MFA1_YEAST
ID MFA1_YEAST Reviewed; 36 AA.
AC P34165; D6VT85;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Mating hormone A-factor 1;
DE Flags: Precursor;
GN Name=MFA1; OrderedLocusNames=YDR461W; ORFNames=D8035.5;
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 [GENOMIC DNA].
RA Brake A.J., Brenner C., Najarian R., Laybourn P., Merryweather J.;
RT "Structure of genes encoding precursors of the yeast peptide mating
RT pheromone a-factor.";
RL (In) Gething M.-J. (eds.);
RL Protein transport and secretion, pp.103-108, Cold Spring Harbor Laboratory
RL Press, New York (1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3285180; DOI=10.1128/mcb.8.3.1309-1318.1988;
RA Michaelis S., Herskowitz I.;
RT "The a-factor pheromone of Saccharomyces cerevisiae is essential for
RT mating.";
RL Mol. Cell. Biol. 8:1309-1318(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PROTEIN SEQUENCE OF 22-33.
RX PubMed=3542988; DOI=10.1016/s0021-9258(19)75817-7;
RA Betz R., Crabb J.W., Meyer H.E., Wittig R., Duntze W.;
RT "Amino acid sequences of a-factor mating peptides from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 262:546-548(1987).
RN [7]
RP ISOPRENYLATION AT CYS-33, METHYLATION AT CYS-33, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=3056940; DOI=10.1016/s0021-9258(19)81351-0;
RA Anderegg R.J., Betz R., Carr S.A., Crabb J.W., Duntze W.;
RT "Structure of Saccharomyces cerevisiae mating hormone a-factor.
RT Identification of S-farnesyl cysteine as a structural component.";
RL J. Biol. Chem. 263:18236-18240(1988).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=1764063; DOI=10.1016/0006-291x(91)92055-o;
RA Gounarides J.S., Broido M.S., Xue C.-B., Becker J.M., Naider F.R.;
RT "The conformation of a-factor is not influenced by the S-prenylation of
RT Cys12.";
RL Biochem. Biophys. Res. Commun. 181:1125-1130(1991).
CC -!- FUNCTION: The active factor is excreted into the culture medium by
CC haploid cells of the A mating type and acts on cells of the opposite
CC mating type (type alpha). It mediates the conjugation process between
CC the two types by inhibiting the initiation of DNA synthesis in type
CC alpha cells and synchronizing them with type A.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 28900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; U20817; AAA68601.1; -; Genomic_DNA.
DR EMBL; U26203; AAA67687.1; -; Genomic_DNA.
DR EMBL; U33050; AAB64920.1; -; Genomic_DNA.
DR EMBL; AY557797; AAS56123.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12295.1; -; Genomic_DNA.
DR PIR; S59735; S59735.
DR RefSeq; NP_010749.3; NM_001180769.3.
DR AlphaFoldDB; P34165; -.
DR BioGRID; 32515; 17.
DR DIP; DIP-4646N; -.
DR IntAct; P34165; 2.
DR STRING; 4932.YDR461W; -.
DR PaxDb; P34165; -.
DR PRIDE; P34165; -.
DR EnsemblFungi; YDR461W_mRNA; YDR461W; YDR461W.
DR GeneID; 852072; -.
DR KEGG; sce:YDR461W; -.
DR SGD; S000002869; MFA1.
DR VEuPathDB; FungiDB:YDR461W; -.
DR GeneTree; ENSGT00940000180742; -.
DR HOGENOM; CLU_220658_0_0_1; -.
DR InParanoid; P34165; -.
DR BioCyc; YEAST:G3O-29989-MON; -.
DR PRO; PR:P34165; -.
DR Proteomes; UP000002311; Chromosome IV.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000772; F:mating pheromone activity; IMP:SGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
DR InterPro; IPR035296; Mfa1/2.
DR Pfam; PF17317; MFA1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Lipoprotein; Membrane;
KW Methylation; Pheromone; Prenylation; Reference proteome.
FT PROPEP 1..21
FT /evidence="ECO:0000269|PubMed:3542988"
FT /id="PRO_0000021690"
FT PEPTIDE 22..33
FT /note="Mating hormone A-factor 1"
FT /id="PRO_0000021691"
FT PROPEP 34..36
FT /note="Removed in mature form"
FT /id="PRO_0000021692"
FT MOD_RES 33
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:3056940"
FT LIPID 33
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:3056940"
SQ SEQUENCE 36 AA; 3927 MW; 03E051D7D6C2522F CRC64;
MQPSTATAAP KEKTSSEKKD NYIIKGVFWD PACVIA
