ID   A0A067R916_ZOONE        Unreviewed;       432 AA.
AC   A0A067R916;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-NOV-2024, entry version 41.
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   ORFNames=L798_11252 {ECO:0000313|EMBL:KDR14946.1};
OS   Zootermopsis nevadensis (Dampwood termite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Termopsidae; Zootermopsis.
OX   NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR14946.1, ECO:0000313|Proteomes:UP000027135};
RN   [1] {ECO:0000313|EMBL:KDR14946.1, ECO:0000313|Proteomes:UP000027135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KDR14946.1};
RX   PubMed=24845553; DOI=10.1038/ncomms4636;
RA   Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA   Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA   Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA   Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA   Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA   Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA   Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA   Liebig J.;
RT   "Molecular traces of alternative social organization in a termite genome.";
RL   Nat. Commun. 5:3636-3636(2014).
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   -!- SUBUNIT: Monomer and homodimer. Interacts with CXADR. Interacts
CC       presynaptically with the glutamate receptors GRIA2, GRIA3, GRIK3,
CC       isoform 3 of GRIA4, isoform A of GRM4, GRM7 and GRM8; with NAPA and
CC       NAPB; and with BTG2. The interaction with NAPA and NAPB disrupts the
CC       interaction with GRIA2, conducting to the internalization of GRIA2.
CC       Interacts with PRKCA; with the amine transporters SLC6A2 and SLC6A3;
CC       with the channels ASIC1 and ASIC2; with the GTP-binding proteins ARF1
CC       and ARF3; with the ephrin receptor tyrosine kinases EPHA7, EPHB1 and
CC       EPHB2; with ERBB2 and through its PDZ domain with the C-terminal tail
CC       of PRLHR. Interacts with UNC5A. Interacts (via AH domain) with
CC       NCS1/FREQ; in a calcium-dependent manner. Interacts with F-actin and
CC       associates with the ARP2/3 complex. Interacts (via PDZ domain) with
CC       ARF1 (activated); the interaction blocks Arp2/3 complex inhibition.
CC       {ECO:0000256|ARBA:ARBA00046977}.
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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Postsynaptic density
CC       {ECO:0000256|ARBA:ARBA00034105}. Synapse, synaptosome
CC       {ECO:0000256|ARBA:ARBA00034102}.
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DR   EMBL; KK852855; KDR14946.1; -; Genomic_DNA.
DR   STRING; 136037.A0A067R916; -.
DR   EnsemblMetazoa; KDR14946; KDR14946; L798_11252.
DR   eggNOG; KOG3651; Eukaryota.
DR   InParanoid; A0A067R916; -.
DR   Proteomes; UP000027135; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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:0005886; C:plasma membrane; IEA:GOC.
DR   GO; GO:0014069; C:postsynaptic density; IEA:TreeGrafter.
DR   GO; GO:0098842; C:postsynaptic early endosome; IEA:TreeGrafter.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:TreeGrafter.
DR   GO; GO:0032588; C:trans-Golgi network membrane; IEA:TreeGrafter.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR   GO; GO:0005080; F:protein kinase C binding; IEA:TreeGrafter.
DR   GO; GO:0097062; P:dendritic spine maintenance; IEA:TreeGrafter.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:TreeGrafter.
DR   GO; GO:0002092; P:positive regulation of receptor internalization; IEA:TreeGrafter.
DR   GO; GO:0043113; P:receptor clustering; IEA:TreeGrafter.
DR   GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IEA:TreeGrafter.
DR   CDD; cd07659; BAR_PICK1; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   FunFam; 1.20.1270.60:FF:000023; Interacting with PRKCA; 1.
DR   FunFam; 2.30.42.10:FF:000073; Interacting with PRKCA; 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   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Synaptosome {ECO:0000256|ARBA:ARBA00022599};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          46..129
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          168..381
FT                   /note="AH"
FT                   /evidence="ECO:0000259|PROSITE:PS50870"
FT   REGION          393..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..415
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  48689 MW;  C7EFB2C0A518D2FF CRC64;
     MWPSNSRYLG YIPLQRAEVE YNSLHGDSRL KAIMEDRMGM TVTSGSVTIR KDSSNLIGVS
     IGGGATLCPC LYIVQVFDNT PAAKDGTLQS GDELVGVNGA SVKGKTKVEV AKMIQASKDE
     VTINYNKLHA DPQQGKTLDI VLKKVKHRLV ENMSSATADA LGLSRAILCN DTLVKKLEEL
     EQTEMMYRGL VEHAKRVLKA FFDLLQVYKA FGDTFAGIGV REPQPRASEA FRQFGDYHRQ
     MEKFGIKMLK SVKPILSDLG TYLYKAIPDT KLTIRKYADT KFEYLSYCLK VKEMDDEEYS
     YGALQEPLYR VETGNYEYRL ILRCRQDARA RFARLRSDVL VKMELLDNKH VQDVVWQLQR
     LVAGLAEFHG DTLTLLQGXX XXXXXXXXXX XYKSTSPVVQ DGTEEEEEDD DDLLQADEAK
     EEFVSLIPEL GD
//