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Protein

Mating hormone A-factor 1

Gene

MFA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The active factor is excreted into the culture medium by haploid cells of the A mating type and acts on cells of the opposite mating type (type alpha). It mediates the conjugation process between the two types by inhibiting the initiation of DNA synthesis in type alpha cells and synchronizing them with type A.

GO - Molecular functioni

  1. mating pheromone activity Source: SGD

GO - Biological processi

  1. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Pheromone

Enzyme and pathway databases

BioCyciYEAST:G3O-29989-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mating hormone A-factor 1
Gene namesi
Name:MFA1
Ordered Locus Names:YDR461W
ORF Names:D8035.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR461w.
SGDiS000002869. MFA1.

Subcellular locationi

Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated

GO - Cellular componenti

  1. extracellular region Source: SGD
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 21211 PublicationPRO_0000021690Add
BLAST
Peptidei22 – 3312Mating hormone A-factor 1PRO_0000021691Add
BLAST
Propeptidei34 – 363Removed in mature formPRO_0000021692

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331Cysteine methyl ester1 Publication
Lipidationi33 – 331S-farnesyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiP34165.

Miscellaneous databases

PMAP-CutDBP34165.

Expressioni

Gene expression databases

GenevestigatoriP34165.

Interactioni

Protein-protein interaction databases

BioGridi32515. 9 interactions.
DIPiDIP-4646N.
MINTiMINT-567416.
STRINGi4932.YDR461W.

Structurei

3D structure databases

ProteinModelPortaliP34165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

InParanoidiP34165.
KOiK11235.
OrthoDBiEOG7T1RR3.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34165-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
MQPSTATAAP KEKTSSEKKD NYIIKGVFWD PACVIA
Length:36
Mass (Da):3,927
Last modified:January 31, 1994 - v1
Checksum:i03E051D7D6C2522F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20817 Genomic DNA. Translation: AAA68601.1.
U26203 Genomic DNA. Translation: AAA67687.1.
U33050 Genomic DNA. Translation: AAB64920.1.
AY557797 Genomic DNA. Translation: AAS56123.1.
BK006938 Genomic DNA. Translation: DAA12295.1.
PIRiS59735.
RefSeqiNP_010749.3. NM_001180769.3.

Genome annotation databases

EnsemblFungiiYDR461W; YDR461W; YDR461W.
GeneIDi852072.
KEGGisce:YDR461W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20817 Genomic DNA. Translation: AAA68601.1.
U26203 Genomic DNA. Translation: AAA67687.1.
U33050 Genomic DNA. Translation: AAB64920.1.
AY557797 Genomic DNA. Translation: AAS56123.1.
BK006938 Genomic DNA. Translation: DAA12295.1.
PIRiS59735.
RefSeqiNP_010749.3. NM_001180769.3.

3D structure databases

ProteinModelPortaliP34165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32515. 9 interactions.
DIPiDIP-4646N.
MINTiMINT-567416.
STRINGi4932.YDR461W.

Proteomic databases

PaxDbiP34165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR461W; YDR461W; YDR461W.
GeneIDi852072.
KEGGisce:YDR461W.

Organism-specific databases

CYGDiYDR461w.
SGDiS000002869. MFA1.

Phylogenomic databases

InParanoidiP34165.
KOiK11235.
OrthoDBiEOG7T1RR3.

Enzyme and pathway databases

BioCyciYEAST:G3O-29989-MONOMER.

Miscellaneous databases

NextBioi970367.
PMAP-CutDBP34165.

Gene expression databases

GenevestigatoriP34165.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of genes encoding precursors of the yeast peptide mating pheromone a-factor."
    Brake A.J., Brenner C., Najarian R., Laybourn P., Merryweather J.
    (In) Gething M.-J. (eds.); Protein transport and secretion, pp.103-108, Cold Spring Harbor Laboratory Press, New York (1984)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The a-factor pheromone of Saccharomyces cerevisiae is essential for mating."
    Michaelis S., Herskowitz I.
    Mol. Cell. Biol. 8:1309-1318(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Amino acid sequences of a-factor mating peptides from Saccharomyces cerevisiae."
    Betz R., Crabb J.W., Meyer H.E., Wittig R., Duntze W.
    J. Biol. Chem. 262:546-548(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-33.
  7. "Structure of Saccharomyces cerevisiae mating hormone a-factor. Identification of S-farnesyl cysteine as a structural component."
    Anderegg R.J., Betz R., Carr S.A., Crabb J.W., Duntze W.
    J. Biol. Chem. 263:18236-18240(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-33, METHYLATION AT CYS-33, IDENTIFICATION BY MASS SPECTROMETRY.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "The conformation of a-factor is not influenced by the S-prenylation of Cys12."
    Gounarides J.S., Broido M.S., Xue C.-B., Becker J.M., Naider F.R.
    Biochem. Biophys. Res. Commun. 181:1125-1130(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiMFA1_YEAST
AccessioniPrimary (citable) accession number: P34165
Secondary accession number(s): D6VT85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1994
Last sequence update: January 31, 1994
Last modified: January 6, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 28900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.