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PRKCA-binding protein (Protein interacting with C kinase 1) (Protein kinase C-alpha-binding protein)

 PICK1_HUMAN             Reviewed;         415 AA.
Q9NRD5; B3KS52; O95906;
02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
02-AUG-2002, sequence version 2.
10-OCT-2018, entry version 172.
RecName: Full=PRKCA-binding protein;
AltName: Full=Protein interacting with C kinase 1;
AltName: Full=Protein kinase C-alpha-binding protein;
Name=PICK1; Synonyms=PRKCABP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ARF1 AND
ARF3, AND MUTAGENESIS OF 27-LYS-ASP-28.
TISSUE=B-cell;
PubMed=10623590; DOI=10.1006/bbrc.1999.1932;
Takeya R., Takeshige K., Sumimoto H.;
"Interaction of the PDZ domain of human PICK1 with class I ADP-
ribosylation factors.";
Biochem. Biophys. Res. Commun. 267:149-155(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Zhu X., Chung I., Scholl P.R.;
"Protein kinases interacting with the human PICK1 protein.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12529303; DOI=10.1101/gr.695703;
Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J.,
Knowles S., Bye J.M., Beare D.M., Dunham I.;
"Reevaluating human gene annotation: a second-generation analysis of
chromosome 22.";
Genome Res. 13:27-36(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH PRLHR.
PubMed=11641419;
Lin S.H.S., Arai A.C., Wang Z., Nothacker H.-P., Civelli O.;
"The carboxyl terminus of the prolactin-releasing peptide receptor
interacts with PDZ domain proteins involved in alpha-amino-3-hydroxy-
5-methylisoxazole-4-propionic acid receptor clustering.";
Mol. Pharmacol. 60:916-923(2001).
[10]
INTERACTION WITH SLC6A2 AND SLC6A3, AND MUTAGENESIS OF 27-LYS-ASP-28.
PubMed=11343649; DOI=10.1016/S0896-6273(01)00267-7;
Torres G.E., Yao W.-D., Mohn A.R., Quan H., Kim K.-M., Levey A.I.,
Staudinger J., Caron M.G.;
"Functional interaction between monoamine plasma membrane transporters
and the synaptic PDZ domain-containing protein PICK1.";
Neuron 30:121-134(2001).
[11]
INTERACTION WITH ASIC1 AND ASIC2, AND MUTAGENESIS OF 27-LYS-ASP-28.
PubMed=11802773; DOI=10.1042/0264-6021:3610443;
Hruska-Hageman A.M., Wemmie J.A., Price M.P., Welsh M.J.;
"Interaction of the synaptic protein PICK1 (protein interacting with C
kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+
channel 1) and ASIC (acid-sensing ion channel).";
Biochem. J. 361:443-450(2002).
[12]
INTERACTION WITH CXADR.
PubMed=15304526; DOI=10.1242/jcs.01300;
Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L.,
Zabner J.;
"A role for the PDZ-binding domain of the coxsackie B virus and
adenovirus receptor (CAR) in cell adhesion and growth.";
J. Cell Sci. 117:4401-4409(2004).
[13]
INTERACTION WITH GRIA2 AND PRKCA, AND MUTAGENESIS OF LYS-27.
PubMed=15247289; DOI=10.1074/jbc.M404499200;
Dev K.K., Nakanishi S., Henley J.M.;
"The PDZ domain of PICK1 differentially accepts protein kinase C-alpha
and GluR2 as interacting ligands.";
J. Biol. Chem. 279:41393-41397(2004).
[14]
FUNCTION, AND PHOSPHORYLATION AT THR-82.
PubMed=20403402; DOI=10.1016/j.neuint.2010.04.006;
Shao X., Zhu L., Wang Y., Lu Y., Wang W., Zhu J., Shen Y., Xia J.,
Luo J.;
"Threonine 82 at the PDZ domain of PICK1 is critical for AMPA receptor
interaction and localization.";
Neurochem. Int. 56:962-970(2010).
[15]
X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 19-105.
PubMed=17384233; DOI=10.1110/ps.062657507;
Elkins J.M., Papagrigoriou E., Berridge G., Yang X., Phillips C.,
Gileadi C., Savitsky P., Doyle D.A.;
"Structure of PICK1 and other PDZ domains obtained with the help of
self-binding C-terminal extensions.";
Protein Sci. 16:683-694(2007).
-!- 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 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.
{ECO:0000269|PubMed:20403402}.
-!- 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 ASIC1 and ASIC2;
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.
Interacts with UNC5A. Interacts (via AH domain) with NCS1/FREQ; in
a calcium-dependent manner. Interacts with F-actin and associates
with the ARP2/3 complex. Interacts (via PDZ domain) with ARF1
(activated); the interaction blocks Arp2/3 complex inhibition.
{ECO:0000269|PubMed:10623590, ECO:0000269|PubMed:11343649,
ECO:0000269|PubMed:11641419, ECO:0000269|PubMed:11802773,
ECO:0000269|PubMed:15247289, ECO:0000269|PubMed:15304526}.
-!- INTERACTION:
Q08117-2:AES; NbExp=4; IntAct=EBI-79165, EBI-11741437;
P78348:ASIC1; NbExp=3; IntAct=EBI-79165, EBI-79189;
Q16515:ASIC2; NbExp=3; IntAct=EBI-79165, EBI-79149;
P38432:COIL; NbExp=3; IntAct=EBI-79165, EBI-945751;
Q9NP66:HMG20A; NbExp=4; IntAct=EBI-79165, EBI-740641;
Q03933:HSF2; NbExp=4; IntAct=EBI-79165, EBI-2556750;
Q7L273:KCTD9; NbExp=4; IntAct=EBI-79165, EBI-4397613;
Q9BV20:MRI1; NbExp=4; IntAct=EBI-79165, EBI-747381;
P48775:TDO2; NbExp=4; IntAct=EBI-79165, EBI-743494;
Q8TBB0:THAP6; NbExp=4; IntAct=EBI-79165, EBI-3925505;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane
{ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density {ECO:0000250}.
Cell junction, synapse, synaptosome {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present
at excitatory synapses. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NRD5-1; Sequence=Displayed;
Name=2;
IsoId=Q9NRD5-2; Sequence=VSP_054902, VSP_054903;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The AH domain mediates binding to F-actin. {ECO:0000250}.
-!- DOMAIN: The unoccupied PDZ domain is probably involved in
allosteric modulation by forming an intramolecular bridge with the
AH domain leading to a 'closed' formation. Binding of a PDZ
ligand, such as GRIA2, allows enhanced interactions with F-actin
and the Arp2/3 complex thus enhanced inhibition of actin
polymerization (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylation at Thr-82 appears to inhibit the interaction
with AMPA receptors. {ECO:0000269|PubMed:20403402}.
-!- PTM: Palmitoylation on Cys-413 is essential for long-term synaptic
depression (LTD). {ECO:0000250}.
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EMBL; AB026491; BAA89294.1; -; mRNA.
EMBL; AF231710; AAF97502.1; -; mRNA.
EMBL; AL049654; CAB41082.1; -; mRNA.
EMBL; CR456550; CAG30436.1; -; mRNA.
EMBL; AK092818; BAG52614.1; -; mRNA.
EMBL; AL031587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60208.1; -; Genomic_DNA.
EMBL; BC017561; AAH17561.1; -; mRNA.
CCDS; CCDS13965.1; -. [Q9NRD5-1]
PIR; JC7167; JC7167.
RefSeq; NP_001034672.1; NM_001039583.1. [Q9NRD5-1]
RefSeq; NP_001034673.1; NM_001039584.1. [Q9NRD5-1]
RefSeq; NP_036539.1; NM_012407.3. [Q9NRD5-1]
UniGene; Hs.180871; -.
PDB; 2GZV; X-ray; 1.12 A; A=19-105.
PDB; 6AR4; X-ray; 1.69 A; A/B=1-105.
PDB; 6BJN; X-ray; 2.43 A; A/B=1-105.
PDB; 6BJO; X-ray; 1.75 A; A/B=1-105.
PDBsum; 2GZV; -.
PDBsum; 6AR4; -.
PDBsum; 6BJN; -.
PDBsum; 6BJO; -.
ProteinModelPortal; Q9NRD5; -.
SMR; Q9NRD5; -.
BioGrid; 114849; 70.
CORUM; Q9NRD5; -.
IntAct; Q9NRD5; 341.
MINT; Q9NRD5; -.
STRING; 9606.ENSP00000349465; -.
MoonDB; Q9NRD5; Predicted.
iPTMnet; Q9NRD5; -.
PhosphoSitePlus; Q9NRD5; -.
SwissPalm; Q9NRD5; -.
BioMuta; PICK1; -.
DMDM; 22095990; -.
EPD; Q9NRD5; -.
MaxQB; Q9NRD5; -.
PaxDb; Q9NRD5; -.
PeptideAtlas; Q9NRD5; -.
PRIDE; Q9NRD5; -.
ProteomicsDB; 82339; -.
DNASU; 9463; -.
Ensembl; ENST00000356976; ENSP00000349465; ENSG00000100151. [Q9NRD5-1]
Ensembl; ENST00000404072; ENSP00000385205; ENSG00000100151. [Q9NRD5-1]
GeneID; 9463; -.
KEGG; hsa:9463; -.
UCSC; uc003auq.4; human. [Q9NRD5-1]
CTD; 9463; -.
DisGeNET; 9463; -.
EuPathDB; HostDB:ENSG00000100151.15; -.
GeneCards; PICK1; -.
H-InvDB; HIX0175461; -.
HGNC; HGNC:9394; PICK1.
HPA; HPA067384; -.
HPA; HPA072674; -.
MalaCards; PICK1; -.
MIM; 605926; gene.
neXtProt; NX_Q9NRD5; -.
OpenTargets; ENSG00000100151; -.
PharmGKB; PA33760; -.
eggNOG; KOG3651; Eukaryota.
eggNOG; ENOG410YZG6; LUCA.
GeneTree; ENSGT00440000033690; -.
HOGENOM; HOG000007646; -.
HOVERGEN; HBG053600; -.
InParanoid; Q9NRD5; -.
OMA; TIKPMLH; -.
OrthoDB; EOG091G08SM; -.
PhylomeDB; Q9NRD5; -.
TreeFam; TF314945; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
SignaLink; Q9NRD5; -.
SIGNOR; Q9NRD5; -.
ChiTaRS; PICK1; human.
EvolutionaryTrace; Q9NRD5; -.
GeneWiki; PICK1; -.
GenomeRNAi; 9463; -.
PRO; PR:Q9NRD5; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100151; Expressed in 158 organ(s), highest expression level in adenohypophysis.
CleanEx; HS_PICK1; -.
ExpressionAtlas; Q9NRD5; baseline and differential.
Genevisible; Q9NRD5; HS.
GO; GO:0016235; C:aggresome; IDA:HPA.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0071933; F:Arp2/3 complex binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0001664; F:G-protein coupled receptor binding; ISS:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; ISS:ParkinsonsUK-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; ISS:ParkinsonsUK-UCL.
GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
GO; GO:0036294; P:cellular response to decreased oxygen levels; ISS:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
GO; GO:0097062; P:dendritic spine maintenance; ISS:UniProtKB.
GO; GO:0097061; P:dendritic spine organization; ISS:UniProtKB.
GO; GO:0043045; P:DNA methylation involved in embryo development; NAS:UniProtKB.
GO; GO:0043046; P:DNA methylation involved in gamete generation; TAS:UniProtKB.
GO; GO:0021782; P:glial cell development; ISS:UniProtKB.
GO; GO:0060292; P:long term synaptic depression; ISS:UniProtKB.
GO; GO:0015844; P:monoamine transport; IDA:UniProtKB.
GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
GO; GO:0045161; P:neuronal ion channel clustering; TAS:UniProtKB.
GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; NAS:UniProtKB.
CDD; cd07659; BAR_PICK1; 1.
Gene3D; 1.20.1270.60; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR010504; AH_dom.
InterPro; IPR030798; Arfaptin_fam.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR037959; PICK1_BAR.
PANTHER; PTHR12141; PTHR12141; 1.
Pfam; PF06456; Arfaptin; 1.
Pfam; PF00595; PDZ; 1.
SMART; SM01015; Arfaptin; 1.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50870; AH; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; Calcium;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Lipoprotein; Membrane; Metal-binding; Palmitate;
Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
Synapse; Synaptosome; Zinc.
CHAIN 1 415 PRKCA-binding protein.
/FTId=PRO_0000058427.
DOMAIN 22 105 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 144 357 AH. {ECO:0000255|PROSITE-
ProRule:PRU00294}.
COMPBIAS 382 388 Poly-Glu.
METAL 44 44 Zinc. {ECO:0000250}.
METAL 46 46 Zinc. {ECO:0000250}.
MOD_RES 82 82 Phosphothreonine.
{ECO:0000269|PubMed:20403402}.
LIPID 413 413 S-palmitoyl cysteine; by DHHC8.
{ECO:0000250}.
VAR_SEQ 279 364 ALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKM
ELLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPI
EVDL -> VSVGGGGGLVLPPTWSARDSRWLRPTRERPGGL
GWTLVPGDLGPSSQSRSLGLGVLGTRPGTTPSVWGTLGGKS
DFLHSYEALLSV (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054902.
VAR_SEQ 365 415 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054903.
MUTAGEN 27 28 KD->AA: Abolishes interaction with other
proteins, but not with itself.
{ECO:0000269|PubMed:10623590,
ECO:0000269|PubMed:11343649,
ECO:0000269|PubMed:11802773}.
MUTAGEN 27 27 K->E: Abolishes interaction with GRIA2,
but not with PRKCA.
{ECO:0000269|PubMed:15247289}.
CONFLICT 7 7 Y -> F (in Ref. 2; AAF97502).
{ECO:0000305}.
CONFLICT 16 16 Missing (in Ref. 2; AAF97502).
{ECO:0000305}.
CONFLICT 236 236 N -> NI (in Ref. 2; AAF97502).
{ECO:0000305}.
STRAND 21 26 {ECO:0000244|PDB:2GZV}.
STRAND 34 39 {ECO:0000244|PDB:2GZV}.
STRAND 47 52 {ECO:0000244|PDB:2GZV}.
HELIX 57 61 {ECO:0000244|PDB:2GZV}.
STRAND 69 73 {ECO:0000244|PDB:2GZV}.
HELIX 83 92 {ECO:0000244|PDB:2GZV}.
STRAND 95 102 {ECO:0000244|PDB:2GZV}.
SEQUENCE 415 AA; 46600 MW; C569FD8AA5028B90 CRC64;
MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV QVFDNTPAAL
DGTVAAGDEI TGVNGRSIKG KTKVEVAKMI QEVKGEVTIH YNKLQADPKQ GMSLDIVLKK
VKHRLVENMS SGTADALGLS RAILCNDGLV KRLEELERTA ELYKGMTEHT KNLLRAFYEL
SQTHRAFGDV FSVIGVREPQ PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN
KAIPDTRLTI KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL GEPLYRVSTG NYEYRLILRC
RQEARARFSQ MRKDVLEKME LLDQKHVQDI VFQLQRLVST MSKYYNDCYA VLRDADVFPI
EVDLAHTTLA YGLNQEEFTD GEEEEEEEDT AAGEPSRDTR GAAGPLDKGG SWCDS


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