Protein kinase C iota type - Pongo abelii (Sumatran orangutan)

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Reviewed, UniProtKB/Swiss-Prot Q5R4K9 (KPCI_PONAB)

Last modified September 22, 2009. Version 43. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

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Protein attributes

Sequence length	596 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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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.

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Ontologies

Keywords
Cellular component	Cytoplasm Endosome Membrane Nucleus
Domain	Phorbol-ester binding 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	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 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...

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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

OPR

Domain

254 – 522

269

Protein kinase

Domain

523 – 594

AGC-kinase C-terminal

Zinc finger

140 – 190

Phorbol-ester/DAG-type

Nucleotide binding

260 – 268

ATP By similarity

Region

1 – 253

253

Regulatory domain By similarity

Region

1 – 28

Required for interaction with RAB2 By similarity

Region

72 – 91

Interaction with PARD6A By similarity

Sites

Active site

378

Proton acceptor By similarity

Binding site

283

ATP By similarity

Amino acid modifications

Modified residue

265

Phosphotyrosine; by Src By similarity

Modified residue

280

Phosphotyrosine; by Src By similarity

Modified residue

334

Phosphotyrosine; by Src By similarity

Modified residue

412

Phosphothreonine Probable

Modified residue

564

Phosphothreonine Probable

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Sequences

Sequence

Length

Mass (Da)

Tools

Q5R4K9-1 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: C514AC89C2D59EA2
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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

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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.

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Cross-references

Sequence databases
	CR861237 mRNA. Translation: CAH93307.1. Different initiation.
RefSeq	NP_001126946.1.
UniGene	Pab.1649
3D structure databases
SMR	Q5R4K9. Positions 16-98.
ModBase	Search...
Genome annotation databases
GeneID	100173964.
Organism-specific databases
CTD	100173964.
Phylogenomic databases
HOVERGEN	Q5R4K9.
Enzyme and pathway databases
BRENDA	2.7.11.13. 269192.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR020454. DAG/PE_bd. IPR000270. OPR_PB1. IPR015745. PKC. IPR012233. PKC_zeta. IPR017892. Pkinase_C. 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. 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.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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...

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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:	September 22, 2009
This is version 43 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents