PCK2_SCHPO
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 03-AUG-2022, entry version 197.
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=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=2.7.11.13;
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=2.7.11.13;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_001021859.2.
DR AlphaFoldDB; P36583; -.
DR SMR; P36583; -.
DR BioGRID; 276204; 34.
DR STRING; 4896.SPBC12D12.04c.1; -.
DR iPTMnet; P36583; -.
DR MaxQB; P36583; -.
DR PaxDb; P36583; -.
DR PRIDE; P36583; -.
DR EnsemblFungi; SPBC12D12.04c.1; SPBC12D12.04c.1:pep; SPBC12D12.04c.
DR GeneID; 2539649; -.
DR KEGG; spo:SPBC12D12.04c; -.
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; NRIYFAM; -.
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; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-SPO-450520; HuR (ELAVL1) binds and stabilizes mRNA.
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-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
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-9013026; RHOB GTPase cycle.
DR Reactome; R-SPO-9013106; RHOC GTPase cycle.
DR Reactome; R-SPO-9634635; Estrogen-stimulated signaling through PRKCZ.
DR PRO; PR:P36583; -.
DR Proteomes; UP000002485; Chromosome II.
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:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004697; F:protein kinase C activity; TAS: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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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; cd00029; C1; 2.
DR CDD; cd08689; C2_fungal_Pkc1p; 1.
DR CDD; cd11620; HR1_PKC-like_2_fungi; 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; IPR002219; PE/DAG-bd.
DR InterPro; IPR037312; PKC-like_HR1.
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 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; SSF46585; SSF46585; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
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 78..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..566
FT /note="Basic residues"
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
