Protein kinase C iota type - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot Q62074 (KPCI_MOUSE)

Last modified July 22, 2008. Version 91. 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
    Atypical protein kinase C-lambda/iota
      Short name(s)=aPKC-lambda/iota

Gene names

Name:	Prkci
Synonyms:	Pkcl

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	586 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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 RAB2 and GAPDH and recruitment to vesicular tubular clusters (VTCs) By similarity.
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-402 (activation loop of the kinase domain) and Thr-554 (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 CENTA1. Interaction with SMG1, through the ZN-finger domain, activates the kinase activity. Interacts with CDK7. Forms a complex with RAB2 and GAPDH involved in recruitment onto the membrane of vesicular tubular clusters (VTCs) By similarity.
Subcellular location	CytoplasmBy similarity. MembraneBy similarity. EndosomeBy similarity. NucleusBy 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 Rab2 By similarity.
Domain	The OPR domain mediates interaction with SQSTM1. The C1 domain does not bind diacylglycerol (DAG) By similarity.
Post-translational modification	On neuronal growth factor (NGF) stimulation, phosphorylated on tyrosine residues by Src. Phosphorylation on Tyr-255 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus. Phosphorylation on Tyr-324 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 Oncogene Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	actin filament organization Inferred from mutant phenotype. Source: MGI cell-cell junction assembly and maintenance Inferred from sequence or structural similarity. Source: UniProtKB establishment of apical/basal cell polarity Inferred from mutant phenotype. Source: MGI eye photoreceptor cell development Inferred from mutant phenotype. Source: MGI
Cellular component	apical part of cell Inferred from direct assay. Source: MGI cytosol Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	atypical protein kinase C activity Inferred from sequence or structural similarity. Source: UniProtKB phospholipid binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 586

586

Protein kinase C iota type

Regions

Domain

16 – 99

OPR

Domain

244 – 512

269

Protein kinase

Domain

513 – 584

AGC-kinase C-terminal

Zinc finger

131 – 181

Phorbol-ester/DAG-type

Nucleotide binding

250 – 258

ATP By similarity

Region

1 – 19

Required for interaction with RAB2 By similarity

Sites

Active site

368

Proton acceptor By similarity

Binding site

273

ATP By similarity

Amino acid modifications

Modified residue

255

Phosphotyrosine; by Src By similarity

Modified residue

270

Phosphotyrosine; by Src By similarity

Modified residue

324

Phosphotyrosine; by Src By similarity

Modified residue

402

Phosphothreonine Probable

Modified residue

554

Phosphothreonine Probable

Experimental info

Mutagenesis

R → A: No effect on interaction with SQSTM1

Mutagenesis

V → A: No effect on interaction with SQSTM1; when associated with A-20

Mutagenesis

K → A: No effect on interaction with SQSTM1; when associated with A-19

Mutagenesis

W → A: Loss of interaction with SQSTM1

Mutagenesis

D → A: Loss of interaction with SQSTM1

Mutagenesis

E → A: Loss of interaction with SQSTM1

Mutagenesis

D → A: Loss of interaction with SQSTM1

Mutagenesis

Q → A: No effect on interaction with SQSTM1

Mutagenesis

E → A: Loss of interaction with SQSTM1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q62074-1 [UniParc].

Last modified November 1, 1998. Version 2.
Checksum: F7F8F3022B8E4B06
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FASTA

586

67,199

        10         20         30         40         50         60 
MSHTVACGGG GDHSHQVRVK AYYRGDIMIT HFEPSISFEG LCSEVRDMCS FDNEQPFTMK 

        70         80         90        100        110        120 
WIDEEGDPCT VSSQLELEEA FRLYELNKDS ELLIHVFPCV PERPGMPCPG EDKSIYRRGA 

       130        140        150        160        170        180 
RRWRKLYCAN GHTFQAKRFN RRAHCAICTD RIWGLGRQGY KCINCKLLVH KKCHKLVTIE 

       190        200        210        220        230        240 
CGRHSLPPEP MMPMDQTMHP DHTQTVIPYN PSSHESLDQV GEEKEAMNTR ESGKASSSLG 

       250        260        270        280        290        300 
LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ TEKHVFEQAS 

       310        320        330        340        350        360 
NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL PEEHARFYSA EISLALNYLH 

       370        380        390        400        410        420 
ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC KEGLRPGDTT STFCGTPNYI APEILRGEDY 

       430        440        450        460        470        480 
GFSVDWWALG VLMFEMMAGR SPFDIVGSSD NPDQNTEDYL FQVILEKQIR IPRSLSVKAA 

       490        500        510        520        530        540 
SVLKSFLNKD PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK PNISGEFGLD 

       550        560        570        580 
NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new member of the third class in the protein kinase C family, PKC lambda, expressed dominantly in an undifferentiated mouse embryonal carcinoma cell line and also in many tissues and cells." Akimoto K., Mizuno K., Osada S., Hirai S., Tanuma S., Suzuki K., Ohno S. J. Biol. Chem. 269:12677-12683(1994) [PubMed: 7513693] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42." Joberty G., Petersen C., Gao L., Macara I.G. Nat. Cell Biol. 2:531-539(2000) [PubMed: 10934474] [Abstract] Cited for: SUBUNIT OF A COMPLEX CONTAINING PARD6B; PARD3 AND CDC42.
[4]	"Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins." Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A., Michaelsen E., Bjoerkoey G., Johansen T. J. Biol. Chem. 278:34568-34581(2003) [PubMed: 12813044] [Abstract] Cited for: INTERACTION WITH SQSTM1 AND MAP2K5, MUTAGENESIS OF ARG-18; VAL-19; LYS-20; TRP-61; ASP-63; GLU-65; ASP-67; GLN-74 AND GLU-76.

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Cross-references

Sequence databases
	D28577 mRNA. Translation: BAA32499.1. BC021630 mRNA. Translation: AAH21630.1.
PIR	A53758.
UniGene	Mm.291554
3D structure databases
HSSP	HSSP built from PDB template 1GZK based on UniProtKB P31751.
SMR	Q62074. Positions 16-98.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q62074.
PTM databases
PhosphoSite	Q62074.
Genome annotation databases
Ensembl	ENSMUSG00000037643. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:99260. Prkci.
Phylogenomic databases
HOVERGEN	Q62074.
Gene expression databases
ArrayExpress	Q62074.
CleanEx	MM_PRKCI.
GermOnline	ENSMUSG00000037643. Mus musculus.
Family and domain databases
InterPro	IPR002219. DAG_PE_bd. IPR000270. OPR_PB1. IPR015745. PKC. IPR012233. PKC_zeta. IPR000961. Pkinase_C. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. 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]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

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Entry information

Entry name

KPCI_MOUSE

Accession

Primary (citable) accession number: Q62074

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1998
Last modified:	July 22, 2008
This is version 91 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents