SRK1_SCHPO
ID SRK1_SCHPO Reviewed; 580 AA.
AC O94547;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Serine/threonine-protein kinase srk1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:15629716};
DE AltName: Full=Sty1-regulated kinase 1;
GN Name=srk1 {ECO:0000303|PubMed:12080074, ECO:0000312|PomBase:SPCC1322.08};
GN Synonyms=mkp1 {ECO:0000303|PubMed:12589433};
GN ORFNames=SPCC1322.08 {ECO:0000312|PomBase:SPCC1322.08};
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], FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND PHOSPHORYLATION.
RX PubMed=12080074; DOI=10.1074/jbc.m204593200;
RA Smith D.A., Toone W.M., Chen D., Baehler J., Jones N., Morgan B.A.,
RA Quinn J.;
RT "The Srk1 protein kinase is a target for the Sty1 stress-activated MAPK in
RT fission yeast.";
RL J. Biol. Chem. 277:33411-33421(2002).
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 FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH STY1.
RX PubMed=12589433; DOI=10.1007/s00438-002-0786-y;
RA Asp E., Sunnerhagen P.;
RT "Mkp1 and Mkp2, two MAPKAP-kinase homologues in Schizosaccharomyces pombe,
RT interact with the MAP kinase Sty1.";
RL Mol. Genet. Genomics 268:585-597(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LYS-153.
RX PubMed=15629716; DOI=10.1016/j.molcel.2004.11.043;
RA Lopez-Aviles S., Grande M., Gonzalez M., Helgesen A.L., Alemany V.,
RA Sanchez-Piris M., Bachs O., Millar J.B., Aligue R.;
RT "Inactivation of the Cdc25 phosphatase by the stress-activated Srk1 kinase
RT in fission yeast.";
RL Mol. Cell 17:49-59(2005).
CC -!- FUNCTION: Delays the mitotic G2/M transition by promoting nuclear
CC exclusion of cdc25 (PubMed:15629716, PubMed:12080074). During osmotic
CC stress, inhibits the G2/M transition in a sty1 stress-activated MAPK
CC pathway-dependent manner (PubMed:15629716, PubMed:12080074,
CC PubMed:12589433). {ECO:0000269|PubMed:12080074,
CC ECO:0000269|PubMed:12589433, ECO:0000269|PubMed:15629716}.
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=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:15629716};
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=2.7.11.1; Evidence={ECO:0000269|PubMed:15629716};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15629716};
CC -!- INTERACTION:
CC O94547; Q09892: sty1; NbExp=3; IntAct=EBI-3648527, EBI-3648525;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12080074,
CC ECO:0000269|PubMed:12589433}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:12080074, ECO:0000269|PubMed:15629716}. Spore core
CC {ECO:0000269|PubMed:12589433}. Note=Translocates from the cytoplasm to
CC the nucleus during environmental stress in a sty1-dependent manner.
CC {ECO:0000269|PubMed:12080074}.
CC -!- INDUCTION: Induced during environmental stress.
CC {ECO:0000269|PubMed:12080074}.
CC -!- PTM: Phosphorylated by sty1. {ECO:0000269|PubMed:12080074,
CC ECO:0000269|PubMed:12589433}.
CC -!- DISRUPTION PHENOTYPE: Decreases the interaction between rad24 and cdc25
CC (PubMed:15629716). Small cells at septation (PubMed:15629716).
CC Sensitive to osmotic stress (PubMed:15629716).
CC {ECO:0000269|PubMed:15629716}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAA22861.1; -; Genomic_DNA.
DR PIR; T40939; T40939.
DR RefSeq; NP_588136.1; NM_001023126.2.
DR AlphaFoldDB; O94547; -.
DR SMR; O94547; -.
DR BioGRID; 275600; 40.
DR IntAct; O94547; 1.
DR STRING; 4896.SPCC1322.08.1; -.
DR iPTMnet; O94547; -.
DR MaxQB; O94547; -.
DR PaxDb; O94547; -.
DR PRIDE; O94547; -.
DR EnsemblFungi; SPCC1322.08.1; SPCC1322.08.1:pep; SPCC1322.08.
DR GeneID; 2539027; -.
DR KEGG; spo:SPCC1322.08; -.
DR PomBase; SPCC1322.08; srk1.
DR VEuPathDB; FungiDB:SPCC1322.08; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_006421_1_0_1; -.
DR InParanoid; O94547; -.
DR OMA; MAAIQNF; -.
DR PhylomeDB; O94547; -.
DR PRO; PR:O94547; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0042764; C:ascospore-type prospore; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:PomBase.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Meiosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..580
FT /note="Serine/threonine-protein kinase srk1"
FT /id="PRO_0000086680"
FT DOMAIN 124..421
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 51..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 130..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 153
FT /note="K->A: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:15629716"
SQ SEQUENCE 580 AA; 66136 MW; 85BA8DA3C0ED405B CRC64;
MRFKSIQQNI EDEGKVNVRE VNPDSYAERD HGYTAGIFSD AEENFGITQQ VADSTQNPTS
KPKSRHAHFH ETVHENPSEY SRSKCKQPTN EKEYDKAIEA LVAKAIVEEH SGQQFPVYKG
LEQYTLLQKM GDGAFSNVYK AIHNRTGEKV AIKVVQRAQP NTDPRDPRKR QGVESHNILK
EVQIMRRVKH PNIIQLLEFI QTPEYYYLVL ELADGGELFH QIVRLTYFSE DLSRHVITQV
AHAIRYLHED CGVVHRDIKP ENLLFDSIDF VPSRVRKYRA GDDPDKVDEG EFIPGVGAGT
IGRIRLADFG LSKVVWDSHT QTPCGTMGYT APEIVRDERY SKGVDMWALG CVLYTILCGF
PPFYDESISL LTKKVSRGEY SFLSPWWDDI SKSAKDLISH LLTVDPESRY DIHQFLAHPW
ISGSREPTFP ATDAPNTAQR ENPFTYDFLE PEDVAAAGSA ARTPGVNSLR EVFNISYAAH
RMEQEKIRKR GQRGNQGIMN FMGDMDDLME ENDDYDDGTK SVEHSMKRVN LSGENDPSLA
SRQPAQSQQQ SSQRSRNKFK GFQLNLSKAT LYNRRHRQKV
