Plasma membrane fusion protein PRM1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53835 (PRM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	661 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Conjugation
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	plasma membrane fusion involved in cytogamy Inferred from mutant phenotype Ref.7. Source: SGD response to pheromone Inferred from mutant phenotype Ref.3. Source: SGD
Cellular_component	integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD mating projection tip Inferred from direct assay Ref.3. Source: SGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

661

Plasma membrane fusion protein PRM1

PRO_0000203377

Regions

Topological domain

16

Extracellular Potential

Transmembrane

21

Helical; Potential

Topological domain

68

Cytoplasmic Potential

Transmembrane

21

Helical; Potential

Topological domain

170

Extracellular Potential

Transmembrane

21

Helical; Potential

Topological domain

107

Cytoplasmic Potential

Transmembrane

21

Helical; Potential

Topological domain

184

Extracellular Potential

Transmembrane

21

Helical; Potential

Topological domain

11

Cytoplasmic Potential

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P53835 [UniParc].

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

661

73,353

        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

References

	« Hide 'large scale' referencesShow '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. Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.
PIR	S63253.
RefSeq	NP_014120.1. NM_001183117.1.
3D structure databases
ProteinModelPortal	P53835.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1385N.
IntAct	P53835. 2 interactions.
MINT	MINT-384905.
STRING	4932.YNL279W.
Proteomic databases
PaxDb	P53835.
PeptideAtlas	P53835.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL279W; YNL279W; YNL279W.
GeneID	855442.
KEGG	sce:YNL279W.
Organism-specific databases
CYGD	YNL279w.
SGD	S000005223. PRM1.
Phylogenomic databases
eggNOG	NOG74887.
HOGENOM	HOG000115701.
OMA	MASMPHY.
OrthoDB	EOG46HKM5.
Gene expression databases
Genevestigator	P53835.
GermOnline	YNL279W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR026777. PRM1. [Graphical view]
PANTHER	PTHR31030. PTHR31030. 1 hit.
ProtoNet	Search...
Other
NextBio	979337.

Entry information

Entry name

PRM1_YEAST

Accession

Primary (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 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

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

Yeast chromosome XIV

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

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents