ID A0A067R916_ZOONE Unreviewed; 432 AA. AC A0A067R916; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 14-DEC-2022, entry version 32. 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 -!- 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}. Synapse, synaptosome CC {ECO:0000256|ARBA:ARBA00034102}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KK852855; KDR14946.1; -; Genomic_DNA. DR STRING; 136037.KDR14946; -. DR EnsemblMetazoa; KDR14946; KDR14946; L798_11252. DR eggNOG; KOG3651; Eukaryota. DR Proteomes; UP000027135; Unassembled WGS sequence. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt. DR GO; GO:0016020; C:membrane; 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:0045202; C:synapse; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro. DR CDD; cd07659; BAR_PICK1; 1. DR Gene3D; 1.20.1270.60; -; 1. DR Gene3D; 2.30.42.10; -; 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 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:UP000027135}; KW Synapse {ECO:0000256|ARBA:ARBA00022599}; KW Synaptosome {ECO:0000256|ARBA:ARBA00022599}. 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 //