ID U3J688_ANAPP Unreviewed; 429 AA.
AC U3J688;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=PRKCA-binding protein {ECO:0000256|ARBA:ARBA00017975};
DE AltName: Full=Protein interacting with C kinase 1 {ECO:0000256|ARBA:ARBA00032804};
DE AltName: Full=Protein kinase C-alpha-binding protein {ECO:0000256|ARBA:ARBA00031097};
GN Name=PICK1 {ECO:0000313|Ensembl:ENSAPLP00000015015.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000015015.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000015015.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000015015.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Probable adapter protein that bind to and organize the
CC subcellular localization of a variety of membrane proteins containing
CC some PDZ recognition sequence. Involved in the clustering of various
CC receptors, possibly by acting at the receptor internalization level.
CC Plays a role in synaptic plasticity by regulating the trafficking and
CC internalization of AMPA receptors. May be regulated upon PRKCA
CC activation. May regulate ASIC1/ASIC3 channel. Regulates actin
CC polymerization by inhibiting the actin-nucleating activity of the
CC Arp2/3 complex; the function is competitive with nucleation promoting
CC factors and is linked to neuronal morphology regulation and AMPA
CC receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex
CC involved in regulation of synaptic plasicity of excitatory synapses and
CC required for spine shrinkage during long-term depression (LTD).
CC Involved in regulation of astrocyte morphology, antagonistic to Arp2/3
CC complex activator WASL/N-WASP function.
CC {ECO:0000256|ARBA:ARBA00033721}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Synapse, synaptosome
CC {ECO:0000256|ARBA:ARBA00034102}.
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DR AlphaFoldDB; U3J688; -.
DR STRING; 8840.ENSAPLP00000015015; -.
DR Ensembl; ENSAPLT00000015805.2; ENSAPLP00000015015.2; ENSAPLG00000015117.2.
DR GeneTree; ENSGT00950000183040; -.
DR Proteomes; UP000016666; Chromosome 1.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0140090; F:membrane curvature sensor activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR GO; GO:0015844; P:monoamine transport; IEA:Ensembl.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
DR CDD; cd07659; BAR_PICK1; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR010504; AH_dom.
DR InterPro; IPR030798; Arfaptin_fam.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR037959; PICK1_BAR.
DR PANTHER; PTHR12141; ARFAPTIN-RELATED; 1.
DR PANTHER; PTHR12141:SF1; PRKCA-BINDING PROTEIN; 1.
DR Pfam; PF06456; Arfaptin; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM01015; Arfaptin; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50870; AH; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Synaptosome {ECO:0000256|ARBA:ARBA00022599}.
FT DOMAIN 42..125
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 164..377
FT /note="AH"
FT /evidence="ECO:0000259|PROSITE:PS50870"
FT REGION 393..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 47988 MW; 69E68543E3E6C888 CRC64;
MFFKGAQERC GADGLCSGGR MFAELDYDIE EDKLGIPTVP GTVTLKKDAQ NLIGISIGGG
AQYCPCLYIV QVFDNTPAAL DGTVAAGDEI TGVNGKSVKG KTKVEVAKMI QMVKGEVTIH
YNKLQADPKQ GKSLDIVLKK VKHRLVENMS SGTADALGLS RAILCNDGLV KRLEELERTA
ELYKGLTEHT KSLLRAFFEL SQTHRAFGDV FSVIGVREPQ PAASEAFVKF ADAHRNIEKF
GIHLLKTIKP MLTDLNTYLN KAIPDTRLTI KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL
GEPLYRVSTG NYEYRLILRC RQEARTRFAK MRKDVLEKIE LLDQKHVQDI VFQLQRFVST
MSKYYDDCYA VLRDADVFPI EVDLARTTLS YGQKDTYTDG AEEEEEGGGS DREKSGKEDA
NGEKLIDDA
//
