KPC1_CAEEL
ID KPC1_CAEEL Reviewed; 704 AA.
AC P34722;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Protein kinase C-like 1;
DE Short=PKC;
DE EC=2.7.11.13;
DE AltName: Full=Tetradecanoyl phorbol acetate-resistant protein 1;
GN Name=tpa-1; ORFNames=B0545.1;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=7658466; DOI=10.1006/jmbi.1995.0449;
RA Sano T., Tabuse Y., Nishiwaki K., Miwa J.;
RT "The tpa-1 gene of Caenorhabditis elegans encodes two proteins similar to
RT Ca(2+)-independent protein kinase Cs: evidence by complete genomic and
RT complementary DNA sequences of the tpa-1 gene.";
RL J. Mol. Biol. 251:477-485(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 148-704.
RX PubMed=2538925; DOI=10.1126/science.2538925;
RA Tabuse Y., Nishiwaki K., Miwa J.;
RT "Mutations in a protein kinase C homolog confer phorbol ester resistance on
RT Caenorhabditis elegans.";
RL Science 243:1713-1716(1989).
RN [4]
RP SEQUENCE REVISION.
RA Miwa J.;
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=17891142; DOI=10.1038/nn1981;
RA Van Buskirk C., Sternberg P.W.;
RT "Epidermal growth factor signaling induces behavioral quiescence in
RT Caenorhabditis elegans.";
RL Nat. Neurosci. 10:1300-1307(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-544.
RX PubMed=19380113; DOI=10.1016/j.chom.2009.03.006;
RA Ziegler K., Kurz C.L., Cypowyj S., Couillault C., Pophillat M., Pujol N.,
RA Ewbank J.J.;
RT "Antifungal innate immunity in C. elegans: PKCdelta links G protein
RT signaling and a conserved p38 MAPK cascade.";
RL Cell Host Microbe 5:341-352(2009).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF LYS-404.
RX PubMed=23072806; DOI=10.1038/ncomms2136;
RA Pastuhov S.I., Fujiki K., Nix P., Kanao S., Bastiani M., Matsumoto K.,
RA Hisamoto N.;
RT "Endocannabinoid-Goalpha signalling inhibits axon regeneration in
RT Caenorhabditis elegans by antagonizing Gqalpha-PKC-JNK signalling.";
RL Nat. Commun. 3:1136-1136(2012).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-384.
RX PubMed=22470487; DOI=10.1371/journal.pone.0033887;
RA Labed S.A., Omi S., Gut M., Ewbank J.J., Pujol N.;
RT "The pseudokinase NIPI-4 is a novel regulator of antimicrobial peptide gene
RT expression.";
RL PLoS ONE 7:E33887-E33887(2012).
CC -!- FUNCTION: Diacylglycerol (DAG)-dependent serine/threonine-protein
CC kinase that phosphorylates a range of cellular proteins (Probable).
CC Phosphorylates mlk-1, a component of the JNK pathway. Involved in axon
CC regeneration after injury probably by activating the JNK pathway
CC (PubMed:23072806). Plays a role in resistance to fungal infection and
CC in wound healing by promoting expression of antimicrobial peptide nlp-
CC 29 in the epidermis downstream of gpa-12 and plc-3 and upstream of tir-
CC 1-p38-like pathway (PubMed:22470487, PubMed:19380113). Probably by
CC regulating neuronal transmission in ALA neurons, regulates the decrease
CC in pharyngeal pumping during the quiescent state that precedes each
CC larval molt, downstream of lin-3 and receptor let-23 and phospholipase
CC plc-3 (PubMed:17891142). {ECO:0000269|PubMed:17891142,
CC ECO:0000269|PubMed:19380113, ECO:0000269|PubMed:22470487,
CC ECO:0000269|PubMed:23072806, ECO:0000305}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P34722-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34722-2; Sequence=VSP_004744;
CC -!- DISRUPTION PHENOTYPE: Up-regulation of nlp-29 is severely impaired in
CC the hyp7 and vulva epidermal cells following fungal infection by
CC D.coniospora or physical injury. {ECO:0000269|PubMed:19380113}.
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; D49525; BAA08470.1; -; Genomic_DNA.
DR EMBL; D49525; BAA08471.1; -; Genomic_DNA.
DR EMBL; FO080226; CCD62171.1; -; Genomic_DNA.
DR EMBL; FO080226; CCD62172.1; -; Genomic_DNA.
DR EMBL; D14815; BAA03556.1; -; mRNA.
DR PIR; S60117; S60117.
DR PIR; T33400; T33400.
DR RefSeq; NP_499860.1; NM_067459.3.
DR RefSeq; NP_499861.1; NM_067460.4.
DR AlphaFoldDB; P34722; -.
DR SMR; P34722; -.
DR BioGRID; 41988; 7.
DR STRING; 6239.B0545.1a; -.
DR iPTMnet; P34722; -.
DR EPD; P34722; -.
DR PaxDb; P34722; -.
DR PeptideAtlas; P34722; -.
DR EnsemblMetazoa; B0545.1a.1; B0545.1a.1; WBGene00006599. [P34722-1]
DR EnsemblMetazoa; B0545.1b.1; B0545.1b.1; WBGene00006599. [P34722-2]
DR EnsemblMetazoa; B0545.1b.2; B0545.1b.2; WBGene00006599. [P34722-2]
DR EnsemblMetazoa; B0545.1b.3; B0545.1b.3; WBGene00006599. [P34722-2]
DR UCSC; B0545.1a; c. elegans. [P34722-1]
DR WormBase; B0545.1a; CE17353; WBGene00006599; tpa-1. [P34722-1]
DR WormBase; B0545.1b; CE17354; WBGene00006599; tpa-1. [P34722-2]
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000169708; -.
DR InParanoid; P34722; -.
DR OMA; ENACRLK; -.
DR OrthoDB; 222529at2759; -.
DR PhylomeDB; P34722; -.
DR BRENDA; 2.7.11.13; 1045.
DR Reactome; R-CEL-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-CEL-111933; Calmodulin induced events.
DR Reactome; R-CEL-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-CEL-1489509; DAG and IP3 signaling.
DR Reactome; R-CEL-202424; Downstream TCR signaling.
DR Reactome; R-CEL-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-CEL-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-CEL-373752; Netrin-1 signaling.
DR Reactome; R-CEL-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-CEL-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-9648002; RAS processing.
DR PRO; PR:P34722; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006599; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IGI:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IMP: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; 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; IPR017892; Pkinase_C.
DR InterPro; IPR014376; Prot_kin_PKC_delta.
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; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000551; PKC_delta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
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; 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..704
FT /note="Protein kinase C-like 1"
FT /id="PRO_0000055734"
FT DOMAIN 375..634
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 635..704
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 165..215
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 237..287
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ACT_SITE 499
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 381..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 89
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 139
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 324
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..137
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_004744"
FT MUTAGEN 384
FT /note="G->E: Severe loss of nlp-29 expression upon
FT D.coniospora infection."
FT /evidence="ECO:0000269|PubMed:22470487"
FT MUTAGEN 404
FT /note="K->R: Probable loss of kinase activity. Loss of mlk-
FT 1 phosphorylation."
FT /evidence="ECO:0000269|PubMed:23072806"
FT MUTAGEN 544
FT /note="P->S: In k501; normal up-regulation of nlp-29 upon
FT D.coniospora infection or physical injury."
FT /evidence="ECO:0000269|PubMed:19380113"
SQ SEQUENCE 704 AA; 80298 MW; C44F2E25F58057E3 CRC64;
MAQAENACRL KLLRADVPVD LLPAGCSATD LQPAVNVKEK IEVNGESRLV QKKKTLYPEW
EKCWDTAVAE GRILQIVLMF NQTPVVEATM RLEDIISKCK SDAITHIWIN TKPNGRILAQ
TRHLKNAPDD DHPVEDIMTS RSNSGPGIQR RRGAIKHARV HEIRGHQFVA TFFRQPHFCS
LCSDFMWGLN KQGYQCQLCS AAVHKKCHEK VIMQCPGSAK NTKETMALKE RFKVDIPHRF
KTYNFKSPTF CDHCGSMLYG LFKQGLRCEV CNVACHHKCE RLMSNLCGVN QKQLSEMYHE
IKRGTHATAS CPPNIANLHL NGETSKNNGS LPNKLKNLFK SHQYSVEEQK ETDEYMDNIW
GGGDGPVKKF ALPHFNLLKV LGKGSFGKVM LVELKGKNEF YAMKCLKKDV ILEDDDTECT
YIERRVLILA SQCPFLCQLF CSFQTNEYLF FVMEYLNGGD LMHHIQQIKK FDEARTRFYA
CEIVVALQFL HTNNIIYRDL KLDNVLLDCD GHIKLADFGM AKTEMNRENG MASTFCGTPD
YISPEIIKGQ LYNEAVDFWS FGVLMYEMLV GQSPFHGEGE DELFDSILNE RPYFPKTISK
EAAKCLSALF DRNPNTRLGM PECPDGPIRQ HCFFRGVDWK RFENRQVPPP FKPNIKSNSD
ASNFDDDFTN EKAALTPVHD KNLLASIDPE AFLNFSYTNP HFSK
