Q7XSQ5 · CDPKC_ORYSJ
- ProteinCalcium-dependent protein kinase 12
- GeneCPK12
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids533 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
May play a role in signal transduction pathways that involve calcium as a second messenger (By similarity).
Functions in signal transduction pathways that positively regulate responses to low-nitrogen (Ref.7). Functions in multiple signaling pathways, positively regulating salt tolerance and negatively modulating rice blast fungus resistance. May promote tolerance to salt stress by negatively regulating NADPH oxidase and positively regulating reactive oxygen species (ROS) scavengers (PubMed:21883553).
Functions in signal transduction pathways that positively regulate responses to low-nitrogen (Ref.7). Functions in multiple signaling pathways, positively regulating salt tolerance and negatively modulating rice blast fungus resistance. May promote tolerance to salt stress by negatively regulating NADPH oxidase and positively regulating reactive oxygen species (ROS) scavengers (PubMed:21883553).
Miscellaneous
Plants over-expressing CPK12 show enhanced tolerance to low nitrogen stress (Ref.7). Plants over-expressing CPK12 show increased tolerance to salt stress, increased sensitivity to abscisic acid (ABA) and increased susceptibility to rice blast fungus (M.oryzae) (PubMed:21883553).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by calcium. Autophosphorylation may play an important role in the regulation of the kinase activity.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 97-105 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGSGQFGTT | ||||||
Binding site | 120 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 215 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 404 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 406 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 408 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 410 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 415 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 440 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 442 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 444 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 446 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 451 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 476 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 478 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 480 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 482 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 487 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 511 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 513 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 515 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 517 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 522 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent protein serine/threonine kinase activity | |
Molecular Function | calmodulin binding | |
Molecular Function | calmodulin-dependent protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Biological Process | defense response to fungus | |
Biological Process | intracellular signal transduction | |
Biological Process | positive regulation of response to salt stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCalcium-dependent protein kinase 12
- EC number
- Short namesOsCDPK12 ; OsCPK12
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ7XSQ5
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Lipidation | 2 | UniProt | N-myristoyl glycine | ||||
Sequence: G | |||||||
Chain | PRO_0000437556 | 2-533 | UniProt | Calcium-dependent protein kinase 12 | |||
Sequence: GNCFTKTYEIPITSGTMRRPASTAERSKARGGDEPGTWRRPSFPRHGAPPHRPPTGSSSAAGALSRRASGGGGEMGPVLQRAMVSVRSLYQLDRKLGSGQFGTTYLCTERATGNRYACKSVSKRKLVRRTDVDDVRREITILQHLSGQPNIAEFRGAYEDNDHVHLVMEFCSGGELFDRITAKGSYSERQAAAVCRDILTVVHVCHFMGVIHRDLKPENFLLASADDDAPLKAIDFGLSVFIEEGKVYKDIVGSAYYVAPEVLQRNYGKEADIWSAGVILYILLCGTPPFWAETEKGIFDAILVNQVDFSTSPWPSISESAKDLIRQMLHRDPQKRITASQALEHRWLKEGGASDRPIDSAVLSRMKQFKAMNKLKQLALKVIAENLSPEEIKGLKQMFNNMDTDRSGTITVEELKVGLTKLGSRISEAEVQKLMEAVDVDKSGSIDYSEFLTAMINKHKLEKEEDLLRAFQHFDKDNSGYITRDELEQAMAEYGMGDEANIKQVLDEVDKDKDGRIDYEEFVEMMRKGIQT | |||||||
Modified residue (large scale data) | 70 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Expressed in roots, leaf blades and developing seeds (Ref.7). Expressed in vascular tissues of roots and leaf blades. Expressed in the phloem tissue of the large vascular bundle in leaf blades (PubMed:21883553).
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MGNCFTKTYEIPITSGTMRRPA | ||||||
Region | 1-77 | Disordered | ||||
Sequence: MGNCFTKTYEIPITSGTMRRPASTAERSKARGGDEPGTWRRPSFPRHGAPPHRPPTGSSSAAGALSRRASGGGGEMG | ||||||
Domain | 91-349 | Protein kinase | ||||
Sequence: YQLDRKLGSGQFGTTYLCTERATGNRYACKSVSKRKLVRRTDVDDVRREITILQHLSGQPNIAEFRGAYEDNDHVHLVMEFCSGGELFDRITAKGSYSERQAAAVCRDILTVVHVCHFMGVIHRDLKPENFLLASADDDAPLKAIDFGLSVFIEEGKVYKDIVGSAYYVAPEVLQRNYGKEADIWSAGVILYILLCGTPPFWAETEKGIFDAILVNQVDFSTSPWPSISESAKDLIRQMLHRDPQKRITASQALEHRWL | ||||||
Region | 354-384 | Autoinhibitory domain | ||||
Sequence: ASDRPIDSAVLSRMKQFKAMNKLKQLALKVI | ||||||
Domain | 391-426 | EF-hand 1 | ||||
Sequence: EEIKGLKQMFNNMDTDRSGTITVEELKVGLTKLGSR | ||||||
Domain | 427-462 | EF-hand 2 | ||||
Sequence: ISEAEVQKLMEAVDVDKSGSIDYSEFLTAMINKHKL | ||||||
Domain | 463-498 | EF-hand 3 | ||||
Sequence: EKEEDLLRAFQHFDKDNSGYITRDELEQAMAEYGMG | ||||||
Domain | 499-533 | EF-hand 4 | ||||
Sequence: DEANIKQVLDEVDKDKDGRIDYEEFVEMMRKGIQT |
Domain
There are 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (354-384) inactivates kinase activity under calcium-free conditions.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length533
- Mass (Da)59,562
- Last updated2004-03-01 v2
- ChecksumE9E784F05B8433D9
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MGNCFTKTYEIPITSGTMRRPA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL606687 EMBL· GenBank· DDBJ | CAE01846.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008210 EMBL· GenBank· DDBJ | BAF15462.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014960 EMBL· GenBank· DDBJ | BAS90471.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000141 EMBL· GenBank· DDBJ | EAZ31624.1 EMBL· GenBank· DDBJ | Genomic DNA |