[1]	NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRIA2; GRIA3 AND ISOFORM 4C OF GRIA4, AND MUTAGENESIS OF 27-LYS-ASP-28. STRAIN=Sprague-Dawley; TISSUE=Brain; DOI=10.1016/S0896-6273(00)80689-3; PubMed=10027300 [NCBI, ExPASy, EBI, Israel, Japan] Xia J., Zhang X., Staudinger J., Huganir R.L.; "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1."; Neuron 22:179-187(1999).
[2]	NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRM4; GRM7; GRM8; GRIK3 AND PRKCA, AND MUTAGENESIS OF 27-LYS-ASP-28. TISSUE=Brain; DOI=10.1046/j.1460-9568.2000.01309.x; PubMed=11122333 [NCBI, ExPASy, EBI, Israel, Japan] El Far O., Airas J., Wischmeyer E., Nehring R.B., Karschin A., Betz H.; "Interaction of the C-terminal tail region of the metabotropic glutamate receptor 7 with the protein kinase C substrate PICK1."; Eur. J. Neurosci. 12:4215-4221(2000).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH BTG2. DOI=10.1042/0264-6021:3540635; PubMed=11237868 [NCBI, ExPASy, EBI, Israel, Japan] Lin W.-J., Chang Y.-F., Wang W.-L., Huang C.-Y.F.; "Mitogen-stimulated TIS21 protein interacts with a protein-kinase-Calpha-binding protein rPICK1."; Biochem. J. 354:635-643(2001).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Brain; Chen W., Rosenberg P.A.; "Interaction of glutamate transporter GLT1b with PICK1, a protein regulating targeting and trafficking at excitatory synapses."; Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[5]	INTERACTION WITH GRIA2; GRIA3 AND GRIA4 ISOFORM 4C. DOI=10.1016/S0028-3908(98)00230-5; PubMed=10340301 [NCBI, ExPASy, EBI, Israel, Japan] Dev K.K., Nishimune A., Henley J.M., Nakanishi S.; "The protein kinase C alpha binding protein PICK1 interacts with short but not long form alternative splice variants of AMPA receptor subunits."; Neuropharmacology 38:635-644(1999).
[6]	CHARACTERIZATION, AND MUTAGENESIS OF 27-LYS-ASP-28. DOI=10.1074/jbc.M102991200; PubMed=11375398 [NCBI, ExPASy, EBI, Israel, Japan] Boudin H., Craig A.M.; "Molecular determinants for PICK1 synaptic aggregation and mGluR7a receptor coclustering: role of the PDZ, coiled-coil, and acidic domains."; J. Biol. Chem. 276:30270-30276(2001).
[7]	INTERACTION WITH NAPA AND NAPB. DOI=10.1016/S0896-6273(02)00638-4; PubMed=11931741 [NCBI, ExPASy, EBI, Israel, Japan] Hanley J.G., Khatri L., Hanson P.I., Ziff E.B.; "NSF ATPase and alpha-/beta-SNAPs disassemble the AMPA receptor-PICK1 complex."; Neuron 34:53-67(2002).
[8]	INTERACTION WITH UNC5A. PubMed=14672991 [NCBI, ExPASy, EBI, Israel, Japan] Williams M.E., Wu S.C.-Y., McKenna W.L., Hinck L.; "Surface expression of the netrin receptor UNC5H1 is regulated through a protein kinase C-interacting protein/protein kinase-dependent mechanism."; J. Neurosci. 23:11279-11288(2003).

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. May be regulated upon PRKCA activation. May regulate ACCN3/ACCN2 channel.
SUBUNIT: 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.
INTERACTION:
P27049:Btg2; NbExp=2; IntAct=EBI-77728, EBI-78953;
P19491:Gria2; NbExp=6; IntAct=EBI-77728, EBI-77718;
P19492:Gria3; NbExp=4; IntAct=EBI-77728, EBI-77764;
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.
PTM: Phosphorylated (By similarity).
SIMILARITY: Contains 1 AH domain.
SIMILARITY: Contains 1 PDZ (DHR) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF327562; AAG48152.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ240083; CAC17808.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF373289; AAK54603.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF542094; AAO49507.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_445912.1; -.

UniGene

Rn.24750

3D structure databases

PDB

2PKU; NMR; -; A=18-104.

[ExPASy / RCSB / EBI]

PDBsum

2PKU; -.

ModBase

Q9EP80.

Protein-protein interaction databases

IntAct

Q9EP80; -.

PTM databases

PhosphoSite

Q9EP80; -.

Organism-specific databases

RGD

69437; Pick1.

Gene expression databases

ArrayExpress

Q9EP80; -.

GermOnline

ENSRNOG00000011507; Rattus norvegicus.

Ontologies

GO:0005794;	Cellular component: Golgi apparatus (inferred from sequence or structural similarity from UniProtKB).
GO:0048471;	Cellular component: perinuclear region of cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0005886;	Cellular component: plasma membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0014069;	Cellular component: postsynaptic density (inferred from direct assay from UniProtKB).
GO:0042734;	Cellular component: presynaptic membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0043234;	Cellular component: protein complex (inferred from physical interaction from UniProtKB).
GO:0019717;	Cellular component: synaptosome (inferred from direct assay from UniProtKB).
GO:0016887;	Molecular function: ATPase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0046875;	Molecular function: ephrin receptor binding (traceable author statement from UniProtKB).
GO:0051020;	Molecular function: GTPase binding (traceable author statement from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from direct assay from UniProtKB).
GO:0035256;	Molecular function: metabotropic glutatmate receptor binding (traceable author statement from UniProtKB).
GO:0008022;	Molecular function: protein C-terminus binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005080;	Molecular function: protein kinase C binding (inferred from direct assay from UniProtKB).
GO:0030971;	Molecular function: receptor tyrosine kinase binding (traceable author statement from UniProtKB).
GO:0007205;	Biological process: activation of protein kinase C activity (inferred from sequence or structural similarity from UniProtKB).
GO:0015872;	Biological process: dopamine transport (non-traceable author statement from UniProtKB).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from direct assay from UniProtKB).
GO:0043113;	Biological process: receptor clustering (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR010504; Arfaptin.
IPR001478; PDZ.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.1270.60; Arfaptin; 1.

Pfam

PF06456; Arfaptin; 1.
PF00595; PDZ; 1.
Pfam graphical view of domain structure.

SMART

SM00228; PDZ; 1.
SMART graphical view of domain structure.

PROSITE

PS50870; AH; 1.
PS50106; PDZ; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q9EP80.

Genome annotation databases

Ensembl

ENSRNOG00000011507; Rattus norvegicus. [Contig view]

GeneID

84591; -.

KEGG

rno:84591; -.

Phylogenomic databases

HOVERGEN

Q9EP80; -.

Other

NextBio

617193; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Membrane; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 416`	`416`	`PRKCA-binding protein.`	`PRO_0000058429`
`DOMAIN`	`22 105`	`84`	`PDZ.`
`DOMAIN`	`144 357`	`214`	`AH.`
`COMPBIAS`	`382 389`	`8`	`Poly-Glu.`
`MUTAGEN`	`27 28`		`KD->AA: Abolishes interaction with other proteins, but not with itself.`
`CONFLICT`	`401 402`		`RG -> TW (in Ref. 3; AAK54603).`
`STRAND`	`19 26`	`8`
`STRAND`	`35 38`	`4`
`STRAND`	`41 43`	`3`
`STRAND`	`48 52`	`5`
`HELIX`	`57 61`	`5`
`STRAND`	`69 73`	`5`
`HELIX`	`83 92`	`10`
`STRAND`	`95 103`	`9`

Sequence information

Length: 416 AA [This is the length of the unprocessed precursor]

Molecular weight: 46606 Da [This is the MW of the unprocessed precursor]

CRC64: 8FDE0D78BB26C006 [This is a checksum on the sequence]

        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

Q9EP80 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools