Q19266 · KPC3_CAEEL
- ProteinProtein kinase C-like 3
- Genepkc-3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids597 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for the normal progression of embryogenesis and viability of the organism (PubMed:9422779).
Plays an indispensable role in establishing embryonic polarity and in recruiting and maintaining par-6 to the periphery, through interaction with par-3 (PubMed:9716526, PubMed:9834192).
Required for epithelial cell polarity in the distal spermatheca (PubMed:15151982).
Phosphorylates serine residues of num-1 (PubMed:11134025).
Required for the expression of antimicrobial peptide nlp-29 in response in response to fungal infection or physical injury (PubMed:19380113).
Plays an indispensable role in establishing embryonic polarity and in recruiting and maintaining par-6 to the periphery, through interaction with par-3 (PubMed:9716526, PubMed:9834192).
Required for epithelial cell polarity in the distal spermatheca (PubMed:15151982).
Phosphorylates serine residues of num-1 (PubMed:11134025).
Required for the expression of antimicrobial peptide nlp-29 in response in response to fungal infection or physical injury (PubMed:19380113).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | cell cortex | |
Cellular Component | cortical actin cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | diacylglycerol-dependent serine/threonine kinase activity | |
Molecular Function | metal ion binding | |
Molecular Function | protein domain specific binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | cell differentiation | |
Biological Process | defense response to fungus | |
Biological Process | embryo development ending in birth or egg hatching | |
Biological Process | establishment or maintenance of cell polarity | |
Biological Process | gastrulation | |
Biological Process | gonad development | |
Biological Process | gonadal mesoderm development | |
Biological Process | intracellular signal transduction | |
Biological Process | protein localization | |
Biological Process | response to wounding | |
Biological Process | single fertilization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein kinase C-like 3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ19266
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Targeted and anchored at the apical surface (villi) of intestinal and pharyngeal cells, and in proximity with the cortical actin cytoskeleton that lies under the plasma membrane. Tightly bound to organelles/cytoskeleton in six of the seven developmental stages. Accumulation in cytoplasm is restricted to L1 larvae and adults. Colocalized with par-3 at the anterior cortex of the 1-cell embryo.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Worms show defects in embryogenesis. Mutant embryos show defects in their polarity and cleavage patterns which disrupt hatching (PubMed:9716526).
RNAi-mediated knockdown causes a complete loss of nlp-29 expression following fungal infection by D.coniospora or physical injury (PubMed:19380113).
RNAi-mediated knockdown causes a complete loss of nlp-29 expression following fungal infection by D.coniospora or physical injury (PubMed:19380113).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 214 | Prevents binding with num-1 (isoform a and isoform c). | ||||
Sequence: I → A | ||||||
Mutagenesis | 216 | Prevents binding with num-1 (isoform a and isoform c). | ||||
Sequence: N → A | ||||||
Mutagenesis | 219 | Prevents binding with num-1 (isoform a and isoform c). | ||||
Sequence: F → A | ||||||
Mutagenesis | 222 | No effect on binding with num-1 (isoform a and isoform c). | ||||
Sequence: H → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000055737 | 1-597 | Protein kinase C-like 3 | |||
Sequence: MSSPTSLEEDGDIKLKTRFQGQVVVLYARPPLILDDFFALLKDACKQHKKQDITVKWIDEDGDPISIDSQMELDEAVRCLNSSQEAELNIHVFVGKPELPGLPCQGEDKTVYRRGARRWKKIYLYNGHRFQAKRLNRRIQCFICHDYIWGIGRQGFRCVDCRLCVHKKCHRHVRTHCGQALQGPNIIPMAPASGSLKGARSNTSSSTTRSGGGIDNGAFHEHEIESPGSTSHDASRAMNGNGSSKWAVSLNDFRLLTVIGRGSYAKVVQAEHVSTRQIYAIKIIKKEMFNEDEDIDWVQTEKSVFEAASNYPFLVGLHSCFQTESRLFFVIEFVPGGDLMFHMQQQRKLPEEHARFYSGEIILALHFLHSRGIIYRDLKLDNVLIDAEGHIKLTDYGMCKENIKDGDLTSTFCGTPNYIAPEILRGDEYGFSVDWWALGVLMFEMMAGRSPFDIVGMQNSEENTEDYLFQIILERQIRIPRSLSVRASGILKGFLNKDPTERLGCKLDINEGLRDMKEHQFFRGFIDWEALEQKAVAPPYHPAVESDRDLTHFDHQFTDELPQLSPDNPDVIARIDQSEFDGFEYVNPLQMSREDSV |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Abundantly expressed in the anterior and posterior pharyngeal bulbs, the pharyngeal-intestinal valve, vulval cells, and a region at the posterior end of the intestine that corresponds to site of co-assembly of the intestinal-rectal valve and anal sphincter, and depressor muscles. Modest expression apparent in four hypodermal cells that provide cuticle and muscle anchorage in the tail. Strong expression observed in discrete patches and spots in vulval cells and in somatic cells of the spermatheca. Transiently coexpressed and colocalized with par-6 and par-3, asymmetrically in the developing somatic gonad, including the spermathecal precursor cells of L4 larvae.
Developmental stage
Expressed throughout development, at highest level in the L1 stage and lowest in L3. Peripheral staining pattern in early embryos. The staining in 1-cell embryos is weak and uniform just after the completion of meiosis, but increases in intensity and becomes concentrated at the anterior periphery during pronuclear migration. The peripheral staining becomes restricted to about 50% embryo length during the pronuclear meeting and pronuclear fusion stage. By early anaphase, the staining extends posteriorly beyond the midline of the zygote and covers about 60% of the total length of embryos. In 2- and 4-cell stages, staining is uniform at the periphery of the AB cell, its daughters and the EMS cell, but peripheral staining in P1 and P2 is restricted to the boundaries with other blastomeres.
Gene expression databases
Interaction
Subunit
Interaction with par-3 required for the peripheral localization of par-6 and to form a par-3/par-6/pkc-3 complex, which is activated when cdc-42 interacts with par-6. Binds avidly to the phosphotyrosine interaction domain (PID) of a novel pkc-3 adapter protein num-1, which enables tethering and targeting of pkc-3 to the cell periphery.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q19266 | num-1 Q9XTY6 | 5 | EBI-319158, EBI-495781 | |
BINARY | Q19266 | num-1 Q9XTY6-1 | 5 | EBI-319158, EBI-495798 | |
BINARY | Q19266 | par-3 Q17353 | 3 | EBI-319158, EBI-321762 | |
BINARY | Q19266 | par-6 Q9NAN2 | 4 | EBI-319158, EBI-318782 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, zinc finger, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-95 | PB1 | ||||
Sequence: DIKLKTRFQGQVVVLYARPPLILDDFFALLKDACKQHKKQDITVKWIDEDGDPISIDSQMELDEAVRCLNSSQEAELNIHVFVG | ||||||
Zinc finger | 127-177 | Phorbol-ester/DAG-type | ||||
Sequence: GHRFQAKRLNRRIQCFICHDYIWGIGRQGFRCVDCRLCVHKKCHRHVRTHC | ||||||
Region | 192-238 | Disordered | ||||
Sequence: ASGSLKGARSNTSSSTTRSGGGIDNGAFHEHEIESPGSTSHDASRAM | ||||||
Compositional bias | 196-213 | Polar residues | ||||
Sequence: LKGARSNTSSSTTRSGGG | ||||||
Domain | 253-522 | Protein kinase | ||||
Sequence: FRLLTVIGRGSYAKVVQAEHVSTRQIYAIKIIKKEMFNEDEDIDWVQTEKSVFEAASNYPFLVGLHSCFQTESRLFFVIEFVPGGDLMFHMQQQRKLPEEHARFYSGEIILALHFLHSRGIIYRDLKLDNVLIDAEGHIKLTDYGMCKENIKDGDLTSTFCGTPNYIAPEILRGDEYGFSVDWWALGVLMFEMMAGRSPFDIVGMQNSEENTEDYLFQIILERQIRIPRSLSVRASGILKGFLNKDPTERLGCKLDINEGLRDMKEHQFF | ||||||
Domain | 524-595 | AGC-kinase C-terminal | ||||
Sequence: GFIDWEALEQKAVAPPYHPAVESDRDLTHFDHQFTDELPQLSPDNPDVIARIDQSEFDGFEYVNPLQMSRED |
Domain
Residues 212-224 are capable of binding the PID domain of num-1 isoform a and isoform c.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length597
- Mass (Da)68,035
- Last updated1996-11-01 v1
- ChecksumA92760E880DB11B8
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 196-213 | Polar residues | ||||
Sequence: LKGARSNTSSSTTRSGGG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB007320 EMBL· GenBank· DDBJ | BAF80143.1 EMBL· GenBank· DDBJ | mRNA | ||
AF025666 EMBL· GenBank· DDBJ | AAB88885.1 EMBL· GenBank· DDBJ | mRNA | ||
FO081044 EMBL· GenBank· DDBJ | CCD68754.1 EMBL· GenBank· DDBJ | Genomic DNA |