PCP4

Purkinje cell protein 4 is a protein that in humans is encoded by the PCP4 gene.^[5][6][7] Also known as PEP-19, PCP4 is a 7.6 kDa protein with an IQ-motif that binds to calmodulin (CaM).^[8] PCP4 is abundant in Purkinje cells of the cerebellum, and plays an important role in synaptic plasticity.^[8][9]

PCP4
Identifiers
Aliases	PCP4, PEP-19, Purkinje cell protein 4
External IDs	OMIM: 601629; MGI: 97509; HomoloGene: 4519; GeneCards: PCP4; OMA:PCP4 - orthologs
Gene location (Human) Chr. Chromosome 21 (human)[1] Band 21q22.2 Start 39,867,438 bp[1] End 39,929,397 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16 C4|16 56.97 cM Start 96,268,806 bp[2] End 96,326,993 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in lateral nuclear group of thalamus external globus pallidus middle frontal gyrus Epithelium of choroid plexus putamen caudate nucleus nucleus accumbens seminal vesicula retinal pigment epithelium internal globus pallidus Top expressed in striatum of neuraxis olfactory bulb Cerebellum layer of retina neural layer of retina cerebellar cortex superior frontal gyrus dentate gyrus of hippocampal formation granule cell urinary bladder primary visual cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding calcium ion binding calmodulin binding Cellular component cytosol nucleus protein-containing complex Biological process positive regulation of neuron differentiation calmodulin dependent kinase signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5121 18546 Ensembl ENSG00000183036 ENSMUSG00000090223 UniProt P48539 P63054 RefSeq (mRNA) NM_006198 NM_008791 RefSeq (protein) NP_006189 NP_032817 Location (UCSC) Chr 21: 39.87 – 39.93 Mb Chr 16: 96.27 – 96.33 Mb PubMed search [3] [4]
Wikidata
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Function

PCP4 knockout mice have been reported to exhibit impaired locomotor learning and markedly altered synaptic plasticity in cerebellar Purkinje neurons.^[8] PCP4 accelerates both the association and dissociation of calcium (Ca²⁺) with calmodulin (CaM), which is postulated to influence the activity of CaM-dependent enzymes, especially CaM kinase II (CaMK-II).^[8][10][11]