INDUCTION: By pheromones during mating, through the regulation by the
CC STE12 transcription factor. Also induced in respiratory-deficient
CC cells. {ECO:0000269|PubMed:11062271, ECO:0000269|PubMed:11179416,
CC ECO:0000269|PubMed:12732146}.
CC -!- SIMILARITY: Belongs to the PRM1 family. {ECO:0000305}.
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DR EMBL; Z71555; CAA96191.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10281.1; -; Genomic_DNA.
DR PIR; S63253; S63253.
DR RefSeq; NP_014120.1; NM_001183117.1.
DR AlphaFoldDB; P53835; -.
DR BioGRID; 35562; 25.
DR DIP; DIP-1385N; -.
DR IntAct; P53835; 3.
DR MINT; P53835; -.
DR STRING; 4932.YNL279W; -.
DR TCDB; 9.B.63.1.1; the yeast pheromone-induced plasma membrane mating cell fusion protein (prm1) family.
DR PaxDb; P53835; -.
DR PRIDE; P53835; -.
DR EnsemblFungi; YNL279W_mRNA; YNL279W; YNL279W.
DR GeneID; 855442; -.
DR KEGG; sce:YNL279W; -.
DR SGD; S000005223; PRM1.
DR VEuPathDB; FungiDB:YNL279W; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR HOGENOM; CLU_010191_1_0_1; -.
DR InParanoid; P53835; -.
DR OMA; QTYLCLF; -.
DR BioCyc; YEAST:G3O-33271-MON; -.
DR PRO; PR:P53835; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53835; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032220; P:plasma membrane fusion involved in cytogamy; IMP:SGD.
DR InterPro; IPR026777; PRM1.
DR PANTHER; PTHR31030; PTHR31030; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Conjugation; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..661
FT /note="Plasma membrane fusion protein PRM1"
FT /id="PRO_0000203377"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..629
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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; 73353 MW; 2038CACDCEDD927D CRC64;
MSGFKCYLQL GDRLSQIWLN KYTLVLLLAM LKLLFFSKSI QHAIEVSETY ILSNCYSIDS
LYSKMTDNTP HYLGIMGNYL IEKGMEETVK ATLETLSLIV YASEGLVNFA IDLYLGTYAC
LIVSAVDGTV DVATNITEKL ISLVNDTVSS VANELDTGLN DISKIINKVI KAASKVENFF
TGDDDDSNMT SSIKSVNLTI SALHNLYIPS SINDKLEELS AKTPDFAQVK NTTKNLISVP
FNEVRKNIKA VNASNIIGDT SVLYVPPVSL DNSTGICSSN QSEILAFYSI LGHVLKIATV
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 LAKQTDNSTI PTASSTSAAT
ENLLENLVND MREGLLKILR AYHRITLGEL TVALVILAVW LVQLPIALVI LRLRLRKATF
D
