Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00079
Entry Name
UniProt Accession
Theoretical PI
5.34
Molecular Weight
46597.08
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
PRKCA-binding protein
Protein Synonyms/Alias
Protein interacting with C kinase 1; Protein kinase C-alpha-binding protein;
Gene Name
Pick1
Gene Synonyms/Alias
Prkcabp;
Created Date
02-AUG-2002
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
414
Canonical
TDKGGSWCDS*****
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Thomas GM, Hayashi T, Huganir RL, Linden DJ. DHHC8-dependent PICK1palmitoylation is required for induction of cerebellar long-term synapticdepression. J Neurosci. 2013 Sep 25;33(39):15401-7. doi:10.1523/JNEUROSCI.1283-13.2013.[PMID:24068808]
Functional Description
Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function.
Sequence Annotation
Domain: 22 105 PDZ.
Domain: 144 357 AH.
Metal binding site: 44 44 Zinc.
Metal binding site: 46 46 Zinc.
Modified residue: 82 82 Phosphothreonine.
Protein Length
416 AA.
Protein Sequence
(Canonical)
MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV QVFDNTPAAL  60
DGTVAAGDEI TGVNGKSIKG KTKVEVAKMI QEVKGEVTIH YNKLQADPKQ GMSLDIVLKK  120
VKHRLVENMS SGTADALGLS RAILCNDGLV KRLEELERTA ELYKGMTEHT KNLLRAFYEL  180
SQTHRAFGDV FSVIGVREPQ PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN  240
KAIPDTRLTI KKYLDVKFEY LSYCLKVKEM DDEEYSCIGP RRALYRVSTG NYEYRLILRC  300
RQEARARFSQ MRKDVLEKME LLDQKHVQDI VFQLQRFVST MSKYYNDCYA VLQDADVFPI  360
EVDLAHTTLA YGPNQGSFTD GEEEDEEEED GAAREVSKDA CGATGPTDKG GSWCDS      416
FASTA
(Canonical)
>LipidDB-10090-00079|Q62083
MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAAL
DGTVAAGDEITGVNGKSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKK
VKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYEL
SQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLN
KAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIGPRRALYRVSTGNYEYRLILRC
RQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRFVSTMSKYYNDCYAVLQDADVFPI
EVDLAHTTLAYGPNQGSFTDGEEEDEEEEDGAAREVSKDACGATGPTDKGGSWCDS
Gene Ontology
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005794; C:Golgi apparatus; IDA:UniProtKB
GO:0005739; C:mitochondrion; IDA:MGI
GO:0043005; C:neuron projection; ISS:UniProtKB
GO:0097481; C:neuronal postsynaptic density; IDA:MGI
GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB
GO:0005886; C:plasma membrane; ISS:UniProtKB
GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW
GO:0042734; C:presynaptic membrane; ISS:UniProtKB
GO:0045202; C:synapse; IDA:UniProtKB
GO:0051015; F:actin filament binding; ISS:UniProtKB
GO:0071933; F:Arp2/3 complex binding; ISS:UniProtKB
GO:0016887; F:ATPase activity; IDA:UniProtKB
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0008022; F:protein C-terminus binding; ISS:UniProtKB
GO:0005080; F:protein kinase C binding; IPI:UniProtKB
GO:0005102; F:receptor binding; IPI:UniProtKB
GO:0006200; P:ATP catabolic process; IDA:GOC
GO:0036294; P:cellular response to decreased oxygen levels; ISS:UniProtKB
GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB
GO:0097062; P:dendritic spine maintenance; ISS:UniProtKB
GO:0097061; P:dendritic spine organization; ISS:UniProtKB
GO:0021782; P:glial cell development; ISS:UniProtKB
GO:0035556; P:intracellular signal transduction; NAS:UniProtKB
GO:0060292; P:long term synaptic depression; ISS:UniProtKB
GO:0015844; P:monoamine transport; ISS:UniProtKB
GO:0007275; P:multicellular organismal development; NAS:UniProtKB
GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB
GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB
GO:0051260; P:protein homooligomerization; TAS:UniProtKB
GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB
GO:0006468; P:protein phosphorylation; ISS:UniProtKB
GO:0006605; P:protein targeting; IDA:MGI
GO:0043113; P:receptor clustering; IDA:UniProtKB
GO:0050803; P:regulation of synapse structure and activity; NAS:UniProtKB
Interpro
InterPro; IPR027267; AH/BAR-dom
InterPro; IPR010504; AH_dom
InterPro; IPR001478; PDZ
Pfam
Pfam; PF06456; Arfaptin;
Pfam; PF00595; PDZ;
SMART
SMART; SM01015; Arfaptin;
SMART; SM00228; PDZ;
PROSITE
PROSITE; PS50870; AH;
PROSITE; PS50106; PDZ;
PRINTS