KCC2_SCHPO
ID KCC2_SCHPO Reviewed; 504 AA.
AC O42844;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type II;
DE Short=CAM kinase II;
DE EC=2.7.11.17 {ECO:0000269|PubMed:12135745};
GN Name=cmk2 {ECO:0000303|PubMed:12135745, ECO:0000312|PomBase:SPAC23A1.06c};
GN ORFNames=SPAC23A1.06c {ECO:0000312|PomBase:SPAC23A1.06c};
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 [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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RX PubMed=12135745; DOI=10.1016/s0014-5793(02)03006-5;
RA Alemany V., Sanchez-Piris M., Bachs O., Aligue R.;
RT "Cmk2, a novel serine/threonine kinase in fission yeast.";
RL FEBS Lett. 524:79-86(2002).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-252, AND IDENTIFICATION BY
RP 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: Has a role in the regulation of G2/M transition during the
CC mitotic cell cycle. {ECO:0000269|PubMed:12135745,
CC ECO:0000269|PubMed:12589433}.
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=2.7.11.17;
CC Evidence={ECO:0000269|PubMed:12135745};
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=2.7.11.17; Evidence={ECO:0000269|PubMed:12135745};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12135745};
CC -!- SUBUNIT: Interacts with sty1. {ECO:0000269|PubMed:12589433}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12135745,
CC ECO:0000269|PubMed:12589433}. Barrier septum
CC {ECO:0000269|PubMed:12589433}. Forespore membrane
CC {ECO:0000269|PubMed:12589433}. Ascus epiplasm
CC {ECO:0000269|PubMed:12589433}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:12135745,
CC ECO:0000269|PubMed:18257517}.
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; CU329670; CAA16980.1; -; Genomic_DNA.
DR PIR; T38226; T38226.
DR RefSeq; NP_594436.1; NM_001019865.2.
DR AlphaFoldDB; O42844; -.
DR SMR; O42844; -.
DR BioGRID; 278467; 35.
DR STRING; 4896.SPAC23A1.06c.1; -.
DR iPTMnet; O42844; -.
DR MaxQB; O42844; -.
DR PaxDb; O42844; -.
DR PRIDE; O42844; -.
DR EnsemblFungi; SPAC23A1.06c.1; SPAC23A1.06c.1:pep; SPAC23A1.06c.
DR GeneID; 2541982; -.
DR KEGG; spo:SPAC23A1.06c; -.
DR PomBase; SPAC23A1.06c; cmk2.
DR VEuPathDB; FungiDB:SPAC23A1.06c; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_006421_3_2_1; -.
DR InParanoid; O42844; -.
DR OMA; SKNVDMW; -.
DR PhylomeDB; O42844; -.
DR PRO; PR:O42844; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0072324; C:ascus epiplasm; IDA:PomBase.
DR GO; GO:0005938; C:cell cortex; IDA:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein 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:0034599; P:cellular response to oxidative stress; IMP:PomBase.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; 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; Calmodulin-binding; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..504
FT /note="Calcium/calmodulin-dependent protein kinase type II"
FT /id="PRO_0000086104"
FT DOMAIN 65..351
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 366..?
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 71..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 504 AA; 56609 MW; 90929078D9F0DEBB CRC64;
MSILAGFKNL LKHSKSSKGR SNASKSVDVS VNRDVAAYTE LAAKNVNAGG DEEIRVANYP
GLEKYQLIEN LGDGAFSQVY KAYSIDRKEH VAVKVIRKYE MNKKQRQGVF KEVNIMRRVK
HKNVVNLFDF VETEDFYHLV MELAEGGELF HQIVNFTYFS ENLARHIIIQ VAEAVKHLHD
VCGIVHRDIK PENLLFQPIE YLPSQNYTPP SLEPNKLDEG MFLEGIGAGG IGRILIADFG
FSKVVWNSKT ATPCGTVGYA APEIVNDELY SKNVDMWAMG CVLHTMLCGF PPFFDENIKD
LASKVVNGEF EFLSPWWDDI SDSAKDLITH LLTVDPRERY DIHQFFQHPW IKGESKMPEN
FTYKPKLHGT PGGPKLSLPR SLVSKGEIDI PTTPIKSATH PLLSSYSEPK TPGVSSVHEA
MGVAYDIRRL NHLGFSPEQL SKKSMNTGSI KELILDEETT TDDDDYIISS FPLNDTLGSE
GKDPFSLNLK ESSLYSRRSA KRVN
