OCA2_SCHPO
ID OCA2_SCHPO Reviewed; 650 AA.
AC O59763;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Serine/threonine-protein kinase oca2;
DE EC=2.7.11.1;
GN Name=oca2 {ECO:0000312|EMBL:CAA18998.1}; ORFNames=SPCC1020.10;
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] {ECO:0000312|EMBL:CAA18998.1}
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] {ECO:0000305}
RP FUNCTION.
RX PubMed=12237855; DOI=10.1002/yea.902;
RA Tallada V.A., Daga R.R., Palomeque C., Garzon A., Jimenez J.;
RT "Genome-wide search of Schizosaccharomyces pombe genes causing
RT overexpression-mediated cell cycle defects.";
RL Yeast 19:1139-1151(2002).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-286, 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: Overexpression causes cell cycle arrest.
CC {ECO:0000269|PubMed:12237855}.
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:0000250|UniProtKB:Q08732};
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:0000250|UniProtKB:Q08732};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Note=Barrier septum. Cell tip. {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CU329672; CAA18998.1; -; Genomic_DNA.
DR PIR; T40830; T40830.
DR RefSeq; NP_587949.1; NM_001022940.2.
DR AlphaFoldDB; O59763; -.
DR SMR; O59763; -.
DR BioGRID; 275809; 48.
DR STRING; 4896.SPCC1020.10.1; -.
DR iPTMnet; O59763; -.
DR MaxQB; O59763; -.
DR PaxDb; O59763; -.
DR PRIDE; O59763; -.
DR EnsemblFungi; SPCC1020.10.1; SPCC1020.10.1:pep; SPCC1020.10.
DR GeneID; 2539239; -.
DR KEGG; spo:SPCC1020.10; -.
DR PomBase; SPCC1020.10; oca2.
DR VEuPathDB; FungiDB:SPCC1020.10; -.
DR eggNOG; KOG0590; Eukaryota.
DR HOGENOM; CLU_000288_82_2_1; -.
DR InParanoid; O59763; -.
DR OMA; CCMALRR; -.
DR PhylomeDB; O59763; -.
DR PRO; PR:O59763; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA: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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IMP:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
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; Cell cycle; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..650
FT /note="Serine/threonine-protein kinase oca2"
FT /id="PRO_0000337145"
FT DOMAIN 302..614
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P39009,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 308..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00517,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39009,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 650 AA; 73232 MW; 568253FEF1867B7D CRC64;
MSVTPPNVQF NLNGDSDHKS DNSSSSLENK LDTELKITSP PRNPPQRLHP VDFSEHADTD
DDMNHPLPRV QSPVHIKNHI DPKLAEDRYR SSAARHFEPI SIPPSAITSE DEDDYHGSAN
SSTVLPPRTE NALHAASPKP SGSTGYTSPA LSQNSGSGGE GESDEGSFNT QHHRSPIFQA
YPSSEDLVGD PNDPYRRTRR APIKTNPHDI PSQFIFRKLG LHHGKHGHHG HSGSLSLKSL
VPNHHDKHDK HDKHEKHHSS LDLRRFFKSH QKTDKEKKPS VSKSKSSANL QDDHFGLFKK
YGKFGRMLGS GAGGSVRIMK RSSDGKIFAV KEFRARRPTE TEREYARKVT AEFCIGSALH
HTNIIETLDI VEENKKFYEV MEYAPYDMFS IVMSGKMTMP EVYCCFKQLL SGVAYLHSMG
LAHRDLKLDN LVVDSNCFVK IIDFGSAVVF KYPFEADIVE ATGVVGSDPY LAPETLVRKL
YDPRAVDIWS SAIIFCCMAL RRFPWKYPKL SDNSFRLFCM KQPSNDAESP SDILADIKKQ
RLVEQGCEPI RKTDESHSPN SKTDNSSTHK QELYGPWRLL RLLPRETRAV IAHMLELDPV
KRYDIHRVFA DNWINDISMC HMENGKVIHS PTHVHNLVAS EESPAPPAKH
