KPC2_CAEEL
ID KPC2_CAEEL Reviewed; 682 AA.
AC P90980; P90981; Q19024; Q8MQ87; Q8MQ88;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Protein kinase C-like 2;
DE Short=PKC2;
DE EC=2.7.11.13;
GN Name=pkc-2; Synonyms=kin-11; ORFNames=E01H11.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC STRAIN=Bristol N2;
RX PubMed=9045693; DOI=10.1074/jbc.272.10.6629;
RA Islas-Trejo A., Land M., Tcherepanova I., Freedman J.H., Rubin C.S.;
RT "Structure and expression of the Caenorhabditis elegans protein kinase C2
RT gene. Origins and regulated expression of a family of Ca2+-activated
RT protein kinase C isoforms.";
RL J. Biol. Chem. 272:6629-6640(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: PKC is activated by diacylglycerol which in turn
CC phosphorylates a range of cellular proteins. PKC also serves as the
CC receptor for phorbol esters, a class of tumor promoters.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b; Synonyms=PKC2B;
CC IsoId=P90980-1; Sequence=Displayed;
CC Name=a; Synonyms=PKC2A;
CC IsoId=P90980-2; Sequence=VSP_009370;
CC Name=c;
CC IsoId=P90980-3; Sequence=VSP_009369, VSP_009371;
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; U82935; AAB40868.1; -; mRNA.
DR EMBL; U82936; AAB40869.1; -; mRNA.
DR EMBL; FO080629; CCD65287.1; -; Genomic_DNA.
DR EMBL; FO080629; CCD65288.1; -; Genomic_DNA.
DR EMBL; FO080629; CCD65289.1; -; Genomic_DNA.
DR PIR; T15902; T15902.
DR RefSeq; NP_001024516.1; NM_001029345.3. [P90980-2]
DR RefSeq; NP_001024517.1; NM_001029346.2. [P90980-1]
DR RefSeq; NP_001024518.1; NM_001029347.1.
DR AlphaFoldDB; P90980; -.
DR SMR; P90980; -.
DR BioGRID; 46082; 8.
DR DIP; DIP-24386N; -.
DR STRING; 6239.E01H11.1c; -.
DR EPD; P90980; -.
DR PaxDb; P90980; -.
DR PeptideAtlas; P90980; -.
DR PRIDE; P90980; -.
DR EnsemblMetazoa; E01H11.1a.1; E01H11.1a.1; WBGene00004033. [P90980-2]
DR EnsemblMetazoa; E01H11.1b.1; E01H11.1b.1; WBGene00004033. [P90980-1]
DR EnsemblMetazoa; E01H11.1c.1; E01H11.1c.1; WBGene00004033.
DR GeneID; 181166; -.
DR UCSC; E01H11.1d; c. elegans. [P90980-1]
DR CTD; 181166; -.
DR WormBase; E01H11.1a; CE30927; WBGene00004033; pkc-2. [P90980-2]
DR WormBase; E01H11.1b; CE30928; WBGene00004033; pkc-2. [P90980-1]
DR WormBase; E01H11.1c; CE30929; WBGene00004033; pkc-2. [P90980-3]
DR eggNOG; KOG0696; Eukaryota.
DR GeneTree; ENSGT00940000167637; -.
DR InParanoid; P90980; -.
DR OMA; EGEFYNI; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; P90980; -.
DR Reactome; R-CEL-111933; Calmodulin induced events.
DR Reactome; R-CEL-114516; Disinhibition of SNARE formation.
DR Reactome; R-CEL-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-CEL-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-CEL-3000170; Syndecan interactions.
DR Reactome; R-CEL-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-CEL-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-CEL-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-CEL-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-CEL-76005; Response to elevated platelet cytosolic Ca2+.
DR PRO; PR:P90980; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004033; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; P90980; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IDA:WormBase.
DR GO; GO:0004697; F:protein kinase C activity; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IDA:WormBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:WormBase.
DR CDD; cd00029; C1; 2.
DR Gene3D; 2.60.40.150; -; 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; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014375; Protein_kinase_C_a/b/g.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000550; PKC_alpha; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 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; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Calcium; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..682
FT /note="Protein kinase C-like 2"
FT /id="PRO_0000055736"
FT DOMAIN 160..278
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 348..609
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 610..681
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 38..88
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 103..153
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 312..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 354..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..13
FT /note="MSLSTNSSVKEDE -> MSLRPKQKSSSTSVFLKSHKFSLTSHILRKAKKRE
FT TMDSAERRRSETDIGGGPRNSADARPSLDLSSDPMLESNLALRKLSEAFAAAALISPVK
FT NNSTGGGGNQQLCIRKSISNPSSLKVYAHHEAPGIIHFPRFEFSHRLSIRPLLKRLHEQ
FT (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_009369"
FT VAR_SEQ 632..682
FT /note="TDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFSFVNPFYVKDVEP
FT -> SADDTSNFDSEFTHEVPKLTPIDRLFLMNLDQTEFEGFSFVNPEYVQEC (in
FT isoform a)"
FT /evidence="ECO:0000303|PubMed:9045693"
FT /id="VSP_009370"
FT VAR_SEQ 682
FT /note="P -> PHIFYVLFIFLILRPFLLLPYLSHLQLTLSAIHSPLLLLSASVFFKF
FT LFKNNFSQSPYNKIKVLLKSADDTSNFDSEFTHEVPKLTPIDRLFLMNLDQTEFEGFSF
FT VNPEYVQEC (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_009371"
FT CONFLICT 200
FT /note="C -> W (in Ref. 1; AAB40868/AAB40869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 78000 MW; E41C5C12DA38ED3C CRC64;
MSLSTNSSVK EDEAQRIEGK AFVRRGALRQ KNVHEIKSHK FIARFFKQPT FCSHCKDFLW
GITKQGFQCQ VCTLVVHKRC HEFVNFACPG ADKGVDTDDP RQQHKWKVQT YSSPTFCDHC
GSLLYGILHQ GMKCQSCDTN VHHRCVKNVP NMCGTDNTEK RGRLRIEAHI ENDQLTIKIL
EAKNLIPMDP NGLSDPYVKC KLIPEDSGCK SKQKTKTLRA TLNPQWNETF TYKLLPGDKD
RRLSIEVWDW DRTSRNDFMG SLSFGISELM KEAASGWYKL LSAEEGEFYN INITPEYDED
MEKVRKKMNE NFITRDNSSS KPKDPAAPRA STLPLGSSNH NVIKASDFNF LTVLGKGSFG
KVLLGEQKTT KELFAIKVLK KDVIIQDDDV ECTMTEKRVL ALPEKPSFLV ALHSCFQTMD
RLYFVMEFVN GGDLMYQIQQ VGKFKEPVAV FYAAEIAVGL FFLHSKGIIY RDLKLDNVML
ERDGHIKITD FGMCKENIFG DATTKTFCGT PDYIAPEIIL YQPYGKSVDW WAYGVLLFEM
LAGQPPFDGE DEDELFTAIT EHNVSYPKSL SKEAVSLCKA LLIKNPSKRL GCTGDDESAS
RDIKEHPFFR RIDWFKIETR QIQPPFKPKL KTDRSTENFD HSFLKLPTKM TPPDWEVLEN
LKGDEFSNFS FVNPFYVKDV EP
