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Database: UniProt
Entry: A0A1I8B203_MELHA
LinkDB: A0A1I8B203_MELHA
Original site: A0A1I8B203_MELHA 
ID   A0A1I8B203_MELHA        Unreviewed;       213 AA.
AC   A0A1I8B203;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
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};
OS   Meloidogyne hapla (Root-knot nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig1234.frz3.gene1};
RN   [1] {ECO:0000313|WBParaSite:MhA1_Contig1234.frz3.gene1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) 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, 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; A0A1I8B203; -.
DR   WBParaSite; MhA1_Contig1234.frz3.gene1; MhA1_Contig1234.frz3.gene1; MhA1_Contig1234.frz3.gene1.
DR   OMA; HCPCIYI; -.
DR   Proteomes; UP000095281; Unplaced.
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; 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   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; SM00228; PDZ; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Synaptosome {ECO:0000256|ARBA:ARBA00022599}.
FT   DOMAIN          14..97
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   213 AA;  23501 MW;  C6F87C6848A48C72 CRC64;
     MFDLTNNLRL NADVIEIEKD TKGRIGIAIG GGAPICPCLY IVQIFENTPA KKNALIGLGD
     EIVAINGESV RGFDKSEVAS LIKEAQGPIK ISVNRLQFDS ENASLTIDIL LKKFKHRFVA
     SIDDNTADAL GLSRAILCND VLAKLKEKLE SNQKFYRNLI KKAEEMVKYY QAISDTQSGI
     GSVFSEISIK EVIGDEAIIA RMILMVFQMF ISL
//
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