Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P09215 (KPCD_RAT)

Entry version 210 (07 Apr 2021)
Sequence version 1 (01 Jul 1989)
Previous versions | rss
Add a publicationFeedback
Protein

Protein kinase C delta type

Gene

Prkcd

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin (By similarity). The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion. Phosphorylates ELAVL1 in response to angiotensin-2 treatment (By similarity). Phosphorylates mitochondrial phospolipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis (By similarity). Phosphorylates SMPD1 which induces SMPD1 secretion (By similarity).By similarity
Truncated isoform 2 is inactive.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are calcium-insensitive, but activated by diacylglycerol (DAG) and phosphatidylserine. Three specific sites; Thr-505 (activation loop of the kinase domain), Ser-643 (turn motif) and Ser-662 (hydrophobic region), need to be phosphorylated for its full activation. Activated by caspase-3 (CASP3) cleavage during apoptosis. After cleavage, the pseudosubstrate motif in the regulatory subunit is released from the substrate recognition site of the catalytic subunit, which enables PRKCD to become constitutively activated. The catalytic subunit which displays properties of a sphingosine-dependent protein kinase is activated by D-erythro-sphingosine (Sph) or N,N-dimethyl-D-erythrosphingosine (DMS) or N,N,N-trimethyl-D-erythrosphingosine (TMS), but not by ceramide or Sph-1-P and is strongly inhibited by phosphatidylserine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei376ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei471Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri158 – 208Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri230 – 280Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi353 – 361ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Cell cycle
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.13, 5301

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-111465, Apoptotic cleavage of cellular proteins
R-RNO-111933, Calmodulin induced events
R-RNO-114508, Effects of PIP2 hydrolysis
R-RNO-1250196, SHC1 events in ERBB2 signaling
R-RNO-1489509, DAG and IP3 signaling
R-RNO-2029485, Role of phospholipids in phagocytosis
R-RNO-450520, HuR (ELAVL1) binds and stabilizes mRNA
R-RNO-5218921, VEGFR2 mediated cell proliferation
R-RNO-5607764, CLEC7A (Dectin-1) signaling
R-RNO-5668599, RHO GTPases Activate NADPH Oxidases
R-RNO-6798695, Neutrophil degranulation
R-RNO-877300, Interferon gamma signaling

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protein kinase C delta typeCurated (EC:2.7.11.13By similarity)
Alternative name(s):
nPKC-delta
Cleaved into the following 2 chains:
Protein kinase C delta type regulatory subunit
Protein kinase C delta type catalytic subunit
Alternative name(s):
Sphingosine-dependent protein kinase-1
Short name:
SDK1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PrkcdImported
Synonyms:Pkcd
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		67383, Prkcd

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi505T → A: Decrease in the phosphorylation level. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3633

DrugCentral

More...DrugCentrali		P09215

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000556961 – 673Protein kinase C delta typeAdd BLAST673
ChainiPRO_00004216711 – 327Protein kinase C delta type regulatory subunitAdd BLAST327
ChainiPRO_0000421672328 – 673Protein kinase C delta type catalytic subunitAdd BLAST346

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei43PhosphothreonineBy similarity1
Modified residuei50PhosphothreonineBy similarity1
Modified residuei64Phosphotyrosine1 Publication1
Modified residuei130PhosphoserineBy similarity1
Modified residuei141PhosphothreonineBy similarity1
Modified residuei155Phosphotyrosine1 Publication1
Modified residuei218PhosphothreonineBy similarity1
Modified residuei299Phosphoserine; by autocatalysisBy similarity1
Modified residuei311Phosphotyrosine; by SRCCombined sources1 Publication1
Modified residuei332Phosphotyrosine; by SRC1 Publication1
Modified residuei372PhosphotyrosineBy similarity1
Modified residuei449PhosphothreonineBy similarity1
Modified residuei504PhosphoserineBy similarity1
Modified residuei505Phosphothreonine; by autocatalysis3 Publications1
Modified residuei565PhosphotyrosineBy similarity1
Modified residuei643PhosphoserineCombined sources1
Modified residuei652PhosphoserineBy similarity1
Modified residuei662PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated and/or phosphorylated at Thr-505, within the activation loop; phosphorylation at Thr-505 is not a prerequisite for enzymatic activity. Autophosphorylated at Ser-299. Upon TNFSF10/TRAIL treatment, phosphorylated at Tyr-155; phosphorylation is required for its translocation to the endoplasmic reticulum and cleavage by caspase-3. Phosphorylated at Tyr-311, Tyr-332 and Tyr-565; phosphorylation of Tyr-311 and Tyr-565 following thrombin stimulation potentiates its kinase activity. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2 (By similarity). Phosphorylated at Tyr-311 and Tyr-332 by SRC; phosphorylation leads to enhanced autophosphorylation at Thr-505.By similarity5 Publications
Proteolytically cleaved into a catalytic subunit and a regulatory subunit by caspase-3 during apoptosis which results in kinase activation.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei327 – 328Cleavage; by caspase-3Curated2

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P09215

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P09215

PRoteomics IDEntifications database

More...PRIDEi		P09215

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P09215

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P09215

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with PDPK1 (via N-terminal region).

Interacts with RAD9A (By similarity).

Interacts with CDCP1.

Interacts with MUC1.

Interacts with VASP.

Interacts with CAVIN3.

Interacts with PRKD2 (via N-terminus and zing-finger domain 1 and 2) in response to oxidative stress; the interaction is independent of PRKD2 tyrosine phosphorylation (By similarity).

Interacts with PLSC3; interaction is enhanced by UV irradiation (By similarity).

By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei48Interaction with phosphotyrosine-containing peptideBy similarity1
Sitei62Interaction with phosphotyrosine-containing peptideBy similarity1
Sitei67Interaction with phosphotyrosine-containing peptideBy similarity1
Sitei123Interaction with phosphotyrosine-containing peptideBy similarity1

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		250924, 10 interactors

Protein interaction database and analysis system

More...IntActi		P09215, 6 interactors

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000025858

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P09215

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1673
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P09215

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P09215

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 106C2PROSITE-ProRule annotationAdd BLAST106
Domaini347 – 601Protein kinasePROSITE-ProRule annotationAdd BLAST255
Domaini602 – 673AGC-kinase C-terminalPROSITE-ProRule annotationAdd BLAST72

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor.
The C2 domain is a non-calcium binding domain. It binds proteins containing phosphotyrosine in a sequence-specific manner (By similarity).By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri158 – 208Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri230 – 280Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0694, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P09215

Database of Orthologous Groups

More...OrthoDBi		222529at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P09215

Family and domain databases

Conserved Domains Database

More...CDDi		cd00029, C1, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.150, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000961, AGC-kinase_C
IPR035892, C2_domain_sf
IPR020454, DAG/PE-bd
IPR011009, Kinase-like_dom_sf
IPR002219, PE/DAG-bd
IPR027436, PKC_delta
IPR017892, Pkinase_C
IPR014376, Prot_kin_PKC_delta
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00130, C1_1, 2 hits
PF00069, Pkinase, 1 hit
PF00433, Pkinase_C, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000551, PKC_delta, 1 hit
PIRSF501104, Protein_kin_C_delta, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00008, DAGPEDOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00109, C1, 2 hits
SM00133, S_TK_X, 1 hit
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51285, AGC_KINASE_CTER, 1 hit
PS50004, C2, 1 hit
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit
PS00479, ZF_DAG_PE_1, 2 hits
PS50081, ZF_DAG_PE_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P09215-1) [UniParc]FASTAAdd to basket
Also known as: PKC-delta-I

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAPFLRISFN SYELGSLQAE DDASQPFCAV KMKEALTTDR GKTLVQKKPT 
        60         70         80         90        100
MYPEWKSTFD AHIYEGRVIQ IVLMRAAEDP MSEVTVGVSV LAERCKKNNG 
       110        120        130        140        150
KAEFWLDLQP QAKVLMCVQY FLEDGDCKQS MRSEEEAMFP TMNRRGAIKQ 
       160        170        180        190        200
AKIHYIKNHE FIATFFGQPT FCSVCKEFVW GLNKQGYKCR QCNAAIHKKC 
       210        220        230        240        250
IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS PTFCDHCGTL 
       260        270        280        290        300
LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQKASR 
       310        320        330        340        350
KPETPETVGI YQGFEKKTAV SGNDIPDNNG TYGKIWEGSN RCRLENFTFQ 
       360        370        380        390        400
KVLGKGSFGK VLLAELKGKE RYFAIKYLKK DVVLIDDDVE CTMVEKRVLA 
       410        420        430        440        450
LAWENPFLTH LICTFQTKDH LFFVMEFLNG GDLMFHIQDK GRFELYRATF 
       460        470        480        490        500
YAAEIICGLQ FLHGKGIIYR DLKLDNVMLD KDGHIKIADF GMCKENIFGE 
       510        520        530        540        550
NRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML IGQSPFHGDD 
       560        570        580        590        600
EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPAKRLG VTGNIRLHPF 
       610        620        630        640        650
FKTINWNLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI 
       660        670 
DSMDQTAFKG FSFVNPKYEQ FLE
Length:673
Mass (Da):77,520
Last modified:July 1, 1989 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD2C767E55863A23C
GO
Isoform 2 (identifier: P09215-2) [UniParc]FASTAAdd to basket
Also known as: PKC-delta-III

The sequence of this isoform differs from the canonical sequence as follows:
     327-673: DNNGTYGKIW...VNPKYEQFLE → GESGSHIPLK...AALARYCLQN

Show »
Length:393
Mass (Da):44,305
Checksum:i88104F3B17991F6C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A140UHX0A0A140UHX0_RAT
Protein kinase C delta type
Prkcd rCG_42255
673Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D4A0U0D4A0U0_RAT
Protein kinase C
Prkcd
672Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti147A → S AA sequence (PubMed:1915352).Curated1
Sequence conflicti249T → S in CAB75578 (PubMed:10721703).Curated1
Sequence conflicti249T → S in AAH76505 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004742327 – 673DNNGT…EQFLE → GESGSHIPLKLPFPDRAREK NSSETWDKTTTGPMARSGRG ATGAALRTSPSRKYLAKAAL ARYCLQN in isoform 2. 1 PublicationAdd BLAST347

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M18330 mRNA Translation: AAA41871.1
AJ230617 AJ230633 Genomic DNA Translation: CAB75578.1
AF219629 mRNA Translation: AAF32345.1
BC076505 mRNA Translation: AAH76505.1

Protein sequence database of the Protein Information Resource

More...PIRi		A28163, KIRTCD

NCBI Reference Sequences

More...RefSeqi		NP_579841.1, NM_133307.1 [P09215-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		170538

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:170538

UCSC genome browser

More...UCSCi		RGD:67383, rat [P09215-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18330 mRNA Translation: AAA41871.1
AJ230617 AJ230633 Genomic DNA Translation: CAB75578.1
AF219629 mRNA Translation: AAF32345.1
BC076505 mRNA Translation: AAH76505.1
PIRiA28163, KIRTCD
RefSeqiNP_579841.1, NM_133307.1 [P09215-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BDYX-ray2.20A/B1-123[»]
SMRiP09215
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi250924, 10 interactors
IntActiP09215, 6 interactors
STRINGi10116.ENSRNOP00000025858

Chemistry databases

BindingDBiP09215
ChEMBLiCHEMBL3633
DrugCentraliP09215

PTM databases

iPTMnetiP09215
PhosphoSitePlusiP09215

Proteomic databases

jPOSTiP09215
PaxDbiP09215
PRIDEiP09215

Genome annotation databases

GeneIDi170538
KEGGirno:170538
UCSCiRGD:67383, rat [P09215-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5580
RGDi67383, Prkcd

Phylogenomic databases

eggNOGiKOG0694, Eukaryota
InParanoidiP09215
OrthoDBi222529at2759
PhylomeDBiP09215

Enzyme and pathway databases

BRENDAi2.7.11.13, 5301
ReactomeiR-RNO-111465, Apoptotic cleavage of cellular proteins
R-RNO-111933, Calmodulin induced events
R-RNO-114508, Effects of PIP2 hydrolysis
R-RNO-1250196, SHC1 events in ERBB2 signaling
R-RNO-1489509, DAG and IP3 signaling
R-RNO-2029485, Role of phospholipids in phagocytosis
R-RNO-450520, HuR (ELAVL1) binds and stabilizes mRNA
R-RNO-5218921, VEGFR2 mediated cell proliferation
R-RNO-5607764, CLEC7A (Dectin-1) signaling
R-RNO-5668599, RHO GTPases Activate NADPH Oxidases
R-RNO-6798695, Neutrophil degranulation
R-RNO-877300, Interferon gamma signaling

Miscellaneous databases

EvolutionaryTraceiP09215

Protein Ontology

More...PROi		PR:P09215

Family and domain databases

CDDicd00029, C1, 2 hits
Gene3Di2.60.40.150, 1 hit
InterProiView protein in InterPro
IPR000961, AGC-kinase_C
IPR035892, C2_domain_sf
IPR020454, DAG/PE-bd
IPR011009, Kinase-like_dom_sf
IPR002219, PE/DAG-bd
IPR027436, PKC_delta
IPR017892, Pkinase_C
IPR014376, Prot_kin_PKC_delta
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00130, C1_1, 2 hits
PF00069, Pkinase, 1 hit
PF00433, Pkinase_C, 1 hit
PIRSFiPIRSF000551, PKC_delta, 1 hit
PIRSF501104, Protein_kin_C_delta, 1 hit
PRINTSiPR00008, DAGPEDOMAIN
SMARTiView protein in SMART
SM00109, C1, 2 hits
SM00133, S_TK_X, 1 hit
SM00220, S_TKc, 1 hit
SUPFAMiSSF56112, SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51285, AGC_KINASE_CTER, 1 hit
PS50004, C2, 1 hit
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit
PS00479, ZF_DAG_PE_1, 2 hits
PS50081, ZF_DAG_PE_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKPCD_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09215
Secondary accession number(s): Q6DG48, Q9JK29, Q9JL03
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 7, 2021
This is version 210 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again