P09215 (KPCD_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein kinase C delta type
EC=2.7.11.13

Alternative name(s):
nPKC-delta

Cleaved into the following 2 chains:

1. Protein kinase C delta type regulatory subunit
2. Protein kinase C delta type catalytic subunit
   Alternative name(s):
   Sphingosine-dependent protein kinase-1
   Short name=SDK1

Gene names

Name:	Prkcd
Synonyms:	Pkcd

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	673 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity. Truncated isoform 2 is inactive.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	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. Ref.8
Subunit structure	Interacts with PDPK1 (via N-terminus region), RAD9A, CDCP1, MUC1 and VASP By similarity.
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › perinuclear region. Endoplasmic reticulum By similarity. Mitochondrion By similarity. Membrane; Peripheral membrane protein Ref.10.
Domain	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.
Post-translational modification	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-terminus cleavage product of PKN2 By similarity. Phosphorylated at Tyr-311 and Tyr-332 by SRC; phosphorylation leads to enhanced autophosphorylation at Thr-505. Ref.7 Ref.10 Ref.11 Ref.12 Proteolytically cleaved into a catalytic subunit and a regulatory subunit by caspase-3 during apoptosis which results in kinase activation. Ref.8
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 C2 domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Disease	Tumor suppressor
Domain	Repeat Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell proliferation Inferred from electronic annotation. Source: Compara aging Inferred from expression pattern PubMed 17008461. Source: RGD apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW aspartate transport Inferred from mutant phenotype PubMed 17364745. Source: RGD cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cellular response to glucose starvation Inferred from expression pattern PubMed 17728702. Source: RGD cellular response to insulin stimulus Inferred from expression pattern PubMed 17046201. Source: RGD cellular senescence Inferred from electronic annotation. Source: Compara collagen metabolic process Inferred from mutant phenotype PubMed 17728702. Source: RGD defense response to bacterium Inferred from sequence or structural similarity. Source: UniProtKB immunoglobulin mediated immune response Inferred from electronic annotation. Source: Compara induction of apoptosis Inferred from direct assay PubMed 12426377. Source: RGD interleukin-10 production Inferred from electronic annotation. Source: Compara interleukin-12 production Inferred from electronic annotation. Source: Compara intracellular signal transduction Inferred from direct assay PubMed 11562372. Source: RGD negative regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara negative regulation of actin filament polymerization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of filopodium assembly Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of glial cell apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of insulin receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara negative regulation of platelet aggregation Inferred from sequence or structural similarity. Source: UniProtKB neutrophil activation Inferred from electronic annotation. Source: Compara peptidyl-threonine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of MAP kinase activity Inferred from mutant phenotype PubMed 16935468. Source: RGD positive regulation of ceramide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of glucose import Inferred from mutant phenotype PubMed 17098211. Source: RGD positive regulation of glucosylceramide catabolic process Inferred from electronic annotation. Source: Compara positive regulation of phospholipid scramblase activity Inferred from electronic annotation. Source: Compara positive regulation of protein dephosphorylation Inferred from electronic annotation. Source: Compara positive regulation of response to DNA damage stimulus Inferred from electronic annotation. Source: Compara positive regulation of sphingomyelin catabolic process Inferred from electronic annotation. Source: Compara positive regulation of superoxide anion generation Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from direct assay PubMed 10085132. Source: RGD response to amino acid stimulus Inferred from expression pattern PubMed 17210758. Source: RGD response to drug Inferred from expression pattern PubMed 17123493. Source: RGD response to ethanol Inferred from expression pattern PubMed 17728104. Source: RGD response to glucose stimulus Inferred from expression pattern PubMed 12960081. Source: RGD response to heat Inferred from expression pattern PubMed 16990486. Source: RGD response to hydrogen peroxide Inferred from expression pattern PubMed 12226102PubMed 17397968. Source: RGD response to hypoxia Inferred from expression pattern PubMed 16936002. Source: RGD response to mechanical stimulus Inferred from expression pattern PubMed 17487266. Source: RGD response to organic cyclic compound Inferred from expression pattern PubMed 11478406. Source: RGD termination of signal transduction Inferred from electronic annotation. Source: Compara
Cellular_component	cell-cell junction Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay PubMed 18945317PubMed 9705215PubMed 9950866. Source: RGD endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from direct assay PubMed 17008461. Source: RGD nuclear matrix Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 12663471. Source: RGD perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 18945317. Source: RGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-independent protein kinase C activity Inferred from direct assay Ref.6. Source: RGD enzyme activator activity Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P09215-1)

Also known as: PKC-delta-I;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P09215-2)

Also known as: PKC-delta-III;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 673

673

Protein kinase C delta type

PRO_0000055696

Chain

1 – 327

327

Protein kinase C delta type regulatory subunit

PRO_0000421671

Chain

328 – 673

346

Protein kinase C delta type catalytic subunit

PRO_0000421672

Regions

Domain

1 – 90

90

C2

Domain

347 – 601

255

Protein kinase

Domain

602 – 673

72

AGC-kinase C-terminal

Zinc finger

158 – 208

51

Phorbol-ester/DAG-type 1

Zinc finger

230 – 280

51

Phorbol-ester/DAG-type 2

Nucleotide binding

353 – 361

9

ATP By similarity

Sites

Active site

471

1

Proton acceptor By similarity

Binding site

376

1

ATP By similarity

Site

48

1

Interaction with phosphotyrosine-containing peptide By similarity

Site

62

1

Interaction with phosphotyrosine-containing peptide By similarity

Site

67

1

Interaction with phosphotyrosine-containing peptide By similarity

Site

123

1

Interaction with phosphotyrosine-containing peptide By similarity

Site

327 – 328

2

Cleavage; by caspase-3 Probable

Amino acid modifications

Modified residue

43

1

Phosphothreonine By similarity

Modified residue

64

1

Phosphotyrosine Ref.10

Modified residue

130

1

Phosphoserine By similarity

Modified residue

155

1

Phosphotyrosine Ref.10

Modified residue

218

1

Phosphothreonine By similarity

Modified residue

299

1

Phosphoserine; by autocatalysis By similarity

Modified residue

311

1

Phosphotyrosine; by SRC Ref.12

Modified residue

332

1

Phosphotyrosine; by SRC Ref.12

Modified residue

372

1

Phosphotyrosine By similarity

Modified residue

505

1

Phosphothreonine; by autocatalysis Ref.7 Ref.11 Ref.12

Modified residue

565

1

Phosphotyrosine By similarity

Modified residue

643

1

Phosphoserine Probable

Modified residue

652

1

Phosphoserine By similarity

Modified residue

662

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

327 – 673

347

DNNGT…EQFLE → GESGSHIPLKLPFPDRAREK NSSETWDKTTTGPMARSGRG ATGAALRTSPSRKYLAKAAL ARYCLQN in isoform 2.

VSP_004742

Experimental info

Mutagenesis

505

1

T → A: Decrease in the phosphorylation level. Ref.7

Sequence conflict

147

1

A → S AA sequence Ref.6

Sequence conflict

249

1

T → S in CAB75578. Ref.2

Sequence conflict

249

1

T → S in AAH76505. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

673

Helix Strand Turn

Details...

Beta strand

3 – 13

11

Beta strand

27 – 35

9

Helix

38 – 40

3

Beta strand

43 – 46

4

Beta strand

58 – 62

5

Beta strand

68 – 76

9

Beta strand

79 – 87

9

Helix

88 – 96

9

Turn

97 – 100

4

Beta strand

101 – 107

7

Beta strand

109 – 111

3

Beta strand

113 – 122

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PKC-delta-I) [UniParc]. Last modified July 1, 1989. Version 1. Checksum: D2C767E55863A23C	FASTA	673	77,520
	10 20 30 40 50 60 MAPFLRISFN SYELGSLQAE DDASQPFCAV KMKEALTTDR GKTLVQKKPT MYPEWKSTFD 70 80 90 100 110 120 AHIYEGRVIQ IVLMRAAEDP MSEVTVGVSV LAERCKKNNG KAEFWLDLQP QAKVLMCVQY 130 140 150 160 170 180 FLEDGDCKQS MRSEEEAMFP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKEFVW 190 200 210 220 230 240 GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS 250 260 270 280 290 300 PTFCDHCGTL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQKASR 310 320 330 340 350 360 KPETPETVGI YQGFEKKTAV SGNDIPDNNG TYGKIWEGSN RCRLENFTFQ KVLGKGSFGK 370 380 390 400 410 420 VLLAELKGKE RYFAIKYLKK DVVLIDDDVE CTMVEKRVLA LAWENPFLTH LICTFQTKDH 430 440 450 460 470 480 LFFVMEFLNG GDLMFHIQDK GRFELYRATF YAAEIICGLQ FLHGKGIIYR DLKLDNVMLD 490 500 510 520 530 540 KDGHIKIADF GMCKENIFGE NRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML 550 560 570 580 590 600 IGQSPFHGDD EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPAKRLG VTGNIRLHPF 610 620 630 640 650 660 FKTINWNLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI DSMDQTAFKG 670 FSFVNPKYEQ FLE
	Isoform 2 (PKC-delta-III) [UniParc]. Checksum: 88104F3B17991F6C	FASTA	393	44,305
	10 20 30 40 50 60 MAPFLRISFN SYELGSLQAE DDASQPFCAV KMKEALTTDR GKTLVQKKPT MYPEWKSTFD 70 80 90 100 110 120 AHIYEGRVIQ IVLMRAAEDP MSEVTVGVSV LAERCKKNNG KAEFWLDLQP QAKVLMCVQY 130 140 150 160 170 180 FLEDGDCKQS MRSEEEAMFP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKEFVW 190 200 210 220 230 240 GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS 250 260 270 280 290 300 PTFCDHCGTL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQKASR 310 320 330 340 350 360 KPETPETVGI YQGFEKKTAV SGNDIPGESG SHIPLKLPFP DRAREKNSSE TWDKTTTGPM 370 380 390 ARSGRGATGA ALRTSPSRKY LAKAALARYC LQN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The structure, expression, and properties of additional members of the protein kinase C family." Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y. J. Biol. Chem. 263:6927-6932(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Genomic structure and chromosomal localization of the rat PKCdelta-gene." Kurkinen K.M.A., Keinanen R.A., Karhu R., Koistinaho J. Gene 242:115-123(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Wistar Kyoto.
[3]	"cDNA cloning of an alternative splicing variant of protein kinase C delta (PKC deltaIII), a new truncated form of PKCdelta, in rats." Ueyama T., Ren Y., Ohmori S., Sakai K., Tamaki N., Saito N. Biochem. Biophys. Res. Commun. 269:557-563(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[5]	"Identification of three additional members of rat protein kinase C family: delta-, epsilon- and zeta-subspecies." Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y. FEBS Lett. 226:125-128(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 123-286.
[6]	"Expression and characterization of protein kinase C-delta." Olivier A.R., Parker P.J. Eur. J. Biochem. 200:805-810(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 142-153.
[7]	"The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation." Garcia-Paramio P., Cabrerizo Y., Bornancin F., Parker P.J. Biochem. J. 333:631-636(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF THR-505, PHOSPHORYLATION AT THR-505.
[8]	"Sphingosine-dependent protein kinase-1, directed to 14-3-3, is identified as the kinase domain of protein kinase C delta." Hamaguchi A., Suzuki E., Murayama K., Fujimura T., Hikita T., Iwabuchi K., Handa K., Withers D.A., Masters S.C., Fu H., Hakomori S. J. Biol. Chem. 278:41557-41565(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CLEAVAGE BY CASPASE-3, ENZYME REGULATION.
[9]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662, MASS SPECTROMETRY. Strain: Fischer. Tissue: Liver.
[10]	"Induction of apoptosis is driven by nuclear retention of protein kinase C delta." DeVries-Seimon T.A., Ohm A.M., Humphries M.J., Reyland M.E. J. Biol. Chem. 282:22307-22314(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-64 AND TYR-155.
[11]	"Protein kinase Cepsilon (PKCepsilon) and Src control PKCdelta activation loop phosphorylation in cardiomyocytes." Rybin V.O., Guo J., Gertsberg Z., Elouardighi H., Steinberg S.F. J. Biol. Chem. 282:23631-23638(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-505.
[12]	"Tyrosine phosphorylation modifies protein kinase C delta-dependent phosphorylation of cardiac troponin I." Sumandea M.P., Rybin V.O., Hinken A.C., Wang C., Kobayashi T., Harleton E., Sievert G., Balke C.W., Feinmark S.J., Solaro R.J., Steinberg S.F. J. Biol. Chem. 283:22680-22689(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-311; TYR-332 AND THR-505.
[13]	"Crystal structure of the C2 domain from protein kinase C-delta." Pappa H., Murray-Rust J., Dekker L.V., Parker P.J., McDonald N.Q. Structure 6:885-894(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-123.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M18330 mRNA. Translation: AAA41871.1.
AJ230617 , AJ230618, AJ230619, AJ230620, AJ230621, AJ230622, AJ230623, AJ230624, AJ230625, AJ230626, AJ230627, AJ230628, AJ230629, AJ230630, AJ230631, AJ230632, AJ230633 Genomic DNA. Translation: CAB75578.1.
AF219629 mRNA. Translation: AAF32345.1.
BC076505 mRNA. Translation: AAH76505.1.

IPI

IPI00212816.
IPI00231534.

PIR

KIRTCD. A28163.

RefSeq

NP_579841.1. NM_133307.1.

UniGene

Rn.98279.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BDY	X-ray	2.20	A/B	1-123	[»]

ProteinModelPortal

P09215.

SMR

P09215. Positions 1-123, 149-218, 227-283, 343-666.

ModBase

Search...

Protein-protein interaction databases

IntAct

P09215. 2 interactions.

MINT

MINT-143019.

PTM databases

PhosphoSite

P09215.

Proteomic databases

PaxDb

P09215.

PRIDE

P09215.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

170538.

KEGG

rno:170538.

UCSC

RGD:67383. rat.

Organism-specific databases

CTD

5580.

RGD

67383. Prkcd.

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233022.

HOVERGEN

HBG108317.

KO

K06068.

Enzyme and pathway databases

BRENDA

2.7.11.13. 5301.

Gene expression databases

ArrayExpress

P09215.

Genevestigator

P09215.

GermOnline

ENSRNOG00000016346. Rattus norvegicus.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR027436. PKC_delta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000551. PKC_delta. 1 hit.
PIRSF501104. Protein_kin_C_delta. 1 hit.

PRINTS

PR00008. DAGPEDOMAIN.

SMART

SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. False negative.
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.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P09215.

ChEMBL

CHEMBL3633.

EvolutionaryTrace

P09215.

NextBio

621024.

PMAP-CutDB

P09215.

Entry information

Entry name

KPCD_RAT

Accession

Primary (citable) accession number: P09215
Secondary accession number(s): Q6DG48, Q9JK29, Q9JL03

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 29, 2013
This is version 152 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program