ID A0A0L0C6C9_LUCCU Unreviewed; 649 AA.
AC A0A0L0C6C9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=FF38_12502 {ECO:0000313|EMBL:KNC27835.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC27835.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC27835.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC27835.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC27835.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC27835.1}.
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DR EMBL; JRES01000841; KNC27835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0C6C9; -.
DR STRING; 7375.A0A0L0C6C9; -.
DR EnsemblMetazoa; KNC27835; KNC27835; FF38_12502.
DR OMA; APYCPCI; -.
DR Proteomes; UP000037069; 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:0046872; F:metal ion 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 Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Synaptosome {ECO:0000256|ARBA:ARBA00022599}.
FT DOMAIN 125..208
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 247..460
FT /note="AH"
FT /evidence="ECO:0000259|PROSITE:PS50870"
FT REGION 480..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 72077 MW; 4800AFF9B7C861BD CRC64;
MEDNTTTPLL PIEALSFDIT PICTDPFEPK MGELLNMSST APPIAELASV NDSTNTGTTK
ESSLTLDTDD SPATVCQLVD DNLLSNDVTA TVVYTASAFE ADRFSELAKQ KFELERLGMT
VSTKSVVVVK DDTNLIGISI GGGAPLCPCL YIVQVFDGTP AAREGSLESG DELLAINNTS
VKGKTKVQVA KMIQTATQQV VIHYNKLHAD PERGKSLDII LKKLKHRIVD NMSSNTADTL
GLSRAILCND SLVKRLEELE GTEMMYKGMV DHARRMLKAY YDLLQTYRAF GDCFMRISTR
EPQLRASEAF RMFGELHRNL EKDGLDVIKN IKPILDDLGT YLHKAIPDTK LTVRRYMDAK
FTYLSYCLKV KEMDDEEHSF AAIQEPLYRV ETGNYEYRLI LRCRQDARGK FAKLRTDVLE
KMELLECKHA NDLSKQLRNL LDSLAKLNKT ITDRMDTIPN LFPIEVDFKD TDFQYKSSVL
EPQKLDDNEE EEQNQISKTK AKNSTTADDS ADVICGLEAI EQPAPILNVP AKVQDIVSLT
DNPADNLMME TANENDQLLK DLGLLDIDLS SKSISSTPTL NKITSPNGFY DFDLFLNQNS
GMTTASCVNA ADTTTQFETK QTSSSAATTS QLGNDLMAAN ALETDLLLQ
//
