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Database: UniProt
Entry: A0A0M5J3W9_DROBS
LinkDB: A0A0M5J3W9_DROBS
Original site: A0A0M5J3W9_DROBS 
ID   A0A0M5J3W9_DROBS        Unreviewed;       567 AA.
AC   A0A0M5J3W9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=Dbus_chr2Lg1529 {ECO:0000313|EMBL:ALC39444.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC39444.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC39444.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC39444.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CP012523; ALC39444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M5J3W9; -.
DR   STRING; 30019.A0A0M5J3W9; -.
DR   OMA; APYCPCI; -.
DR   Proteomes; UP000494163; Chromosome 2l 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   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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Synaptosome {ECO:0000256|ARBA:ARBA00022599};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          95..178
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          217..430
FT                   /note="AH"
FT                   /evidence="ECO:0000259|PROSITE:PS50870"
SQ   SEQUENCE   567 AA;  63665 MW;  019A32B3E03D7B43 CRC64;
     MLTDDDDFYY EDKIVRPCNS STEATPVLIQ LNDDSITGTE VTKRQPELKP NLSAWQSDAD
     TAVLCAGHNT MSDYGQHQKQ LNELDRLGMT VTTNAVVITK DQSNLIGISI GGGAPMCPCL
     YIVQVFDGTP AAREGSLQSG DELLAVNSVS VKGKTKVEVA KMIQTATDEV TVHYNKLHAD
     PEQGKTLDII LKKLKHRIVD NLSSNTADTL GLSRAILCND SLVKRLEELE GTELMYKGLV
     EHARRMLKAY YDLLQTYKSF GDCFTQISAH EPQQRASEAF RTFGEFHRAL EKDGLTIIKQ
     IKPVLADLGT YLNKAIPDTK LTVRRYADAK FTYLSYCLKV KEMDDEEHGF AALQEPLYRV
     ETGNYEYRLI LRCRQDARSK FAKLRTDVLE KMELLECKHA MDLNKQLRSL LESLADLHRS
     LVDRLDTLPP LFPIEVDFKE TDFQYKSSTL KPQELDDDEI EDNANSHTNN KVIYGLEAVE
     QPAPIITMET KAAEPSSNEN ESLLKELGLQ DVDLLSNPQT ISNQKDSIAA QKEAYDFDLF
     LNQANATTSL ERDLMSANAS ETDLLLQ
//
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