Calcium/calmodulin-dependent protein kinase type IV

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Reviewed, UniProtKB/Swiss-Prot P08414 (KCC4_MOUSE)

Last modified October 13, 2009. Version 99. 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:
    Calcium/calmodulin-dependent protein kinase type IV
    EC=2.7.11.17
Alternative name(s):
    CAM kinase-GR
    CaMK IV

Gene names

Name:

Camk4

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	469 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/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. May be involved in transcriptional regulation. May be involved in regulation of microtubule dynamics. In vitro, phosphorylates CREB1, CREBBP, PRM2, MEF2A, MEF2D and STMN1/OP18. May be involved in spermatogenesis. May play a role in the consolidation/retention of hippocampus-dependent long-term memory. Ref.4 Ref.5 Ref.6 Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by Ca²⁺/calmodulin. Binding of calmodulin may releave intrasteric autoinhibition. Must be phosphorylated to be maximally active. Phosphorylated by CAMKK1 or CAMKK2. Autophosphorylation of the N-terminus is required for full activation. In part, activity is independent on Ca²⁺/calmodulin and autophosphorylation of Ser-332 allows to switch to a Ca²⁺/calmodulin-independent state. Probably inactivated by serine/threonine protein phosphatase 2A By similarity.
Subunit structure	Monomer By similarity. Interacts with serine/threonine protein phosphatase 2A catalytic subunit, PPP2CA or PPP2CB. The interaction with PP2CA or PP2CB is mutually exclusive with binding to Ca²⁺/calmodulin By similarity.
Subcellular location	Cytoplasm. Nucleus. Note: Substantial localization in certain neuronal nuclei By similarity. In spermatids associated with chromatin and nuclear matrix.
Post-translational modification	Autophosphorylated and phosphorylated by CAMKK1 and CAMKK2. Dephosphorylated by serine/threonine protein phosphatase 2A, probably on Thr-196 By similarity.
Miscellaneous	Camk4 deficient male mice are infertile with impairment of spermiogenesis in late elongating spermatids. The sequential deposition of sperm basic nuclear proteins on chromatin is disrupted, with a specific loss of protamine-2 and prolonged retention of Tnp2 in step-15 spermatids.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. Contains 1 protein kinase domain.

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Calcium Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	nerve-nerve synaptic transmission Inferred from mutant phenotype. Source: MGI nucleocytoplasmic transport Inferred from direct assay. Source: MGI protein amino acid phosphorylation Inferred from mutant phenotype. Source: MGI signal transduction Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Traceable author statement. Source: MGI transcription activator activity Inferred from mutant phenotype. Source: MGI
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 469

469

Calcium/calmodulin-dependent protein kinase type IV

PRO_0000086107

Regions

Domain

42 – 296

255

Protein kinase

Nucleotide binding

48 – 56

ATP By similarity

Region

297 – 336

Autoinhibitory domain By similarity

Region

318 – 337

Calmodulin-binding Potential

Sites

Active site

160

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine; by autocatalysis By similarity

Modified residue

Phosphoserine; by autocatalysis By similarity

Modified residue

186

N6-acetyllysine By similarity

Modified residue

196

Phosphothreonine By similarity

Modified residue

332

Phosphoserine; by autocatalysis By similarity

Modified residue

337

Phosphoserine By similarity

Experimental info

Sequence conflict

278 – 280

VLD → CFGI in AAA37366. Ref.2

Sequence conflict

302

N → T in AAA37366. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P08414-1 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: CE1F98670822F975
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FASTA

469

52,628

        10         20         30         40         50         60 
MLKVTVPSCP SSPCSSVTAS TENLVPDYWI DGSNRDPLGD FFEVESELGR GATSIVYRCK 

        70         80         90        100        110        120 
QKGTQKPYAL KVLKKTVDKK IVRTEIGVLL RLSHPNIIKL KEIFETPTEI SLVLELVTGG 

       130        140        150        160        170        180 
ELFDRIVEKG YYSERDARDA VKQILEAVAY LHENGIVHRD LKPENLLYAT PAPDAPLKIA 

       190        200        210        220        230        240 
DFGLSKIVEH QVLMKTVCGT PGYCAPEILR GCAYGPEVDM WSVGIITYIL LCGFEPFYDE 

       250        260        270        280        290        300 
RGDQFMFRRI LNCEYYFISP WWDEVSLNAK DLVKKLIVLD PKKRLTTFQA LQHPWVTGKA 

       310        320        330        340        350        360 
ANFVHMDTAQ KKLQEFNARR KLKAAVKAVV ASSRLGSASS SHTSIQENHK ASSDPPSTQD 

       370        380        390        400        410        420 
AKDSTDLLGK KMQEEDQEED QVEAEASADE MRKLQSEEVE KDAGVKEEET SSMVPQDPED 

       430        440        450        460 
ELETDDPEMK RDSEEKLKSV EEEMDPMTEE EAPDAGLGVP QQDAIQPEY

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References

[1]	"cDNA sequence and differential expression of the mouse Ca2+/calmodulin-dependent protein kinase IV gene." Jones D.A., Glod J., Wilson-Shaw D., Hahn W.E., Sikela J.M. FEBS Lett. 289:105-109(1991) [PubMed: 1893997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Brain.
[2]	"Chromosomal localization of the human gene for brain Ca2+/calmodulin-dependent protein kinase type IV." Sikela J.M., Law M.L., Kao F.-T., Hartz J.A., Wei Q., Hahn W.E. Genomics 4:21-27(1989) [PubMed: 2536634] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 240-469.
[3]	"Screening an expression library with a ligand probe: isolation and sequence of a cDNA corresponding to a brain calmodulin-binding protein." Sikela J.M., Hahn W.E. Proc. Natl. Acad. Sci. U.S.A. 84:3038-3042(1987) [PubMed: 3033675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 315-469. Tissue: Brain.
[4]	"Characterization of Ca2+/calmodulin-dependent protein kinase IV. Role in transcriptional regulation." Enslen H., Sun P., Brickey D., Soderling S.H., Klamo E., Soderling T.R. J. Biol. Chem. 269:15520-15527(1994) [PubMed: 8195196] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1.
[5]	"CBP: a signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV." Chawla S., Hardingham G.E., Quinn D.R., Bading H. Science 281:1505-1509(1998) [PubMed: 9727976] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CREBBP.
[6]	"Spermiogenesis and exchange of basic nuclear proteins are impaired in male germ cells lacking AC:." Wu J.Y., Ribar T.J., Cummings D.E., Burton K.A., McKnight G.S., Means A.R. Nat. Genet. 25:448-452(2000) [PubMed: 10932193] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PRM2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[7]	"An important role of neural activity-dependent CaMKIV signaling in the consolidation of long-term memory." Kang H., Sun L.D., Atkins C.M., Soderling T.R., Wilson M.A., Tonegawa S. Cell 106:771-783(2001) [PubMed: 11572782] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M16206 mRNA. Translation: AAA39933.1. M64266 mRNA. Translation: AAA37364.1. J03057 mRNA. Translation: AAA37366.1. X58995 mRNA. Translation: CAA41741.1.
IPI	IPI00132526.
PIR	S17656.
UniGene	Mm.222329
3D structure databases
HSSP	HSSP built from PDB template 1KWP based on UniProtKB P49137.
ModBase	Search...
Protein-protein interaction databases
STRING	P08414.
PTM databases
PhosphoSite	P08414.
Proteomic databases
PRIDE	P08414.
Genome annotation databases
Ensembl	ENSMUST00000042868; ENSMUSP00000046539; ENSMUSG00000038128; Mus musculus. [Genome view]
UCSC	uc008ejq.1. mouse.
Organism-specific databases
MGI	MGI:88258. Camk4.
Phylogenomic databases
HOGENOM	P08414.
HOVERGEN	P08414.
Enzyme and pathway databases
BRENDA	2.7.11.17. 244.
Gene expression databases
ArrayExpress	P08414.
Bgee	P08414.
CleanEx	MM_CAMK4.
Genevestigator	P08414.
GermOnline	ENSMUSG00000038128. Mus musculus.
Family and domain databases
InterPro	IPR015733. Ca/calmodulin-dep_kinase_4. 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	PTHR22982:SF33. CaMKIV. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

KCC4_MOUSE

Accession

Primary (citable) accession number: P08414
Secondary accession number(s): Q61381

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	April 1, 1993
Last modified:	October 13, 2009
This is version 99 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

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

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents