Reviewed, UniProtKB/Swiss-Prot Q5R4K9 (KPCI_PONAB)

Names and origin

Protein names

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

Gene names

Name:

PRKCI

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	596 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Calcium-independent, phospholipid-dependent, serine- and threonine-specific kinase. May play a role in the secretory response to nutrients. Involved in cell polarization processes and the formation of epithelial tight junctions. Implicated in the activation of several signaling pathways including Ras, c-Src and NF-kappa-B pathways. Functions in both pro- and anti-apoptotic pathways. Functions in the RAC1/ERK signaling required for transformed growth. Plays a role in microtubule dynamics through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs).
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Might be a target for novel lipid activators that are elevated during nutrient-stimulated insulin secretion. Two specific sites, Thr-412 (activation loop of the kinase domain) and Thr-564 (turn motif), need to be phosphorylated for its full activation By similarity. Atypical PCKs are not regulated by diacylglycerol, phorbol esters nor calcium ions.
Subunit structure	Forms a complex with SQSTM1 and MP2K5 By similarity. Interacts directly with SQSTM1 Probable. Interacts with IKBKB. Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary complex containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or PARD6G) and a GTPase protein (CDC42 or RAC1). Part of a complex with LLGL1 and PARD6B. Interacts with ADAP1/CENTA1. Interaction with SMG1, through the ZN-finger domain, activates the kinase activity. Interacts with CDK7. Forms a complex with RAB2A and GAPDH involved in recruitment onto the membrane of vesicular tubular clusters (VTCs) By similarity.
Subcellular location	Cytoplasm By similarity. Membrane By similarity. Endosome By similarity. Nucleus By similarity. Note: Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by cSrc, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Vesicular tubular clusters. Transported to VTCs through interaction with RAB2A By similarity.
Domain	The OPR domain mediates interaction with SQSTM1 By similarity. The C1 domain does not bind diacylglycerol (DAG) By similarity.
Post-translational modification	On neuronal growth factor (NGF) stimulation, phosphorylated by Src on Tyr-265, Tyr-280 and Tyr-334. Phosphorylation on Tyr-265 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus. Phosphorylation on Tyr-334 is important for NF-kappa-B stimulation 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 OPR domain. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Endosome Membrane Nucleus
Domain	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
Cellular component	endosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP 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 – 596	596	Protein kinase C iota type		PRO_0000055712
Regions
	Domain	25 – 108	84	OPR
	Domain	254 – 522	269	Protein kinase
	Domain	523 – 594	72	AGC-kinase C-terminal
	Zinc finger	140 – 190	51	Phorbol-ester/DAG-type
	Nucleotide binding	260 – 268	9	ATP By similarity
	Region	1 – 253	253	Regulatory domain By similarity
	Region	1 – 28	28	Required for interaction with RAB2 By similarity
	Region	72 – 91	20	Interaction with PARD6A By similarity
Sites
	Active site	378	1	Proton acceptor By similarity
	Binding site	283	1	ATP By similarity
Amino acid modifications
	Modified residue	265	1	Phosphotyrosine; by Src By similarity
	Modified residue	280	1	Phosphotyrosine; by Src By similarity
	Modified residue	334	1	Phosphotyrosine; by Src By similarity
	Modified residue	412	1	Phosphothreonine Probable
	Modified residue	564	1	Phosphothreonine Probable

Sequences

	Sequence		Length	Mass (Da)
	Q5R4K9-1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: C514AC89C2D59EA2	FASTA	596	68,263
	10 20 30 40 50 60 MPTQRDSSTM SHTVAGGGSG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CNEVRDMCSF 70 80 90 100 110 120 DNEQLFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE 130 140 150 160 170 180 DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK 190 200 210 220 230 240 KCHKLVTIEC GRHSLPPEPM MPMDQSSMHS DHAQTVIPYN PSSHESLDQV GEEKEAMNTR 250 260 270 280 290 300 ESGKASSSLG LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ 310 320 330 340 350 360 TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL PEEHARFYSA 370 380 390 400 410 420 EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC KEGLRPGDTT STFCGTPNYI 430 440 450 460 470 480 APEILRGEDY GFSVDWWALG VLMFEMMAGR SPFDIVGSSD NPDQNTEDYL FQVILEKQIR 490 500 510 520 530 540 IPRSLSVKAA SVLKSFLNKD PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK 550 560 570 580 590 PNISGEFGLD NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECV

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR861237 mRNA. Translation: CAH93307.1. Different initiation.
RefSeq	NP_001126946.1.
UniGene	Pab.1649
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	100173964.
Organism-specific databases
CTD	100173964.
Phylogenomic databases
HOVERGEN	Q5R4K9.
InParanoid	Q5R4K9.
Enzyme and pathway databases
BRENDA	2.7.11.13. 269192.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR020454. DAG/PE_bd. IPR011009. Kinase-like_dom. IPR000270. OPR_PB1. IPR015745. PKC. IPR012233. PKC_zeta. IPR017892. Pkinase_C. IPR002219. Prot_Kinase_C-like_PE/DAG_bd. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
PANTHER	PTHR22985:SF86. PKC. 1 hit.
Pfam	PF00130. C1_1. 1 hit. PF00564. PB1. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
PIRSF	PIRSF000554. PKC_zeta. 1 hit.
PRINTS	PR00008. DAGPEDOMAIN.
SMART	SM00109. C1. 1 hit. SM00666. PB1. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 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. 1 hit. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPCI_PONAB

Accession

Primary (citable) accession number: Q5R4K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	June 16, 2009
Last modified:	January 19, 2010
This is version 46 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)