ID KPC3_CAEBR Reviewed; 597 AA.
AC A8WUG4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 100.
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:0000250|UniProtKB:Q19266}; ORFNames=CBG02381;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Required for the normal progression of embryogenesis and
CC viability of the organism. Plays an indispensable role in establishing
CC embryonic polarity and in recruiting and maintaining par-6 to the
CC periphery, through interaction with par-3. Required for epithelial cell
CC polarity in the distal spermatheca. Phosphorylates serine residues of
CC num-1. Required for the expression of antimicrobial peptide nlp-29 in
CC response in response to fungal infection or physical injury.
CC {ECO:0000250|UniProtKB:Q19266}.
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:0000250|UniProtKB:Q19266};
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:0000250|UniProtKB:Q19266};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q19266};
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 (By similarity). {ECO:0000250|UniProtKB:Q19266}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q19266}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q19266}. Note=Targeted
CC and anchored at the apical surface (villi) of intestinal and pharyngeal
CC cells, and in proximity with the cortical actin cytoskeleton that lies
CC under the plasma membrane. Tightly bound to organelles/cytoskeleton in
CC six of the seven developmental stages. Accumulation in cytoplasm is
CC restricted to L1 larvae and adults. Colocalized with par-3 at the
CC anterior cortex of the 1-cell embryo (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000255}.
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DR EMBL; HE601438; CAP24126.3; -; Genomic_DNA.
DR RefSeq; XP_002630700.1; XM_002630654.1.
DR AlphaFoldDB; A8WUG4; -.
DR SMR; A8WUG4; -.
DR STRING; 6238.A8WUG4; -.
DR EnsemblMetazoa; CBG02381.1; CBG02381.1; WBGene00025443.
DR GeneID; 8572216; -.
DR KEGG; cbr:CBG_02381; -.
DR CTD; 8572216; -.
DR WormBase; CBG02381; CBP00699; WBGene00025443; Cbr-pkc-3.
DR eggNOG; KOG0695; Eukaryota.
DR HOGENOM; CLU_000288_63_29_1; -.
DR InParanoid; A8WUG4; -.
DR OMA; FIDWEAL; -.
DR OrthoDB; 841660at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0016324; C:apical plasma membrane; IEA:EnsemblMetazoa.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblMetazoa.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:EnsemblMetazoa.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISS:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0008406; P:gonad development; ISS: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; IEA:EnsemblMetazoa.
DR GO; GO:0008104; P:protein localization; IEA:EnsemblMetazoa.
DR GO; GO:0009611; P:response to wounding; IEA:EnsemblMetazoa.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR CDD; cd20794; C1_aPKC; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; 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 PANTHER; PTHR24351:SF216; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
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; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 3: Inferred from homology;
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_0000318077"
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 181..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
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"
SQ SEQUENCE 597 AA; 67842 MW; 998A72AF1F4F9C75 CRC64;
MSSPTSVEED GDIKLKTRFH GQVVVLYARP PLILDDFFAL LRDACKQHAK QDITVKWIDE
DGDPISIDSQ MELDEAVRCL NVSQEAELNI HVFVGKPELP GLPCQGEDKT VYRRGARRWK
KIYLYNGHRF QGKRLNRRIQ CFICHDYIWG IGRQGFRCVD CRLCVHKKCH RHVRTHCGQT
PQGPNVPVAP SSGVGSLRGG RLDTSSSTTR SGGGIDNGAF HEHEIESPGS AKDMSRSTNG
NGASKWAVSL NDFRLLTVIG RGSYAKVVQA EHIATRQIYA IKIIKKEMFN EDEDIDWVQT
EKSVFEAASN YPFLVGLHSC FQTESRLFFV IEFVPGGDLM FHMQQQRRLP EEHARFYSGE
IILALHFLHS RGIIYRDLKL DNVLIDAEGH IKLTDYGMCK ENINAGDLTS TFCGTPNYIA
PEILRGDEYG FSVDWWALGV LMFEMMAGRS PFDIVGMQNS EENTEDYLFQ IILERQIRIP
RSLSVRASNI LKGFLNKDPS QRLGCKLDIN DGLNDMKEHD FFRGFIDWEA LEQKAVAPPY
HPAVESDRDL THFDHQFTDE PPQLSPDNSA VIARIDQSEF DGFEYVNPLQ MSREDSV
//
