MFM3_SCHPO
ID MFM3_SCHPO Reviewed; 41 AA.
AC P40849;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=M-factor;
DE Flags: Precursor;
GN Name=mfm3; ORFNames=SPBPJ4664.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8196631; DOI=10.1128/mcb.14.6.3895-3905.1994;
RA Kjaerulff S., Davey J., Nielsen O.;
RT "Analysis of the structural genes encoding M-factor in the fission yeast
RT Schizosaccharomyces pombe: identification of a third gene, mfm3.";
RL Mol. Cell. Biol. 14:3895-3905(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kawamukai M., Sen K., Ozoe F., Omae M.;
RT "S.pombe cDNA for mfm3.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PROTEIN SEQUENCE OF 30-38, ISOPRENYLATION AT CYS-38, AND METHYLATION AT
RP CYS-38.
RX PubMed=1547790; DOI=10.1002/j.1460-2075.1992.tb05134.x;
RA Davey J.;
RT "Mating pheromones of the fission yeast Schizosaccharomyces pombe:
RT purification and structural characterization of M-factor and isolation and
RT analysis of two genes encoding the pheromone.";
RL EMBO J. 11:951-960(1992).
CC -!- FUNCTION: M-factor is a mating pheromone produced by M-type mating
CC cells. All three mfm genes contribute to the production of M-factor.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- INDUCTION: By nitrogen starvation. It is further induced by a pheromone
CC signal. Its transcription is limited to M cells.
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DR EMBL; S69926; AAB30833.1; -; Genomic_DNA.
DR EMBL; AB004296; BAA20362.1; -; mRNA.
DR EMBL; CU329671; CAC38348.1; -; Genomic_DNA.
DR PIR; A56061; A56061.
DR RefSeq; NP_595278.1; NM_001021185.2.
DR AlphaFoldDB; P40849; -.
DR BioGRID; 277863; 13.
DR STRING; 4896.SPBPJ4664.03.1; -.
DR PaxDb; P40849; -.
DR EnsemblFungi; SPBPJ4664.03.1; SPBPJ4664.03.1:pep; SPBPJ4664.03.
DR GeneID; 2541352; -.
DR KEGG; spo:SPBPJ4664.03; -.
DR PomBase; SPBPJ4664.03; mfm3.
DR VEuPathDB; FungiDB:SPBPJ4664.03; -.
DR HOGENOM; CLU_3260799_0_0_1; -.
DR PhylomeDB; P40849; -.
DR PRO; PR:P40849; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005576; C:extracellular region; ISS:PomBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000772; F:mating pheromone activity; IMP:PomBase.
DR GO; GO:0007267; P:cell-cell signaling; IMP:PomBase.
DR GO; GO:0062038; P:positive regulation of pheromone response MAPK cascade; IDA:PomBase.
DR GO; GO:0032005; P:signal transduction involved in positive regulation of conjugation with cellular fusion; NAS:PomBase.
DR InterPro; IPR005555; M-factor.
DR Pfam; PF03855; M-factor; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Lipoprotein; Membrane;
KW Methylation; Pheromone; Prenylation; Reference proteome; Stress response.
FT PROPEP 1..29
FT /evidence="ECO:0000269|PubMed:1547790"
FT /id="PRO_0000021713"
FT PEPTIDE 30..38
FT /note="M-factor"
FT /id="PRO_0000021714"
FT PROPEP 39..41
FT /note="Removed in mature form"
FT /id="PRO_0000021715"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:1547790"
FT LIPID 38
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:1547790,
FT ECO:0000269|PubMed:8196631"
SQ SEQUENCE 41 AA; 4421 MW; 150E0182C0950737 CRC64;
MDSMANTVSS SVVNTGNKPS ETLNKTVKNY TPKVPYMCVI A
