GenomeNet

Database: UniProt
Entry: M7AP48_CHEMY
LinkDB: M7AP48_CHEMY
Original site: M7AP48_CHEMY 
ID   M7AP48_CHEMY            Unreviewed;       457 AA.
AC   M7AP48;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=UY3_15877 {ECO:0000313|EMBL:EMP27031.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP27031.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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   ---------------------------------------------------------------------------
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; KB574221; EMP27031.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7AP48; -.
DR   STRING; 8469.M7AP48; -.
DR   eggNOG; KOG3651; Eukaryota.
DR   Proteomes; UP000031443; 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   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:UP000031443};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Synaptosome {ECO:0000256|ARBA:ARBA00022599};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          72..155
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          194..407
FT                   /note="AH"
FT                   /evidence="ECO:0000259|PROSITE:PS50870"
FT   REGION          426..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  50860 MW;  523F346BB96EA76C CRC64;
     MARPGPAAVI CFSNTHDLPQ MPSNTLALPS QVCDVPPSDM TEAVALFTRL TPPFLMPSSV
     PSVSGIPTVP GTVTLKKDSQ NLIGISIGGG AQYCPCLYIV QVFDNTPAAL DGTVAAGDEI
     TGVNGKSVKG KTKVEVAKMI QVVKGEVTIH YNKLQADPKQ GKSLDIVLKK VKHRLVENMS
     SGTADALGLS RAILCNDGLV KRLEELERTA ELYKGMTEHT KSLLRAFFEL SQTHRAFGDV
     FSVIGVREPQ PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN KAIPDTRLTI
     KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL GEPLYRVSTG NYEYRLVLRC RQEARTRFAK
     MRKDVLEKIE LLDQKHVQDI VFQLQRFVST MSKYNDDCYA VLRDADVFPI EVDLARTTLS
     YGQKDVFSDG AEEEEEVGER EARRKEEANG EKLIDDA
//
DBGET integrated database retrieval system