ID   SPM1_SCHPO              Reviewed;         422 AA.
AC   Q92398;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Mitogen-activated protein kinase spm1;
DE            Short=MAP kinase spm1;
DE            EC=2.7.11.24;
DE   AltName: Full=MAP kinase pmk1;
GN   Name=spm1; Synonyms=pmk1; ORFNames=SPBC119.08;
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=8943330; DOI=10.1128/mcb.16.12.6752;
RA   Toda T., Dhut S., Superti-Furga G., Gotoh G., Nishida E., Sugiura R.,
RA   Kuno T.;
RT   "The fission yeast pmk1+ gene encodes a novel mitogen-activated protein
RT   kinase homolog which regulates cell integrity and functions coordinately
RT   with the protein kinase C pathway.";
RL   Mol. Cell. Biol. 16:6752-6764(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9135147; DOI=10.1093/emboj/16.6.1318;
RA   Zaitsevskaya-Carter T., Cooper J.A.;
RT   "Spm1, a stress-activated MAP kinase that regulates morphogenesis in
RT   S.pombe.";
RL   EMBO J. 16:1318-1331(1997).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186 AND TYR-188, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Regulates cell integrity and functions coordinately with the
CC       protein kinase C pathway (pck1 and pck2). Involved the regulation of
CC       wall architecture, cell shape, cytokinesis in exponential and
CC       stationary phase, and metabolism of ions.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by tyrosine and threonine
CC       phosphorylation by skh1/pek1.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-186 and Tyr-188, which activates the
CC       enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR   EMBL; X98243; CAA66899.1; -; Genomic_DNA.
DR   EMBL; U65405; AAC49707.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA17923.1; -; Genomic_DNA.
DR   PIR; T39306; T39306.
DR   RefSeq; NP_595289.1; NM_001021196.2.
DR   AlphaFoldDB; Q92398; -.
DR   SMR; Q92398; -.
DR   BioGRID; 276464; 136.
DR   STRING; 284812.Q92398; -.
DR   iPTMnet; Q92398; -.
DR   MaxQB; Q92398; -.
DR   PaxDb; 4896-SPBC119-08-1; -.
DR   EnsemblFungi; SPBC119.08.1; SPBC119.08.1:pep; SPBC119.08.
DR   GeneID; 2539920; -.
DR   KEGG; spo:SPBC119.08; -.
DR   PomBase; SPBC119.08; -.
DR   VEuPathDB; FungiDB:SPBC119.08; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; Q92398; -.
DR   OMA; MDIPRPE; -.
DR   PhylomeDB; Q92398; -.
DR   BRENDA; 2.7.11.24; 5613.
DR   Reactome; R-SPO-198753; ERK/MAPK targets.
DR   Reactome; R-SPO-198765; Signalling to ERK5.
DR   Reactome; R-SPO-202670; ERKs are inactivated.
DR   Reactome; R-SPO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-SPO-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-SPO-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
DR   PRO; PR:Q92398; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0004707; F:MAP kinase activity; IDA:PomBase.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000196; P:cell wall integrity MAPK cascade; IDA:PomBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IMP:PomBase.
DR   GO; GO:1902413; P:negative regulation of mitotic cytokinesis; IMP:PomBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IMP:PomBase.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IMP:PomBase.
DR   GO; GO:1903340; P:positive regulation of cell wall organization or biogenesis; EXP:PomBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; EXP:PomBase.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:1903338; P:regulation of cell wall organization or biogenesis; EXP:PomBase.
DR   CDD; cd07857; STKc_MPK1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   PANTHER; PTHR24055:SF603; MITOGEN-ACTIVATED PROTEIN KINASE SLT2_MPK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell shape; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..422
FT                   /note="Mitogen-activated protein kinase spm1"
FT                   /id="PRO_0000186341"
FT   DOMAIN          21..314
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          359..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           186..188
FT                   /note="TXY"
FT   COMPBIAS        363..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         27..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         186
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         188
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   422 AA;  48262 MW;  FD02521E64E8BF82 CRC64;
     MDRRHRVYRV FNQEMYVEPN FKVVKELGQG AYGIVCAARN VASKDQEAVA IKKITNVFSK
     SILTKRALRE IKLLIHFRNH RNITCIYDLD IINPYNFNEV YIYEELMEAD LNAIIKSGQP
     LTDAHFQSFI YQILCGLKYI HSANVIHRDL KPGNLLVNAD CELKICDFGL ARGCSENPEE
     NPGFMTEYVA TRWYRAPEIM LSFSSYHKGI DVWSVGCILA ELLGGTPLFK GKDFVHQLNL
     ILHQLGTPDE ETLSHISSSR AQEYVRSLPK QRPIPFETNF PKANPLALDL LAKLLAFDPN
     RRISVDDALE HPYLAVWHDP SDEPVCDSVF DFSFEYIEDA NELRRVILDE VLNFRQKVRR
     RSHPTNPTVN IPQPAQTVPS NDNGSFNVSS SSSSQTSNKK RHDHSYNETA AIDHKSDDNR
     HN
//