PICK1_RAT
ID PICK1_RAT Reviewed; 416 AA.
AC Q9EP80; Q546X4; Q925D1;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=PRKCA-binding protein;
DE AltName: Full=Protein interacting with C kinase 1;
DE AltName: Full=Protein kinase C-alpha-binding protein;
GN Name=Pick1; Synonyms=Prkcabp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRIA2; GRIA3 AND ISOFORM 4C OF
RP GRIA4, AND MUTAGENESIS OF 27-LYS-ASP-28.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10027300; DOI=10.1016/s0896-6273(00)80689-3;
RA Xia J., Zhang X., Staudinger J., Huganir R.L.;
RT "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein
RT PICK1.";
RL Neuron 22:179-187(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRM4; GRM7; GRM8; GRIK3 AND
RP PRKCA, AND MUTAGENESIS OF 27-LYS-ASP-28.
RC TISSUE=Brain;
RX PubMed=11122333; DOI=10.1046/j.1460-9568.2000.01309.x;
RA El Far O., Airas J., Wischmeyer E., Nehring R.B., Karschin A., Betz H.;
RT "Interaction of the C-terminal tail region of the metabotropic glutamate
RT receptor 7 with the protein kinase C substrate PICK1.";
RL Eur. J. Neurosci. 12:4215-4221(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH BTG2.
RX PubMed=11237868; DOI=10.1042/0264-6021:3540635;
RA Lin W.-J., Chang Y.-F., Wang W.-L., Huang C.-Y.F.;
RT "Mitogen-stimulated TIS21 protein interacts with a protein-kinase-Calpha-
RT binding protein rPICK1.";
RL Biochem. J. 354:635-643(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Chen W., Rosenberg P.A.;
RT "Interaction of glutamate transporter GLT1b with PICK1, a protein
RT regulating targeting and trafficking at excitatory synapses.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH GRIA2; GRIA3 AND GRIA4 ISOFORM 4C.
RX PubMed=10340301; DOI=10.1016/s0028-3908(98)00230-5;
RA Dev K.K., Nishimune A., Henley J.M., Nakanishi S.;
RT "The protein kinase C alpha binding protein PICK1 interacts with short but
RT not long form alternative splice variants of AMPA receptor subunits.";
RL Neuropharmacology 38:635-644(1999).
RN [6]
RP CHARACTERIZATION, AND MUTAGENESIS OF 27-LYS-ASP-28.
RX PubMed=11375398; DOI=10.1074/jbc.m102991200;
RA Boudin H., Craig A.M.;
RT "Molecular determinants for PICK1 synaptic aggregation and mGluR7a receptor
RT coclustering: role of the PDZ, coiled-coil, and acidic domains.";
RL J. Biol. Chem. 276:30270-30276(2001).
RN [7]
RP INTERACTION WITH NAPA AND NAPB.
RX PubMed=11931741; DOI=10.1016/s0896-6273(02)00638-4;
RA Hanley J.G., Khatri L., Hanson P.I., Ziff E.B.;
RT "NSF ATPase and alpha-/beta-SNAPs disassemble the AMPA receptor-PICK1
RT complex.";
RL Neuron 34:53-67(2002).
RN [8]
RP INTERACTION WITH UNC5A.
RX PubMed=14672991; DOI=10.1523/jneurosci.23-36-11279.2003;
RA Williams M.E., Wu S.C.-Y., McKenna W.L., Hinck L.;
RT "Surface expression of the netrin receptor UNC5H1 is regulated through a
RT protein kinase C-interacting protein/protein kinase-dependent mechanism.";
RL J. Neurosci. 23:11279-11288(2003).
RN [9]
RP FUNCTION, AND CALCIUM-BINDING.
RX PubMed=16138078; DOI=10.1038/sj.emboj.7600801;
RA Hanley J.G., Henley J.M.;
RT "PICK1 is a calcium-sensor for NMDA-induced AMPA receptor trafficking.";
RL EMBO J. 24:3266-3278(2005).
RN [10]
RP ZINC-BINDING SITES.
RX PubMed=18429931; DOI=10.1111/j.1471-4159.2008.05434.x;
RA Shi Y., Zhang L., Yuan J., Xiao H., Yang X., Niu L.;
RT "Zinc binding site in PICK1 is dominantly located at the CPC motif of its
RT PDZ domain.";
RL J. Neurochem. 106:1027-1034(2008).
RN [11]
RP FUNCTION, ACTIN-BINDING, ASSOCIATION WITH THE ARP2/3 COMPLEX, AND
RP MUTAGENESIS OF 251-LYS-LYS-252 AND TRP-413.
RX PubMed=18297063; DOI=10.1038/ncb1688;
RA Rocca D.L., Martin S., Jenkins E.L., Hanley J.G.;
RT "Inhibition of Arp2/3-mediated actin polymerization by PICK1 regulates
RT neuronal morphology and AMPA receptor endocytosis.";
RL Nat. Cell Biol. 10:259-271(2008).
RN [12]
RP INTERACTION WITH NCS1.
RX PubMed=19109914; DOI=10.1016/j.neuron.2008.10.050;
RA Jo J., Heon S., Kim M.J., Son G.H., Park Y., Henley J.M., Weiss J.L.,
RA Sheng M., Collingridge G.L., Cho K.;
RT "Metabotropic glutamate receptor-mediated LTD involves two interacting
RT Ca(2+) sensors, NCS-1 and PICK1.";
RL Neuron 60:1095-1111(2008).
RN [13]
RP FUNCTION.
RX PubMed=21252856; DOI=10.1038/emboj.2010.357;
RA Nakamura Y., Wood C.L., Patton A.P., Jaafari N., Henley J.M., Mellor J.R.,
RA Hanley J.G.;
RT "PICK1 inhibition of the Arp2/3 complex controls dendritic spine size and
RT synaptic plasticity.";
RL EMBO J. 30:719-730(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [15]
RP FUNCTION.
RX PubMed=23843614; DOI=10.1242/jcs.125146;
RA Murk K., Blanco Suarez E.M., Cockbill L.M., Banks P., Hanley J.G.;
RT "The antagonistic modulation of Arp2/3 activity by N-WASP, WAVE2 and PICK1
RT defines dynamic changes in astrocyte morphology.";
RL J. Cell Sci. 126:3873-3883(2013).
RN [16]
RP INTERACTION WITH ARF1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 27-LYS-ASP-28.
RX PubMed=23889934; DOI=10.1016/j.neuron.2013.05.003;
RA Rocca D.L., Amici M., Antoniou A., Suarez E.B., Halemani N., Murk K.,
RA McGarvey J., Jaafari N., Mellor J.R., Collingridge G.L., Hanley J.G.;
RT "The small GTPase Arf1 modulates Arp2/3-mediated actin polymerization via
RT PICK1 to regulate synaptic plasticity.";
RL Neuron 79:293-307(2013).
RN [17]
RP STRUCTURE BY NMR OF 18-104 IN COMPLEX WITH GRIA2, INTERACTION WITH GRIA2,
RP AND MUTAGENESIS OF CYS-44; CYS-46; LYS-79 AND LYS-81.
RX PubMed=17914463; DOI=10.1038/sj.emboj.7601860;
RA Pan L., Wu H., Shen C., Shi Y., Jin W., Xia J., Zhang M.;
RT "Clustering and synaptic targeting of PICK1 requires direct interaction
RT between the PDZ domain and lipid membranes.";
RL EMBO J. 26:4576-4587(2007).
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. {ECO:0000269|PubMed:16138078,
CC ECO:0000269|PubMed:18297063, ECO:0000269|PubMed:21252856,
CC ECO:0000269|PubMed:23843614}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with CXADR. Interacts
CC presynaptically with the glutamate receptors GRIA2, GRIA3, GRIK3,
CC isoform 3 of GRIA4, isoform A of GRM4, GRM7 and GRM8; with NAPA and
CC NAPB; and with BTG2. The interaction with NAPA and NAPB disrupts the
CC interaction with GRIA2, conducting to the internalization of GRIA2.
CC Interacts with PRKCA; with the amine transporters SLC6A2 and SLC6A3;
CC with the channels ASIC1 and ASIC2; with the GTP-binding proteins ARF1
CC and ARF3; with the ephrin receptor tyrosine kinases EPHA7, EPHB1 and
CC EPHB2; with ERBB2 and through its PDZ domain with the C-terminal tail
CC of PRLHR (By similarity). Interacts with UNC5A. Interacts (via AH
CC domain) with NCS1/FREQ; in a calcium-dependent manner. Interacts with
CC F-actin and associates with the ARP2/3 complex. Interacts (via PDZ
CC domain) with ARF1 (activated); the interaction blocks Arp2/3 complex
CC inhibition. {ECO:0000250, ECO:0000269|PubMed:10027300,
CC ECO:0000269|PubMed:10340301, ECO:0000269|PubMed:11122333,
CC ECO:0000269|PubMed:11237868, ECO:0000269|PubMed:11931741,
CC ECO:0000269|PubMed:14672991, ECO:0000269|PubMed:17914463,
CC ECO:0000269|PubMed:19109914, ECO:0000269|PubMed:23889934}.
CC -!- INTERACTION:
CC Q9EP80; P27049: Btg2; NbExp=3; IntAct=EBI-77728, EBI-78953;
CC Q9EP80; P19491: Gria2; NbExp=13; IntAct=EBI-77728, EBI-77718;
CC Q9EP80; P19492: Gria3; NbExp=7; IntAct=EBI-77728, EBI-77764;
CC Q9EP80; P35400: Grm7; NbExp=2; IntAct=EBI-77728, EBI-6936416;
CC Q9EP80; Q63337: mGluR7; NbExp=2; IntAct=EBI-77728, EBI-6935714;
CC Q9EP80; Q9EP80: Pick1; NbExp=6; IntAct=EBI-77728, EBI-77728;
CC Q9EP80; P42262: GRIA2; Xeno; NbExp=2; IntAct=EBI-77728, EBI-3909876;
CC Q9EP80; Q01959: SLC6A3; Xeno; NbExp=2; IntAct=EBI-77728, EBI-6661445;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:23889934}. Membrane {ECO:0000269|PubMed:23889934};
CC Peripheral membrane protein {ECO:0000269|PubMed:23889934}. Membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Postsynaptic density
CC {ECO:0000269|PubMed:23889934}. Synapse, synaptosome
CC {ECO:0000269|PubMed:23889934}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23889934}. Note=Also membrane-associated, present
CC at excitatory synapses.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DEVELOPMENTAL STAGE: Expressed early in development (E15), and
CC gradually increases, reaching a peak at around 2 weeks after birth.
CC -!- DOMAIN: The AH domain mediates binding to F-actin.
CC -!- DOMAIN: The unoccupied PDZ domain is probably involved in allosteric
CC modulation by forming an intramolecular bridge with the AH domain
CC leading to a 'closed' formation. Binding of a PDZ ligand, such as
CC GRIA2, allows enhanced interactions with F-actin and the Arp2/3 complex
CC thus enhanced inhibition of actin polymerization.
CC -!- PTM: Phosphorylation at Thr-82 appears to inhibit the interaction with
CC AMPA receptors. {ECO:0000250}.
CC -!- PTM: Palmitoylation on Cys-414 is essential for long-term synaptic
CC depression (LTD). {ECO:0000250}.
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DR EMBL; AF327562; AAG48152.1; -; mRNA.
DR EMBL; AJ240083; CAC17808.2; -; mRNA.
DR EMBL; AF373289; AAK54603.1; -; mRNA.
DR EMBL; AF542094; AAO49507.1; -; mRNA.
DR RefSeq; NP_445912.1; NM_053460.1.
DR PDB; 2LUI; NMR; -; A=19-110.
DR PDB; 2PKU; NMR; -; A=18-104.
DR PDB; 3HPK; X-ray; 2.20 A; A/B=1-110.
DR PDB; 3HPM; X-ray; 2.80 A; A/B=19-110.
DR PDBsum; 2LUI; -.
DR PDBsum; 2PKU; -.
DR PDBsum; 3HPK; -.
DR PDBsum; 3HPM; -.
DR AlphaFoldDB; Q9EP80; -.
DR SASBDB; Q9EP80; -.
DR SMR; Q9EP80; -.
DR BioGRID; 250021; 11.
DR CORUM; Q9EP80; -.
DR DIP; DIP-30941N; -.
DR ELM; Q9EP80; -.
DR IntAct; Q9EP80; 14.
DR MINT; Q9EP80; -.
DR STRING; 10116.ENSRNOP00000016077; -.
DR iPTMnet; Q9EP80; -.
DR PhosphoSitePlus; Q9EP80; -.
DR SwissPalm; Q9EP80; -.
DR jPOST; Q9EP80; -.
DR PaxDb; Q9EP80; -.
DR ABCD; Q9EP80; 1 sequenced antibody.
DR GeneID; 84591; -.
DR KEGG; rno:84591; -.
DR UCSC; RGD:69437; rat.
DR CTD; 9463; -.
DR RGD; 69437; Pick1.
DR eggNOG; KOG3651; Eukaryota.
DR InParanoid; Q9EP80; -.
DR OrthoDB; 545640at2759; -.
DR PhylomeDB; Q9EP80; -.
DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
DR EvolutionaryTrace; Q9EP80; -.
DR PRO; PR:Q9EP80; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098842; C:postsynaptic early endosome; IDA:SynGO.
DR GO; GO:0098843; C:postsynaptic endocytic zone; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0032588; C:trans-Golgi network membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0046875; F:ephrin receptor binding; TAS:UniProtKB.
DR GO; GO:0035256; F:G protein-coupled glutamate receptor binding; TAS:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0051020; F:GTPase binding; TAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:UniProtKB.
DR GO; GO:0140090; F:membrane curvature sensor activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IMP:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IDA:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; TAS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:UniProtKB.
DR GO; GO:0036294; P:cellular response to decreased oxygen levels; IMP:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:UniProtKB.
DR GO; GO:0097062; P:dendritic spine maintenance; IMP:UniProtKB.
DR GO; GO:0097061; P:dendritic spine organization; IDA:UniProtKB.
DR GO; GO:0015872; P:dopamine transport; NAS:UniProtKB.
DR GO; GO:0021782; P:glial cell development; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060292; P:long-term synaptic depression; IDA:UniProtKB.
DR GO; GO:0015844; P:monoamine transport; ISS:UniProtKB.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IDA:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006605; P:protein targeting; ISO:RGD.
DR GO; GO:0043113; P:receptor clustering; IMP:UniProtKB.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0050796; P:regulation of insulin secretion; ISO:RGD.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR CDD; cd07659; BAR_PICK1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.42.10; -; 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; PTHR12141; 1.
DR Pfam; PF06456; Arfaptin; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM01015; Arfaptin; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50870; AH; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Calcium; Cytoplasm; Cytoskeleton; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Phosphoprotein; Reference proteome;
KW Synapse; Synaptosome; Zinc.
FT CHAIN 1..416
FT /note="PRKCA-binding protein"
FT /id="PRO_0000058429"
FT DOMAIN 22..105
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 144..357
FT /note="AH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00294"
FT REGION 373..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRD5"
FT LIPID 414
FT /note="S-palmitoyl cysteine; by DHHC8"
FT /evidence="ECO:0000250"
FT MUTAGEN 27..28
FT /note="KD->AA: Abolishes interaction with other proteins,
FT but not with itself."
FT /evidence="ECO:0000269|PubMed:10027300,
FT ECO:0000269|PubMed:11122333, ECO:0000269|PubMed:11375398,
FT ECO:0000269|PubMed:23889934"
FT MUTAGEN 44
FT /note="C->G: Decreased lipid membrane binding, but no
FT effect on peptide ligand recognition."
FT /evidence="ECO:0000269|PubMed:17914463"
FT MUTAGEN 46
FT /note="C->G: Decreased lipid membrane binding, but no
FT effect on peptide ligand recognition."
FT /evidence="ECO:0000269|PubMed:17914463"
FT MUTAGEN 79
FT /note="K->E: No effect on lipid membrane binding."
FT /evidence="ECO:0000269|PubMed:17914463"
FT MUTAGEN 81
FT /note="K->E: No effect on lipid membrane binding."
FT /evidence="ECO:0000269|PubMed:17914463"
FT MUTAGEN 251..252
FT /note="KK->EE: Abolishes F-actin binding and the inhibitory
FT function on Arp2/3 complex-mediated actin nucleation,
FT impairs lipid vesicle interaction, no effect on Arp2/3
FT complex association."
FT /evidence="ECO:0000269|PubMed:18297063"
FT MUTAGEN 413
FT /note="W->A: Abolishes association with Arp2/3 complex and
FT the inhibitory function on Arp2/3 complex-mediated actin
FT nucleation."
FT /evidence="ECO:0000269|PubMed:18297063"
FT CONFLICT 401..402
FT /note="RG -> TW (in Ref. 3; AAK54603)"
FT /evidence="ECO:0000305"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:3HPK"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3HPK"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2PKU"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:3HPK"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:3HPK"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3HPK"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2LUI"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:3HPK"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:3HPK"
SQ SEQUENCE 416 AA; 46606 MW; 8FDE0D78BB26C006 CRC64;
MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV QVFDNTPAAL
DGTVAAGDEI TGVNGRSIKG KTKVEVAKMI QEVKGEVTIH YNKLQADPKQ GMSLDIVLKK
VKHRLVENMS SGTADALGLS RAILCNDGLV KRLEELERTA ELYKGMTEHT KNLLRAFYEL
SQTHRAFGDV FSVIGVREPQ PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN
KAIPDTRLTI KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL GEPLYRVSTG NYEYRLILRC
RQEARARFSQ MRKDVLEKME LLDQKHVQDI VFQLQRFVST MSKYYNDCYA VLRDADVFPI
EVDLAHTTLA YGPNQGGFTD GEDEEEEEED GAAREVSKDA RGATGPTDKG GSWCDS
