SPM1_SCHPO
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 03-AUG-2022, entry version 186.
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; 4896.SPBC119.08.1; -.
DR iPTMnet; Q92398; -.
DR MaxQB; Q92398; -.
DR PaxDb; Q92398; -.
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-110056; MAPK3 (ERK1) activation.
DR Reactome; R-SPO-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-SPO-170968; Frs2-mediated activation.
DR Reactome; R-SPO-198753; ERK/MAPK targets.
DR Reactome; R-SPO-202670; ERKs are inactivated.
DR Reactome; R-SPO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SPO-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-SPO-445144; Signal transduction by L1.
DR Reactome; R-SPO-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-SPO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-SPO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-SPO-5674135; MAP2K and MAPK activation.
DR Reactome; R-SPO-5674499; Negative feedback regulation of MAPK pathway.
DR Reactome; R-SPO-5675221; Negative regulation of MAPK pathway.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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: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:0006468; P:protein phosphorylation; IEA:InterPro.
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 GO; GO:0032995; P:regulation of fungal-type cell wall biogenesis; IC:GOC-OWL.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
