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P53835 (PRM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plasma membrane fusion protein PRM1
Alternative name(s):
Pheromone-regulated membrane protein 1
Gene names
Name:PRM1
Ordered Locus Names:YNL279W
ORF Names:N0605
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length661 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in cell fusion during mating by stabilizing the plasma membrane fusion event. Ref.3 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein. Note: Localizes at sites of cell fusion during mating. Ref.3 Ref.5

Induction

By pheromones during mating, through the regulation by the STE12 transcription factor. Also induced in respiratory-deficient cells. Ref.3 Ref.4 Ref.6

Sequence similarities

Belongs to the PRM1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 661661Plasma membrane fusion protein PRM1
PRO_0000203377

Regions

Topological domain1 – 1616Extracellular Potential
Transmembrane17 – 3721Helical; Potential
Topological domain38 – 10568Cytoplasmic Potential
Transmembrane106 – 12621Helical; Potential
Topological domain127 – 296170Extracellular Potential
Transmembrane297 – 31721Helical; Potential
Topological domain318 – 424107Cytoplasmic Potential
Transmembrane425 – 44521Helical; Potential
Topological domain446 – 629184Extracellular Potential
Transmembrane630 – 65021Helical; Potential
Topological domain651 – 66111Cytoplasmic Potential

Amino acid modifications

Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation2801N-linked (GlcNAc...) Potential
Glycosylation4901N-linked (GlcNAc...) Potential
Glycosylation5051N-linked (GlcNAc...) Potential
Glycosylation5121N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential
Glycosylation5731N-linked (GlcNAc...) Potential
Glycosylation5871N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P53835 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2038CACDCEDD927D

FASTA66173,353
        10         20         30         40         50         60 
MSGFKCYLQL GDRLSQIWLN KYTLVLLLAM LKLLFFSKSI QHAIEVSETY ILSNCYSIDS 

        70         80         90        100        110        120 
LYSKMTDNTP HYLGIMGNYL IEKGMEETVK ATLETLSLIV YASEGLVNFA IDLYLGTYAC 

       130        140        150        160        170        180 
LIVSAVDGTV DVATNITEKL ISLVNDTVSS VANELDTGLN DISKIINKVI KAASKVENFF 

       190        200        210        220        230        240 
TGDDDDSNMT SSIKSVNLTI SALHNLYIPS SINDKLEELS AKTPDFAQVK NTTKNLISVP 

       250        260        270        280        290        300 
FNEVRKNIKA VNASNIIGDT SVLYVPPVSL DNSTGICSSN QSEILAFYSI LGHVLKIATV 

       310        320        330        340        350        360 
VCITVLICFA VGAMAPVAWN EIKLWRRLCG MRDHYMLSRQ DSYTSFSSEN THELKDPFRD 

       370        380        390        400        410        420 
PPIQNGQYDV IASYQQCFQT WNTRIAGWMT NLVTFGKSPE NIDPKTKQKI EWVVAYMTSE 

       430        440        450        460        470        480 
RALCVLGIGL LGILVCICQF VMIALLKHKI SHSLTSNDGD GVQNLLKSST AVDIENQMSL 

       490        500        510        520        530        540 
WSVQTNKYIN TTETNINQEV FGWINTTTLS VNNTVATMIS DIDTTLADVF NGTLLYNPMK 

       550        560        570        580        590        600 
TVVGCAIENK LYTIEKAMTW IHDKAQLHIP RINGTQIKQA LAKQTDNSTI PTASSTSAAT 

       610        620        630        640        650        660 
ENLLENLVND MREGLLKILR AYHRITLGEL TVALVILAVW LVQLPIALVI LRLRLRKATF 


D 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Prm1p, a pheromone-regulated multispanning membrane protein, facilitates plasma membrane fusion during yeast mating."
Heiman M.G., Walter P.
J. Cell Biol. 151:719-730(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INDUCTION.
[4]"Genome-wide responses to mitochondrial dysfunction."
Epstein C.B., Waddle J.A., Hale W. IV, Dave V., Thornton J., Macatee T.L., Garner H.R., Butow R.A.
Mol. Biol. Cell 12:297-308(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[5]"Cell surface polarization during yeast mating."
Bagnat M., Simons K.
Proc. Natl. Acad. Sci. U.S.A. 99:14183-14188(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"Program-specific distribution of a transcription factor dependent on partner transcription factor and MAPK signaling."
Zeitlinger J., Simon I., Harbison C.T., Hannett N.M., Volkert T.L., Fink G.R., Young R.A.
Cell 113:395-404(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"Prm1 prevents contact-dependent lysis of yeast mating pairs."
Jin H., Carlile C., Nolan S., Grote E.
Eukaryot. Cell 3:1664-1673(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast mating."
Heiman M.G., Engel A., Walter P.
J. Cell Biol. 176:209-222(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The plasma membrane proteins Prm1 and Fig1 ascertain fidelity of membrane fusion during yeast mating."
Aguilar P.S., Engel A., Walter P.
Mol. Biol. Cell 18:547-556(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Ergosterol promotes pheromone signaling and plasma membrane fusion in mating yeast."
Jin H., McCaffery J.M., Grote E.
J. Cell Biol. 180:813-826(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z71555 Genomic DNA. Translation: CAA96191.1.
BK006947 Genomic DNA. Translation: DAA10281.1.
PIRS63253.
RefSeqNP_014120.1. NM_001183117.1.

3D structure databases

ProteinModelPortalP53835.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35562. 17 interactions.
DIPDIP-1385N.
IntActP53835. 3 interactions.
MINTMINT-384905.
STRING4932.YNL279W.

Proteomic databases

PaxDbP53835.
PeptideAtlasP53835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL279W; YNL279W; YNL279W.
GeneID855442.
KEGGsce:YNL279W.

Organism-specific databases

CYGDYNL279w.
SGDS000005223. PRM1.

Phylogenomic databases

eggNOGNOG74887.
HOGENOMHOG000115701.
OMALTWVHDH.
OrthoDBEOG715QCZ.

Enzyme and pathway databases

BioCycYEAST:G3O-33271-MONOMER.

Gene expression databases

GenevestigatorP53835.

Family and domain databases

InterProIPR026777. PRM1.
[Graphical view]
PANTHERPTHR31030. PTHR31030. 1 hit.
ProtoNetSearch...

Other

NextBio979337.

Entry information

Entry namePRM1_YEAST
AccessionPrimary (citable) accession number: P53835
Secondary accession number(s): D6W0R5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families