PRKCA-binding protein - Rattus norvegicus (Rat)

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Q9EP80 (PICK1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
PRKCA-binding protein

Alternative name(s):
Protein interacting with C kinase 1
Protein kinase C-alpha-binding protein

Gene names

Name:	Pick1
Synonyms:	Prkcabp

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 ACCN3/ACCN2 channel. Ref.9
Subunit structure	Monomer and homodimer. Interacts with CXADR. Interacts presynaptically with the glutamate receptors GRIA2, GRIA3, GRIK3, isoform 3 of GRIA4, isoform A of GRM4, GRM7 and GRM8; with NAPA and NAPB; and with BTG2. The interaction with NAPA and NAPB disrupts the interaction with GRIA2, conducting to the internalization of GRIA2. Interacts with PRKCA; with the amine transporters SLC6A2 and SLC6A3; with the channels ACCN1 and ACCN2; with the GTP-binding proteins ARF1 and ARF3; with the ephrin receptor tyrosine kinases EPHA7, EPHB1 and EPHB2; with ERBB2 and through its PDZ domain with the C-terminal tail of PRLHR By similarity. Interacts with UNC5A. Interacts (via AH domain) with NCS1/FREQ; in a calcium-dependent manner. Ref.1 Ref.2 Ref.3 Ref.5 Ref.7 Ref.8 Ref.11 Ref.12
Subcellular location	Cytoplasm › perinuclear region. Membrane; Peripheral membrane protein. Note: Also membrane-associated, present at excitatory synapses.
Tissue specificity	Ubiquitous.
Developmental stage	Expressed early in development (E15), and gradually increases, reaching a peak at around 2 weeks after birth.
Post-translational modification	Phosphorylated By similarity. Phosphorylation at Thr-82 appears to inhibit the interaction with AMPA receptors By similarity.
Sequence similarities	Contains 1 AH domain. Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Ligand	Calcium Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB dopamine transport Non-traceable author statement. Source: UniProtKB protein phosphorylation Inferred from direct assay Ref.3. Source: UniProtKB receptor clustering Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB postsynaptic density Inferred from direct assay Ref.1. Source: UniProtKB presynaptic membrane Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from physical interaction Ref.1. Source: UniProtKB synaptosome Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB G-protein coupled glutamate receptor binding Traceable author statement. Source: UniProtKB GTPase binding Traceable author statement. Source: UniProtKB ephrin receptor binding Traceable author statement. Source: UniProtKB identical protein binding Inferred from direct assay Ref.1. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein C-terminus binding Inferred from sequence or structural similarity. Source: UniProtKB protein domain specific binding Inferred from mutant phenotype. Source: RGD protein kinase C binding Inferred from direct assay. Source: UniProtKB receptor tyrosine kinase binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
Btg2	P27049	3	EBI-77728,EBI-78953
Gria2	P19491	8	EBI-77728,EBI-77718
Gria3	P19492	5	EBI-77728,EBI-77764

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 416

416

PRKCA-binding protein

PRO_0000058429

Regions

Domain

22 – 105

PDZ

Domain

144 – 357

214

Compositional bias

382 – 389

Poly-Glu

Sites

Metal binding

Zinc Probable

Metal binding

Zinc Probable

Amino acid modifications

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphothreonine By similarity

Experimental info

Mutagenesis

27 – 28

KD → AA: Abolishes interaction with other proteins, but not with itself. Ref.1 Ref.2 Ref.6

Mutagenesis

C → G: Decreased lipid membrane binding, but no effect on peptide ligand recognition. Ref.1 Ref.2 Ref.6 Ref.12

Mutagenesis

C → G: Decreased lipid membrane binding, but no effect on peptide ligand recognition. Ref.1 Ref.2 Ref.6 Ref.12

Mutagenesis

K → E: No effect on lipid membrane binding. Ref.1 Ref.2 Ref.6 Ref.12

Mutagenesis

K → E: No effect on lipid membrane binding. Ref.1 Ref.2 Ref.6 Ref.12

Sequence conflict

401 – 402

RG → TW in AAK54603. Ref.3

Secondary structure

416

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9EP80 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 8FDE0D78BB26C006
Show »

FASTA

416

46,606

        10         20         30         40         50         60 
MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV QVFDNTPAAL 

        70         80         90        100        110        120 
DGTVAAGDEI TGVNGRSIKG KTKVEVAKMI QEVKGEVTIH YNKLQADPKQ GMSLDIVLKK 

       130        140        150        160        170        180 
VKHRLVENMS SGTADALGLS RAILCNDGLV KRLEELERTA ELYKGMTEHT KNLLRAFYEL 

       190        200        210        220        230        240 
SQTHRAFGDV FSVIGVREPQ PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN 

       250        260        270        280        290        300 
KAIPDTRLTI KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL GEPLYRVSTG NYEYRLILRC 

       310        320        330        340        350        360 
RQEARARFSQ MRKDVLEKME LLDQKHVQDI VFQLQRFVST MSKYYNDCYA VLRDADVFPI 

       370        380        390        400        410 
EVDLAHTTLA YGPNQGGFTD GEDEEEEEED GAAREVSKDA RGATGPTDKG GSWCDS

« Hide

References

[1]	"Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1." Xia J., Zhang X., Staudinger J., Huganir R.L. Neuron 22:179-187(1999) [PubMed: 10027300] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRIA2; GRIA3 AND ISOFORM 4C OF GRIA4, MUTAGENESIS OF 27-LYS-ASP-28. Strain: Sprague-Dawley. Tissue: Brain.
[2]	"Interaction of the C-terminal tail region of the metabotropic glutamate receptor 7 with the protein kinase C substrate PICK1." El Far O., Airas J., Wischmeyer E., Nehring R.B., Karschin A., Betz H. Eur. J. Neurosci. 12:4215-4221(2000) [PubMed: 11122333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRM4; GRM7; GRM8; GRIK3 AND PRKCA, MUTAGENESIS OF 27-LYS-ASP-28. Tissue: Brain.
[3]	"Mitogen-stimulated TIS21 protein interacts with a protein-kinase-Calpha-binding protein rPICK1." Lin W.-J., Chang Y.-F., Wang W.-L., Huang C.-Y.F. Biochem. J. 354:635-643(2001) [PubMed: 11237868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BTG2.
[4]	"Interaction of glutamate transporter GLT1b with PICK1, a protein regulating targeting and trafficking at excitatory synapses." Chen W., Rosenberg P.A. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain.
[5]	"The protein kinase C alpha binding protein PICK1 interacts with short but not long form alternative splice variants of AMPA receptor subunits." Dev K.K., Nishimune A., Henley J.M., Nakanishi S. Neuropharmacology 38:635-644(1999) [PubMed: 10340301] [Abstract] Cited for: INTERACTION WITH GRIA2; GRIA3 AND GRIA4 ISOFORM 4C.
[6]	"Molecular determinants for PICK1 synaptic aggregation and mGluR7a receptor coclustering: role of the PDZ, coiled-coil, and acidic domains." Boudin H., Craig A.M. J. Biol. Chem. 276:30270-30276(2001) [PubMed: 11375398] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF 27-LYS-ASP-28.
[7]	"NSF ATPase and alpha-/beta-SNAPs disassemble the AMPA receptor-PICK1 complex." Hanley J.G., Khatri L., Hanson P.I., Ziff E.B. Neuron 34:53-67(2002) [PubMed: 11931741] [Abstract] Cited for: INTERACTION WITH NAPA AND NAPB.
[8]	"Surface expression of the netrin receptor UNC5H1 is regulated through a protein kinase C-interacting protein/protein kinase-dependent mechanism." Williams M.E., Wu S.C.-Y., McKenna W.L., Hinck L. J. Neurosci. 23:11279-11288(2003) [PubMed: 14672991] [Abstract] Cited for: INTERACTION WITH UNC5A.
[9]	"PICK1 is a calcium-sensor for NMDA-induced AMPA receptor trafficking." Hanley J.G., Henley J.M. EMBO J. 24:3266-3278(2005) [PubMed: 16138078] [Abstract] Cited for: FUNCTION, CALCIUM-BINDING.
[10]	"Zinc binding site in PICK1 is dominantly located at the CPC motif of its PDZ domain." Shi Y., Zhang L., Yuan J., Xiao H., Yang X., Niu L. J. Neurochem. 106:1027-1034(2008) [PubMed: 18429931] [Abstract] Cited for: ZINC-BINDING SITES.
[11]	"Metabotropic glutamate receptor-mediated LTD involves two interacting Ca(2+) sensors, NCS-1 and PICK1." Jo J., Heon S., Kim M.J., Son G.H., Park Y., Henley J.M., Weiss J.L., Sheng M., Collingridge G.L., Cho K. Neuron 60:1095-1111(2008) [PubMed: 19109914] [Abstract] Cited for: INTERACTION WITH NCS1.
[12]	"Clustering and synaptic targeting of PICK1 requires direct interaction between the PDZ domain and lipid membranes." Pan L., Wu H., Shen C., Shi Y., Jin W., Xia J., Zhang M. EMBO J. 26:4576-4587(2007) [PubMed: 17914463] [Abstract] Cited for: STRUCTURE BY NMR OF 18-104 IN COMPLEX WITH GRIA2, INTERACTION WITH GRIA2, MUTAGENESIS OF CYS-44; CYS-46; LYS-79 AND LYS-81.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF327562 mRNA. Translation: AAG48152.1.
AJ240083 mRNA. Translation: CAC17808.2.
AF373289 mRNA. Translation: AAK54603.1.
AF542094 mRNA. Translation: AAO49507.1.

IPI

IPI00188758.

RefSeq

NP_445912.1. NM_053460.1.

UniGene

Rn.24750.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PKU	NMR	-	A	18-104	[»]
3HPK	X-ray	2.20	A/B	1-110	[»]
3HPM	X-ray	2.80	A/B	19-110	[»]

ProteinModelPortal

Q9EP80.

SMR

Q9EP80. Positions 18-104.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9EP80. 5 interactions.

MINT

MINT-86023.

STRING

Q9EP80.

PTM databases

PhosphoSite

Q9EP80.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

84591.

KEGG

rno:84591.

UCSC

NM_053460. rat.

Organism-specific databases

CTD

9463.

RGD

69437. Pick1.

Phylogenomic databases

eggNOG

roNOG06087.

GeneTree

ENSGT00440000033690.

HOVERGEN

HBG053600.

InParanoid

Q9EP80.

OrthoDB

EOG4GQQ55.

Gene expression databases

ArrayExpress

Q9EP80.

Genevestigator

Q9EP80.

GermOnline

ENSRNOG00000011507. Rattus norvegicus.

Family and domain databases

InterPro

IPR010504. Arfaptin_homology_dom.
IPR001478. PDZ/DHR/GLGF.
[Graphical view]

Gene3D

G3DSA:1.20.1270.60. Arfaptin. 1 hit.

Pfam

PF06456. Arfaptin. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]

SMART

SM01015. Arfaptin. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]

SUPFAM

SSF50156. PDZ. 1 hit.

PROSITE

PS50870. AH. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

617193.

Entry information

Entry name

PICK1_RAT

Accession

Primary (citable) accession number: Q9EP80
Secondary accession number(s): Q546X4, Q925D1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents