Reviewed, UniProtKB/Swiss-Prot Q5PU49 (KPCD_CANFA)

Names and origin

Protein names

Recommended name:
    Protein kinase C delta type
    EC=2.7.11.13
Alternative name(s):
    nPKC-delta

Gene names

Name:

PRKCD

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	674 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May play a role in antigen-dependent control of B-cell function. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	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.
Subunit structure	Interacts with MUC1, PDK1, RAD9A and CDCP1 By similarity.
Subcellular location	Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity.
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	Phosphorylated on Thr-505, within the activation loop. Autophosphorylated and/or phosphorylated. Although the Thr-505 phosphorylation occurs it is not a prerequisite for enzymatic activity By similarity.
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
Cellular component	Cytoplasm Membrane
Domain	Phorbol-ester binding Repeat Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase C activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 674	674	Protein kinase C delta type		PRO_0000055693
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
Amino acid modifications
	Modified residue	43	1	Phosphothreonine By similarity
	Modified residue	50	1	Phosphothreonine By similarity
	Modified residue	130	1	Phosphoserine By similarity
	Modified residue	299	1	Phosphoserine By similarity
	Modified residue	302	1	Phosphoserine By similarity
	Modified residue	310	1	Phosphotyrosine By similarity
	Modified residue	332	1	Phosphotyrosine By similarity
	Modified residue	505	1	Phosphothreonine; by PDPK1 By similarity
	Modified residue	643	1	Phosphoserine Probable
	Modified residue	652	1	Phosphoserine By similarity
	Modified residue	662	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PU49-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 5A25DADDB7A364BA	FASTA	674	77,338
	10 20 30 40 50 60 MAPFLRIAFT SYELGSLQAA DEASQPFCAV KMKEALSTER GKTLVQKKPT MYPEWKSTFD 70 80 90 100 110 120 AHIYEGRVIQ IVLMRAAEEP MSEVTVGVSV LAERCKKNNX KAEFWLDLQP QAKVLMSVQY 130 140 150 160 170 180 FLEDIDCRQS MHGEDEAKLP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKDFVW 190 200 210 220 230 240 GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TAANSRDTIF QKERFNIDMP HRFKVYNYMS 250 260 270 280 290 300 PTFCDHCGSL LWGLVKQGLK CEDCGMNVHH KCQKKVANLC GINQKLLAEA LNQVTQRSSR 310 320 330 340 350 360 KSETESVGIY QNFERKPGVS GDIAPGEDNG TYGKIWEGST RCNIDNFIFH KVLGKGSFGK 370 380 390 400 410 420 VLLVELKGKK EFFAIKALKK DVVLIDDDVE CTMVEKRVLA LAWENPFLTH LFCTFQTKDH 430 440 450 460 470 480 LFFVMEFLNG GDLMYHIQDK GRFELYRATF YAAEIVCGLQ FLHNKGIIYR DLKLDNVMLD 490 500 510 520 530 540 QDGHIKIADF GMCKENIFGE KQASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML 550 560 570 580 590 600 IGQSPFHGDD EDELFESIRV DTPHYPRWIT KESKDILEKL LERDTTKRLG VTGNIKIHPF 610 620 630 640 650 660 FKTINWTLLE KRAVEPPFKP KVKSPGDYSN FDQEFLNEKA RLSYTDKNLI DSMDQTAFAG 670 FSFVNPKFER FLEK

References

[1]	"Canine protein kinase C delta." Hsieh Y.-T., Chen H.-C. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY825360 mRNA. Translation: AAV80465.1.
RefSeq	NP_001008716.1.
UniGene	Cfa.16226
3D structure databases
SMR	Q5PU49. Positions 1-123, 231-280, 344-616.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PU49.
Genome annotation databases
Ensembl	ENSCAFT00000013836; ENSCAFP00000012799; ENSCAFG00000008689; Canis familiaris. [Genome view]
GeneID	494005.
KEGG	cfa:494005.
Organism-specific databases
CTD	494005.
Phylogenomic databases
HOVERGEN	Q5PU49.
Enzyme and pathway databases
BRENDA	2.7.11.13. 463.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000008. C2_Ca-dep. IPR020454. DAG/PE_bd. IPR015745. PKC. IPR017892. Pkinase_C. IPR014376. Prot_kin_PKC_delta. IPR002219. Prot_Kinase_C-like_PE/DAG_bd. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
PANTHER	PTHR22985:SF86. PKC. 1 hit.
Pfam	PF00130. C1_1. 2 hits. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
PIRSF	PIRSF000551. PKC_delta. 1 hit.
PRINTS	PR00008. DAGPEDOMAIN.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00109. C1. 2 hits. SM00239. C2. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
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...

Entry information

Entry name

KPCD_CANFA

Accession

Primary (citable) accession number: Q5PU49

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	January 4, 2005
Last modified:	October 13, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)