MFM1_SCHPO
ID MFM1_SCHPO Reviewed; 42 AA.
AC P34068;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=M-factor;
DE Flags: Precursor;
GN Name=mfm1; ORFNames=SPAPB8E5.05;
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], PROTEIN SEQUENCE OF 31-39,
RP ISOPRENYLATION AT CYS-39, AND METHYLATION AT CYS-39.
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).
RN [2]
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).
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; X63627; CAA45175.1; -; Genomic_DNA.
DR EMBL; CU329670; CAC37424.1; -; Genomic_DNA.
DR PIR; S21027; S21027.
DR RefSeq; NP_594779.1; NM_001020207.2.
DR AlphaFoldDB; P34068; -.
DR BioGRID; 279674; 16.
DR STRING; 4896.SPAPB8E5.05.1; -.
DR PaxDb; P34068; -.
DR EnsemblFungi; SPAPB8E5.05.1; SPAPB8E5.05.1:pep; SPAPB8E5.05.
DR PomBase; SPAPB8E5.05; mfm1.
DR VEuPathDB; FungiDB:SPAPB8E5.05; -.
DR HOGENOM; CLU_3260799_0_0_1; -.
DR PhylomeDB; P34068; -.
DR PRO; PR:P34068; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005576; C:extracellular region; IDA: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 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..30
FT /evidence="ECO:0000269|PubMed:1547790"
FT /id="PRO_0000021707"
FT PEPTIDE 31..39
FT /note="M-factor"
FT /id="PRO_0000021708"
FT PROPEP 40..42
FT /note="Removed in mature form"
FT /id="PRO_0000021709"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:1547790"
FT LIPID 39
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:1547790"
SQ SEQUENCE 42 AA; 4448 MW; C78488648EE780F5 CRC64;
MDSMANSVSS SSVVNAGNKP AETLNKTVKN YTPKVPYMCV IA