KPC1B_CAEEL
ID KPC1B_CAEEL Reviewed; 707 AA.
AC P34885; G3MU31; Q20953;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Protein kinase C-like 1B;
DE Short=PKC1B;
DE EC=2.7.11.13;
GN Name=pkc-1; Synonyms=kin-13, pkc-1b, ttx-4; ORFNames=F57F5.5;
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], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11
RP (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=8132661; DOI=10.1016/s0021-9258(17)37099-0;
RA Land M., Islas-Trejo A., Freedman J.H., Rubin C.S.;
RT "Structure and expression of a novel, neuronal protein kinase C (PKC1B)
RT from Caenorhabditis elegans. PKC1B is expressed selectively in neurons that
RT receive, transmit, and process environmental signals.";
RL J. Biol. Chem. 269:9234-9244(1994).
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).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=IK105;
RX PubMed=15920475; DOI=10.1038/sj.emboj.7600697;
RA Okochi Y., Kimura K.D., Ohta A., Mori I.;
RT "Diverse regulation of sensory signaling by C. elegans nPKC-epsilon/eta
RT TTX-4.";
RL EMBO J. 24:2127-2137(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=IK130;
RX PubMed=17128266; DOI=10.1038/nn1810;
RA Sieburth D., Madison J.M., Kaplan J.M.;
RT "PKC-1 regulates secretion of neuropeptides.";
RL Nat. Neurosci. 10:49-57(2007).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=IK130;
RX PubMed=20837997; DOI=10.1534/genetics.110.119768;
RA Adachi T., Kunitomo H., Tomioka M., Ohno H., Okochi Y., Mori I., Iino Y.;
RT "Reversal of salt preference is directed by the insulin/PI3K and Gq/PKC
RT signaling in Caenorhabditis elegans.";
RL Genetics 186:1309-1319(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=IK105;
RX PubMed=20089839; DOI=10.1091/mbc.e09-08-0673;
RA Zubovych I.O., Straud S., Roth M.G.;
RT "Mitochondrial dysfunction confers resistance to multiple drugs in
RT Caenorhabditis elegans.";
RL Mol. Biol. Cell 21:956-969(2010).
RN [7]
RP FUNCTION.
RC STRAIN=IK130;
RX PubMed=21933341; DOI=10.1111/j.1474-9726.2011.00747.x;
RA Monje J.M., Brokate-Llanos A.M., Perez-Jimenez M.M., Fidalgo M.A.,
RA Munoz M.J.;
RT "pkc-1 regulates daf-2 insulin/IGF signalling-dependent control of dauer
RT formation in Caenorhabditis elegans.";
RL Aging Cell 10:1021-1031(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=RB781;
RX PubMed=21143768; DOI=10.1111/j.1601-183x.2010.00667.x;
RA Hyde R., Corkins M.E., Somers G.A., Hart A.C.;
RT "PKC-1 acts with the ERK MAPK signaling pathway to regulate Caenorhabditis
RT elegans mechanosensory response.";
RL Genes Brain Behav. 10:286-298(2011).
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. Involved in
CC neuropeptide secretion in motor axons. Likely to act via the
CC extracellular signal-regulated kinase/mitogen-activated protein kinase
CC (ERK/MAPK) pathway in the signaling response to various sensory
CC neurons; temperature, odor, taste, and osmolality. Its role in
CC regulation differs depending on the neuron in which it is acting;
CC thermosensation in AFD neurons, osmolality in ASH neurons, olfactory
CC perception in AWA and AWC neurons. Promotes dauer formation mediated by
CC the insulin/IGF pathway. Required for resistance to antimitotic toxins.
CC {ECO:0000269|PubMed:15920475, ECO:0000269|PubMed:17128266,
CC ECO:0000269|PubMed:20089839, ECO:0000269|PubMed:21143768,
CC ECO:0000269|PubMed:21933341}.
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 -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cytoplasm,
CC cytoskeleton. Note=Associated with membranes and the cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P34885-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34885-2; Sequence=VSP_044041;
CC -!- TISSUE SPECIFICITY: Expressed selectively in neurons that receive,
CC transmit and process environmental signals.
CC -!- DISRUPTION PHENOTYPE: Attenuated response to nose touch stimulation.
CC Defects in salt attraction. Disrupted chemotaxis. Hyperactivation of
CC AFD thermosensory neurons but inactivation of the ASH neurons. Reduced
CC dauer formation. Protection from hemiasterlin toxicity by carbonyl
CC cyanide p-[trifluoromethoxy]-phenyl-hydrazone (FCCP) greatly reduced.
CC Reduced neuropeptide secretion. {ECO:0000269|PubMed:15920475,
CC ECO:0000269|PubMed:17128266, ECO:0000269|PubMed:20089839,
CC ECO:0000269|PubMed:20837997, ECO:0000269|PubMed:21143768}.
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; U00181; AAA18259.1; -; mRNA.
DR EMBL; U00965; AAA17996.1; -; Genomic_DNA.
DR EMBL; Z75953; CAB00101.2; -; Genomic_DNA.
DR EMBL; Z81497; CAB00101.2; JOINED; Genomic_DNA.
DR EMBL; Z75953; CCD31083.1; -; Genomic_DNA.
DR PIR; A53530; A53530.
DR PIR; T22856; T22856.
DR RefSeq; NP_001256394.1; NM_001269465.1. [P34885-2]
DR RefSeq; NP_001256395.1; NM_001269466.1. [P34885-1]
DR AlphaFoldDB; P34885; -.
DR SMR; P34885; -.
DR BioGRID; 44672; 2.
DR DIP; DIP-27455N; -.
DR STRING; 6239.F57F5.5c; -.
DR iPTMnet; P34885; -.
DR EPD; P34885; -.
DR PaxDb; P34885; -.
DR PeptideAtlas; P34885; -.
DR EnsemblMetazoa; F57F5.5a.1; F57F5.5a.1; WBGene00004032. [P34885-1]
DR EnsemblMetazoa; F57F5.5a.2; F57F5.5a.2; WBGene00004032. [P34885-1]
DR EnsemblMetazoa; F57F5.5a.3; F57F5.5a.3; WBGene00004032. [P34885-1]
DR EnsemblMetazoa; F57F5.5b.1; F57F5.5b.1; WBGene00004032. [P34885-2]
DR GeneID; 179649; -.
DR UCSC; F57F5.5; c. elegans. [P34885-1]
DR CTD; 179649; -.
DR WormBase; F57F5.5a; CE29092; WBGene00004032; pkc-1. [P34885-1]
DR WormBase; F57F5.5b; CE46445; WBGene00004032; pkc-1. [P34885-2]
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000168328; -.
DR InParanoid; P34885; -.
DR PhylomeDB; P34885; -.
DR BRENDA; 2.7.11.13; 1045.
DR Reactome; R-CEL-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-CEL-1489509; DAG and IP3 signaling.
DR Reactome; R-CEL-2029485; Role of phospholipids in phagocytosis.
DR PRO; PR:P34885; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004032; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; P34885; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IMP:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
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:0004697; F:protein kinase C activity; IDA:WormBase.
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:0008306; P:associative learning; IMP:UniProtKB.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IMP:WormBase.
DR GO; GO:0040024; P:dauer larval development; IMP:UniProtKB.
DR GO; GO:1990504; P:dense core granule exocytosis; IMP:WormBase.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR GO; GO:2001024; P:negative regulation of response to drug; IMP:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IMP:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:WormBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; NAS:UniProtKB.
DR GO; GO:0050920; P:regulation of chemotaxis; IGI:UniProtKB.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR GO; GO:1902074; P:response to salt; IMP:UniProtKB.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IMP:UniProtKB.
DR GO; GO:0050975; P:sensory perception of touch; IMP:UniProtKB.
DR GO; GO:0050893; P:sensory processing; IMP:UniProtKB.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:UniProtKB.
DR CDD; cd00029; C1; 2.
DR CDD; cd05591; STKc_nPKC_epsilon; 1.
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; IPR034669; nPKC_epsilon.
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; PF00168; C2; 1.
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; 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; Cytoplasm; Cytoskeleton; Kinase;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..707
FT /note="Protein kinase C-like 1B"
FT /id="PRO_0000055735"
FT DOMAIN 1..114
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 378..638
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 639..707
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 170..220
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 248..298
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 323..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 502
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 384..392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 2..134
FT /note="LFTGTVRVRVLEARQLRPTEWSRRFRQDEAATAAIDSYVNVDWDEYHIGKTQ
FT VRPKTNEPRWNEEFTASGVHQGKAIGFSVFHSCVMPPDDFVANTRIAFDQLKIGSANDI
FT WVDLEPHGQLHVVVEMHGTNVE -> SFDCLVYDEYAPSSKSRNSSNKAKVKKKNSWGF
FT WVKQDSTSSSSFH (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_044041"
FT CONFLICT 180..181
FT /note="QP -> HA (in Ref. 1; AAA18259)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="I -> T (in Ref. 1; AAA18259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 80151 MW; 08C1BD1B7A911B49 CRC64;
MLFTGTVRVR VLEARQLRPT EWSRRFRQDE AATAAIDSYV NVDWDEYHIG KTQVRPKTNE
PRWNEEFTAS GVHQGKAIGF SVFHSCVMPP DDFVANTRIA FDQLKIGSAN DIWVDLEPHG
QLHVVVEMHG TNVEDVHSHN KTRVFKERTN AFNDRQRRGA MRRKIHEVTG HKFMALFLRQ
PTFCAHCKEF IWGIGKQGYQ CQICTVVVHK RCHEDVVWKC PGNKADAVEE LGKEIQETGA
GRFNINMPHR FSVHSYKRPT FCDHCGSMLY GLINQGLQCS TCKLNVHKRC QRNVANNCGI
NAKQMAAELA QLGLTGDKMS IRSKKKPSIM TDTSTDISGS SNSENSGYLQ QISEDDSGTT
SSRSASKVPG GTLSIHDFTF MKVLGKGSFG KVMLAERKGT DEVYAIKILK KDVIVQDDDV
ECTMCEKRIL SLAAKHPFLT ALHSSFQTSD RLFFVMEYVN GGDLMFQIQR ARKFDESRAR
FYAAEVTCAL QFLHRNDVIY RDLKLDNILL DAEGHCRLAD FGMCKEGINK DNLTSTFCGT
PDYIAPEILQ EMEYGVSVDW WALGVLMYEM MAGQPPFEAD NEDDLFEAIL NDDVLYPVWL
SKEAVNILKA FMTKNAGKRL GCVVSQGGED AIRAHPFFRE IDWDALESRQ VKPPFKPKIK
SKRDANNFDS DFTKEEPVLT PSDPAVVRAI NQDEFRGFSF INPHFTY
