ID   PCK2_SCHPO              Reviewed;        1016 AA.
AC   P36583; Q9UU42;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   02-SEP-2026, entry version 215.
DE   RecName: Full=Protein kinase C-like 2;
DE            EC=2.7.11.13;
GN   Name=pck2; Synonyms=pkc1, sts6; ORFNames=SPBC12D12.04c;
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=8491190; DOI=10.1002/j.1460-2075.1993.tb05848.x;
RA   Toda T., Shimanuki M., Yanagida M.;
RT   "Two novel protein kinase C-related genes of fission yeast are essential
RT   for cell viability and implicated in cell shape control.";
RL   EMBO J. 12:1987-1995(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8463273; DOI=10.1016/s0021-9258(18)53188-4;
RA   Mazzei G.J., Schmid E.M., Knowles J.K., Payton M.A., Maundrell K.G.;
RT   "A Ca(2+)-independent protein kinase C from fission yeast.";
RL   J. Biol. Chem. 268:7401-7406(1993).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 755-928.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [5]
RP   INTERACTION WITH RHO2.
RX   PubMed=11102532; DOI=10.1091/mbc.11.12.4393;
RA   Calonge T.M., Nakano K., Arellano M., Arai R., Katayama S., Toda T.,
RA   Mabuchi I., Perez P.;
RT   "Schizosaccharomyces pombe rho2p GTPase regulates cell wall alpha-glucan
RT   biosynthesis through the protein kinase pck2p.";
RL   Mol. Biol. Cell 11:4393-4401(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-984, 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: Involved in the control of the cell shape. Target of the
CC       inhibitor staurosporine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=2.7.11.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC   -!- SUBUNIT: Interacts with rho2. {ECO:0000269|PubMed:11102532}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000305}.
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DR   EMBL; D14338; BAA03268.1; -; Genomic_DNA.
DR   EMBL; L07637; AAA35323.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA22678.1; -; Genomic_DNA.
DR   EMBL; AB027824; BAA87128.1; -; Genomic_DNA.
DR   PIR; A46079; A46079.
DR   RefSeq; NP_595950.1; NM_001021859.3.
DR   AlphaFoldDB; P36583; -.
DR   SMR; P36583; -.
DR   BioGRID; 276204; 35.
DR   FunCoup; P36583; 212.
DR   STRING; 284812.P36583; -.
DR   iPTMnet; P36583; -.
DR   PaxDb; 284812-P36583; -.
DR   GeneID; 2539649; -.
DR   KEGG; spo:2539649; -.
DR   PomBase; SPBC12D12.04c; pck2.
DR   VEuPathDB; FungiDB:SPBC12D12.04c; -.
DR   eggNOG; KOG0694; Eukaryota.
DR   HOGENOM; CLU_000288_54_1_1; -.
DR   InParanoid; P36583; -.
DR   OMA; QCTHLVP; -.
DR   PhylomeDB; P36583; -.
DR   BRENDA; 2.7.11.13; 5613.
DR   Reactome; R-SPO-114508; Effects of PIP2 hydrolysis.
DR   Reactome; R-SPO-114516; Disinhibition of SNARE formation.
DR   Reactome; R-SPO-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-SPO-1489509; DAG and IP3 signaling.
DR   Reactome; R-SPO-202424; Downstream TCR signaling.
DR   Reactome; R-SPO-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-SPO-2179392; EGFR Transactivation by Gastrin.
DR   Reactome; R-SPO-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-SPO-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-SPO-4419969; Depolymerization of the Nuclear Lamina.
DR   Reactome; R-SPO-5218921; VEGFR2 mediated cell proliferation.
DR   Reactome; R-SPO-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-SPO-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-SPO-5668599; RHO GTPases Activate NADPH Oxidases.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-76005; Response to elevated platelet cytosolic Ca2+.
DR   Reactome; R-SPO-8980692; RHOA GTPase cycle.
DR   Reactome; R-SPO-9013106; RHOC GTPase cycle.
DR   Reactome; R-SPO-9634635; Estrogen-stimulated signaling through PRKCZ.
DR   Reactome; R-SPO-9856530; High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells.
DR   PRO; PR:P36583; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005938; C:cell cortex; ISS:PomBase.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0051286; C:cell tip; HDA:PomBase.
DR   GO; GO:0000935; C:division septum; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; TAS:PomBase.
DR   GO; GO:0008289; F:lipid binding; ISM: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:0009272; P:fungal-type cell wall biogenesis; IMP: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:1903139; P:positive regulation of cell integrity MAPK cascade; IMP:PomBase.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:UniProtKB-ARBA.
DR   GO; GO:0090334; P:regulation of cell wall (1->3)-beta-D-glucan biosynthetic process; IMP:PomBase.
DR   GO; GO:2000769; P:regulation of establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR   GO; GO:0070610; P:regulation of fungal-type cell wall (1->3)-alpha-glucan biosynthetic process; IMP:PomBase.
DR   CDD; cd20822; C1_ScPKC1-like_rpt1; 1.
DR   CDD; cd20823; C1_ScPKC1-like_rpt2; 1.
DR   CDD; cd08689; C2_fungal_Pkc1p; 1.
DR   CDD; cd11621; HR1_PKC-like_1_fungi; 1.
DR   CDD; cd11620; HR1_PKC-like_2_fungi; 1.
DR   CDD; cd05570; STKc_PKC; 1.
DR   FunFam; 1.10.287.160:FF:000004; Protein kinase C; 1.
DR   FunFam; 1.10.510.10:FF:000101; Protein kinase C; 1.
DR   FunFam; 3.30.200.20:FF:000103; Protein kinase C; 1.
DR   FunFam; 3.30.60.20:FF:000014; Protein kinase C; 1.
DR   FunFam; 3.30.60.20:FF:000034; Protein kinase C; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 1.10.287.160; HR1 repeat; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037778; C2_fungal_PKC.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036274; HR1_rpt_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR037312; PKC-like_HR1.
DR   InterPro; IPR002219; PKC_DAG/PE.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF02185; HR1; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00742; Hr1; 2.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF46585; HR1 repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51860; REM_1; 2.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell shape; Coiled coil; Kinase; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1016
FT                   /note="Protein kinase C-like 2"
FT                   /id="PRO_0000055741"
FT   DOMAIN          1..68
FT                   /note="REM-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          111..188
FT                   /note="REM-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT   DOMAIN          195..307
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          683..942
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          943..1013
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   ZN_FING         405..453
FT                   /note="Phorbol-ester/DAG-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   ZN_FING         473..523
FT                   /note="Phorbol-ester/DAG-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          68..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..101
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..568
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..590
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        808
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         689..697
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         712
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         984
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        152
FT                   /note="E -> V (in Ref. 1; BAA03268)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1016 AA;  116005 MW;  060CDC4F718A0069 CRC64;
     MDMIDEAITE VVRKIERERS VIHGALSMKR LTQNQTVHQQ LHSNIEESKK SIIYLEERLE
     KLKLRKNGVR KSNSEKPSVG IEKNPSFSTT KSAKSFSSTS SNIDSNLDLL NYDTPLTISK
     ISFLLQQLEF KLSVEEQYRK GIEKMAKLYE REHDRRSIAE AEKKYVESAQ KITLLKQALK
     RYHDLHIEID EEDVPSTESR GNLNARRPQS GLLKITVGSL RNVTHSAGIS KQTEMIVAIR
     AEDLERARTR PSRTDRFNET FEIDLEKTNE VEIVVYEKKN EKLLLPVGLL WIRLSDLVEK
     QRRKKVEQEV SDKGWVSADK MINQRLSIFL PSALNNISKP ESTDRPNTAS GNQSVSAWFS
     LEPMGQINLT MNFTKHNTRK RPMDAGLGRQ GAIRQRKESV HEVYGHKFLQ HQFYQIMRCA
     LCGEFLKNAA GMQCIDCHYT CHKKCYPKVV TKCISKSSDS ASSEYEKINH RIPHHFESHT
     NIGANWCCHC GYILPLGRKT ARKCTECGIT AHAQCVHLVP DFCGMSMEMA NRVISEIRTT
     KIYKAQQHKQ KSSHHKHHHH KKSKSSSSKH KENDKASVSI TTTTTPSITP ADPVPTSPKP
     LAIEPVKRKP VHAGNLEVTS VSDNKLGATV QVVEQKVDDK ADALTKPPSL DAVKEPIPVP
     SVETSVVAQD LTHKAKRIGL EDFTFLSVLG KGNFGKVMLA ELKSEKQLYA IKVLKKEFIL
     ENDEVESTKS EKRVFLVANR ERHPFLVNLH SCFQTETRIY FVMDFVSGGD LMLHIQQEQF
     SRRRAQFYAA EVCLALKYFH DNGIIYRDLK LDNILLSPDG HVKVADYGLC KEDMWHDNTT
     ATFCGTPEFM APEILLEQQY TRSVDWWAFG VLIYQMLLGQ SPFRGEDEEE IFDAILSDEP
     LYPIHMPRDS VSILQQLLTR DPKKRLGSGP NDAEDVMTHP FFSNINWDDI YHKRTQPPYI
     PSLNSPTDTK YFDEEFTREL PVLTPVNSIL TKEMQQHFEG FSYSCEDDKP STTDNA
//