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Database: UniProt
Entry: A0A016VM04_9BILA
LinkDB: A0A016VM04_9BILA
Original site: A0A016VM04_9BILA 
ID   A0A016VM04_9BILA        Unreviewed;       408 AA.
AC   A0A016VM04;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
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   Name=Acey_s0008.g193 {ECO:0000313|EMBL:EYC27803.1};
GN   Synonyms=Acey-Y57G11C.22 {ECO:0000313|EMBL:EYC27803.1};
GN   ORFNames=Y032_0008g193 {ECO:0000313|EMBL:EYC27803.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC27803.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(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, 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:EYC27803.1}.
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DR   EMBL; JARK01001344; EYC27803.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016VM04; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
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; 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   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
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"
FT   DOMAIN          136..349
FT                   /note="AH"
FT                   /evidence="ECO:0000259|PROSITE:PS50870"
SQ   SEQUENCE   408 AA;  46248 MW;  FBA6AC80962D44BB CRC64;
     MEEDRMGMRI QSETIEIMKD EKGLVGISIG GGHPFCPCVY VVQIFDKSPA EADGRIRAGD
     EVVAVNGICV KGERKSAVAQ LIQCSTNPVK ITINKLETDS SKGKTLDIMM KKIKHKMVEF
     MDADSADALG LSRAILCNDP LLKKMKVLED NTLLYRNLIG FFSDLFYFQE KISHYQKEFG
     DVFCELAAHE AHANANEAFT VFGEAHRQLS KKQSDSLKNL RPLIADLVTY VDKVIPDTQL
     TLKKYLDVKY EYLSYCLKLK EMDDEEMEYH SLNEGLYRVE TGNYEYRLML RCRQETRQKF
     VQMRNDVMVK IELLDQKHVR DIALHLTNLA SIMKDCLSEC SSVLQNTQNS PIEIDITQGG
     KESSLYNSAT GDESTEDNGN VEHVVEEQLV NTSLPEDLAN DINLIDIN
//
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