KPC3_CAEEL
ID KPC3_CAEEL Reviewed; 597 AA.
AC Q19266; A7VJC8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protein kinase C-like 3;
DE EC=2.7.11.13;
DE AltName: Full=Atypical protein kinase C-3;
DE Short=aPKC3;
GN Name=pkc-3 {ECO:0000312|WormBase:F09E5.1}; Synonyms=aPKC; ORFNames=F09E5.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PAR-3, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2; TISSUE=Embryo {ECO:0000269|PubMed:9716526};
RX PubMed=9716526; DOI=10.1242/dev.125.18.3607;
RA Tabuse Y., Izumi Y., Piano F., Kemphues K.J., Miwa J., Ohno S.;
RT "Atypical protein kinase C cooperates with PAR-3 to establish embryonic
RT polarity in Caenorhabditis elegans.";
RL Development 125:3607-3614(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAB88885.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAB88885.1};
RX PubMed=9422779; DOI=10.1074/jbc.273.2.1130;
RA Wu S.-L., Staudinger J., Olson E.N., Rubin C.S.;
RT "Structure, expression, and properties of an atypical protein kinase C
RT (PKC3) from Caenorhabditis elegans. PKC3 is required for the normal
RT progression of embryogenesis and viability of the organism.";
RL J. Biol. Chem. 273:1130-1143(1998).
RN [3]
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 [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PAR-3 AND PAR-6, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:9834192};
RC TISSUE=Embryo {ECO:0000269|PubMed:9834192};
RX PubMed=9834192; DOI=10.1242/dev.126.1.127;
RA Hung T.-J., Kemphues K.J.;
RT "PAR-6 is a conserved PDZ domain-containing protein that colocalizes with
RT PAR-3 in Caenorhabditis elegans embryos.";
RL Development 126:127-135(1999).
RN [5] {ECO:0000305}
RP INTERACTION WITH CDC-42.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:11412997};
RC TISSUE=Embryo {ECO:0000269|PubMed:11412997};
RX PubMed=11412997; DOI=10.1016/s0960-9822(01)00142-7;
RA Gotta M., Abraham M.C., Ahringer J.;
RT "CDC-42 controls early cell polarity and spindle orientation in C.
RT elegans.";
RL Curr. Biol. 11:482-488(2001).
RN [6] {ECO:0000305}
RP INTERACTION WITH NUM-1.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:11134024};
RX PubMed=11134024; DOI=10.1074/jbc.m008990200;
RA Zhang L., Wu S.-L., Rubin C.S.;
RT "A novel adapter protein employs a phosphotyrosine binding domain and
RT exceptionally basic N-terminal domains to capture and localize an atypical
RT protein kinase C: characterization of Caenorhabditis elegans C kinase
RT adapter 1, a protein that avidly binds protein kinase C3.";
RL J. Biol. Chem. 276:10463-10475(2001).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH NUM-1, AND MUTAGENESIS OF ILE-214; ASN-216;
RP PHE-219 AND HIS-222.
RX PubMed=11134025; DOI=10.1074/jbc.m008991200;
RA Zhang L., Wu S.-L., Rubin C.S.;
RT "Structural properties and mechanisms that govern association of C kinase
RT adapter 1 with protein kinase C3 and the cell periphery.";
RL J. Biol. Chem. 276:10476-10484(2001).
RN [8] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15151982; DOI=10.1242/dev.01146;
RA Aono S., Legouis R., Hoose W.A., Kemphues K.J.;
RT "PAR-3 is required for epithelial cell polarity in the distal spermatheca
RT of C. elegans.";
RL Development 131:2865-2874(2004).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Required for the normal progression of embryogenesis and
CC viability of the organism (PubMed:9422779). Plays an indispensable role
CC in establishing embryonic polarity and in recruiting and maintaining
CC par-6 to the periphery, through interaction with par-3 (PubMed:9716526,
CC PubMed:9834192). Required for epithelial cell polarity in the distal
CC spermatheca (PubMed:15151982). Phosphorylates serine residues of num-1
CC (PubMed:11134025). Required for the expression of antimicrobial peptide
CC nlp-29 in response in response to fungal infection or physical injury
CC (PubMed:19380113). {ECO:0000269|PubMed:11134025,
CC ECO:0000269|PubMed:15151982, ECO:0000269|PubMed:19380113,
CC ECO:0000269|PubMed:9422779, ECO:0000269|PubMed:9716526,
CC ECO:0000269|PubMed:9834192}.
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 Evidence={ECO:0000269|PubMed:9422779};
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; Evidence={ECO:0000269|PubMed:9422779};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Interaction with par-3 required for the peripheral
CC localization of par-6 and to form a par-3/par-6/pkc-3 complex, which is
CC activated when cdc-42 interacts with par-6. Binds avidly to the
CC phosphotyrosine interaction domain (PID) of a novel pkc-3 adapter
CC protein num-1, which enables tethering and targeting of pkc-3 to the
CC cell periphery. {ECO:0000269|PubMed:11134024,
CC ECO:0000269|PubMed:11134025, ECO:0000269|PubMed:11412997,
CC ECO:0000269|PubMed:9716526, ECO:0000269|PubMed:9834192}.
CC -!- INTERACTION:
CC Q19266; Q9XTY6: num-1; NbExp=5; IntAct=EBI-319158, EBI-495781;
CC Q19266; Q9XTY6-1: num-1; NbExp=5; IntAct=EBI-319158, EBI-495798;
CC Q19266; Q17353: par-3; NbExp=3; IntAct=EBI-319158, EBI-321762;
CC Q19266; Q9NAN2: par-6; NbExp=4; IntAct=EBI-319158, EBI-318782;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9422779,
CC ECO:0000269|PubMed:9716526}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9422779}. Note=Targeted and anchored at the apical
CC surface (villi) of intestinal and pharyngeal cells, and in proximity
CC with the cortical actin cytoskeleton that lies under the plasma
CC membrane. Tightly bound to organelles/cytoskeleton in six of the seven
CC developmental stages. Accumulation in cytoplasm is restricted to L1
CC larvae and adults. Colocalized with par-3 at the anterior cortex of the
CC 1-cell embryo. {ECO:0000269|PubMed:9422779,
CC ECO:0000269|PubMed:9716526}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the anterior and posterior
CC pharyngeal bulbs, the pharyngeal-intestinal valve, vulval cells, and a
CC region at the posterior end of the intestine that corresponds to site
CC of co-assembly of the intestinal-rectal valve and anal sphincter, and
CC depressor muscles. Modest expression apparent in four hypodermal cells
CC that provide cuticle and muscle anchorage in the tail. Strong
CC expression observed in discrete patches and spots in vulval cells and
CC in somatic cells of the spermatheca. Transiently coexpressed and
CC colocalized with par-6 and par-3, asymmetrically in the developing
CC somatic gonad, including the spermathecal precursor cells of L4 larvae.
CC {ECO:0000269|PubMed:15151982, ECO:0000269|PubMed:9422779,
CC ECO:0000269|PubMed:9834192}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, at highest level
CC in the L1 stage and lowest in L3. Peripheral staining pattern in early
CC embryos. The staining in 1-cell embryos is weak and uniform just after
CC the completion of meiosis, but increases in intensity and becomes
CC concentrated at the anterior periphery during pronuclear migration. The
CC peripheral staining becomes restricted to about 50% embryo length
CC during the pronuclear meeting and pronuclear fusion stage. By early
CC anaphase, the staining extends posteriorly beyond the midline of the
CC zygote and covers about 60% of the total length of embryos. In 2- and
CC 4-cell stages, staining is uniform at the periphery of the AB cell, its
CC daughters and the EMS cell, but peripheral staining in P1 and P2 is
CC restricted to the boundaries with other blastomeres.
CC {ECO:0000269|PubMed:9422779, ECO:0000269|PubMed:9716526}.
CC -!- DOMAIN: Residues 212-224 are capable of binding the PID domain of num-1
CC isoform a and isoform c.
CC -!- DISRUPTION PHENOTYPE: Worms show defects in embryogenesis. Mutant
CC embryos show defects in their polarity and cleavage patterns which
CC disrupt hatching (PubMed:9716526). RNAi-mediated knockdown causes a
CC complete loss of nlp-29 expression following fungal infection by
CC D.coniospora or physical injury (PubMed:19380113).
CC {ECO:0000269|PubMed:19380113, ECO:0000269|PubMed:9716526}.
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; AB007320; BAF80143.1; -; mRNA.
DR EMBL; AF025666; AAB88885.1; -; mRNA.
DR EMBL; FO081044; CCD68754.1; -; Genomic_DNA.
DR PIR; T16006; T16006.
DR RefSeq; NP_495011.1; NM_062610.6.
DR AlphaFoldDB; Q19266; -.
DR SMR; Q19266; -.
DR BioGRID; 39258; 8.
DR DIP; DIP-24814N; -.
DR IntAct; Q19266; 3.
DR MINT; Q19266; -.
DR STRING; 6239.F09E5.1; -.
DR iPTMnet; Q19266; -.
DR EPD; Q19266; -.
DR PaxDb; Q19266; -.
DR PeptideAtlas; Q19266; -.
DR EnsemblMetazoa; F09E5.1.1; F09E5.1.1; WBGene00004034.
DR GeneID; 173914; -.
DR KEGG; cel:CELE_F09E5.1; -.
DR UCSC; F09E5.1.2; c. elegans.
DR CTD; 173914; -.
DR WormBase; F09E5.1; CE02604; WBGene00004034; pkc-3.
DR eggNOG; KOG0695; Eukaryota.
DR GeneTree; ENSGT00940000169305; -.
DR HOGENOM; CLU_000288_63_29_1; -.
DR InParanoid; Q19266; -.
DR OMA; RIQCFIC; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q19266; -.
DR Reactome; R-CEL-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-CEL-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-CEL-9634635; Estrogen-stimulated signaling through PRKCZ.
DR PRO; PR:Q19266; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004034; Expressed in embryo and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IGI:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0008406; P:gonad development; IMP:UniProtKB.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0009611; P:response to wounding; IMP:WormBase.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR CDD; cd00029; C1; 1.
DR CDD; cd06404; PB1_aPKC; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR034877; PB1_aPKC.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR012233; PKC.
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; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000554; PKC_zeta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS51745; PB1; 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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Fertilization; Gastrulation; Gonadal differentiation;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..597
FT /note="Protein kinase C-like 3"
FT /id="PRO_0000055737"
FT DOMAIN 12..95
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 253..522
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 524..595
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 127..177
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 192..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P41743,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 259..267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41743,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41743,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 214
FT /note="I->A: Prevents binding with num-1 (isoform a and
FT isoform c)."
FT /evidence="ECO:0000269|PubMed:11134025"
FT MUTAGEN 216
FT /note="N->A: Prevents binding with num-1 (isoform a and
FT isoform c)."
FT /evidence="ECO:0000269|PubMed:11134025"
FT MUTAGEN 219
FT /note="F->A: Prevents binding with num-1 (isoform a and
FT isoform c)."
FT /evidence="ECO:0000269|PubMed:11134025"
FT MUTAGEN 222
FT /note="H->A: No effect on binding with num-1 (isoform a and
FT isoform c)."
FT /evidence="ECO:0000269|PubMed:11134025"
SQ SEQUENCE 597 AA; 68035 MW; A92760E880DB11B8 CRC64;
MSSPTSLEED GDIKLKTRFQ GQVVVLYARP PLILDDFFAL LKDACKQHKK QDITVKWIDE
DGDPISIDSQ MELDEAVRCL NSSQEAELNI HVFVGKPELP GLPCQGEDKT VYRRGARRWK
KIYLYNGHRF QAKRLNRRIQ CFICHDYIWG IGRQGFRCVD CRLCVHKKCH RHVRTHCGQA
LQGPNIIPMA PASGSLKGAR SNTSSSTTRS GGGIDNGAFH EHEIESPGST SHDASRAMNG
NGSSKWAVSL NDFRLLTVIG RGSYAKVVQA EHVSTRQIYA IKIIKKEMFN EDEDIDWVQT
EKSVFEAASN YPFLVGLHSC FQTESRLFFV IEFVPGGDLM FHMQQQRKLP EEHARFYSGE
IILALHFLHS RGIIYRDLKL DNVLIDAEGH IKLTDYGMCK ENIKDGDLTS TFCGTPNYIA
PEILRGDEYG FSVDWWALGV LMFEMMAGRS PFDIVGMQNS EENTEDYLFQ IILERQIRIP
RSLSVRASGI LKGFLNKDPT ERLGCKLDIN EGLRDMKEHQ FFRGFIDWEA LEQKAVAPPY
HPAVESDRDL THFDHQFTDE LPQLSPDNPD VIARIDQSEF DGFEYVNPLQ MSREDSV
