MATP2_SCHPO
ID MATP2_SCHPO Reviewed; 201 AA.
AC Q09180;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Pro-P-factor;
DE Contains:
DE RecName: Full=P-factor;
DE Contains:
DE RecName: Full=P-factor-like 1;
DE Contains:
DE RecName: Full=P-factor-like 2;
DE Flags: Precursor;
GN Name=map2; ORFNames=SPCC1795.06;
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], AND PROTEIN SEQUENCE OF 66-88.
RX PubMed=8314086; DOI=10.1101/gad.8.3.328;
RA Imai Y., Yamamoto M.;
RT "The fission yeast mating pheromone P-factor: its molecular structure, gene
RT structure, and ability to induce gene expression and G1 arrest in the
RT mating partner.";
RL Genes Dev. 8:328-338(1994).
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).
RN [3]
RP CLEAVAGE BY KPR, AND GLYCOSYLATION.
RX PubMed=7813430; DOI=10.1002/j.1460-2075.1994.tb06936.x;
RA Davey J., Davis K., Imai Y., Yamamoto M., Matthews G.;
RT "Isolation and characterization of krp, a dibasic endopeptidase required
RT for cell viability in the fission yeast Schizosaccharomyces pombe.";
RL EMBO J. 13:5910-5921(1994).
CC -!- FUNCTION: In h- cells under nutritional starvation, P-factor induces
CC alteration of cell morphology toward mating, arrest of the cell cycle
CC at the G1 phase prior to the initiation of DNA synthesis and indirect
CC transcriptional activation of the sxa2 gene which down-regulates the
CC signaling pathway.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The Pro-P-factor precursor carries 4 repetitive units. The
CC second and fourth units generate the major form of the P-factor in the
CC cell. The first and the third units encode slightly different peptides,
CC the fate of which is unclear.
CC -!- PTM: Proteolytically cleaved by kpr, probably at the C-terminal side of
CC dibasic Lys-Arg residues. {ECO:0000269|PubMed:7813430}.
CC -!- PTM: Glycosylated. Most of the precursor molecules are glycosylated on
CC at least one site, but only a small proportion are glycosylated on both
CC sites. {ECO:0000269|PubMed:7813430}.
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DR EMBL; D26072; BAA05067.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA18641.1; -; Genomic_DNA.
DR PIR; A36985; A36985.
DR RefSeq; NP_588038.1; NM_001023030.2.
DR AlphaFoldDB; Q09180; -.
DR BioGRID; 275957; 3.
DR STRING; 4896.SPCC1795.06.1; -.
DR PaxDb; Q09180; -.
DR EnsemblFungi; SPCC1795.06.1; SPCC1795.06.1:pep; SPCC1795.06.
DR GeneID; 2539392; -.
DR KEGG; spo:SPCC1795.06; -.
DR PomBase; SPCC1795.06; map2.
DR VEuPathDB; FungiDB:SPCC1795.06; -.
DR HOGENOM; CLU_1361120_0_0_1; -.
DR OMA; HWWNFRN; -.
DR PRO; PR:Q09180; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0009986; C:cell surface; IC:PomBase.
DR GO; GO:0005576; C:extracellular region; IC:PomBase.
DR GO; GO:0000772; F:mating pheromone activity; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007267; P:cell-cell signaling; IDA:PomBase.
DR GO; GO:0031142; P:induction of conjugation upon nitrogen starvation; IMP:PomBase.
DR GO; GO:0010514; P:induction of conjugation with cellular fusion; IDA: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; TAS:PomBase.
PE 1: Evidence at protein level;
KW Cell cycle; Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Pheromone; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..31
FT /id="PRO_0000021642"
FT PEPTIDE 32..54
FT /note="P-factor-like 1"
FT /id="PRO_0000021643"
FT PROPEP 58..65
FT /evidence="ECO:0000269|PubMed:8314086"
FT /id="PRO_0000021644"
FT PEPTIDE 66..88
FT /note="P-factor"
FT /id="PRO_0000021645"
FT PROPEP 92..99
FT /id="PRO_0000021646"
FT PEPTIDE 100..122
FT /note="P-factor-like 2"
FT /id="PRO_0000021647"
FT PROPEP 126..133
FT /id="PRO_0000021648"
FT PEPTIDE 134..156
FT /note="P-factor"
FT /id="PRO_0000021649"
FT PROPEP 160..201
FT /id="PRO_0000021650"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 201 AA; 23453 MW; DC0E849764127D90 CRC64;
MKITAVIALL FSLAAASPIP VADPGVVSVS KSYADFLRVY QSWNTFANPD RPNLKKREFE
AAPAKTYADF LRAYQSWNTF VNPDRPNLKK REFEAAPEKS YADFLRAYHS WNTFVNPDRP
NLKKREFEAA PAKTYADFLR AYQSWNTFVN PDRPNLKKRT EEDEENEEED EEYYRFLQFY
IMTVPENSTI TDVNITAKFE S
