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Plasma membrane-associated cation-binding protein 1 (AtPCAP1) (Microtubule-destabilizing protein 25)

 PCAP1_ARATH             Reviewed;         225 AA.
Q96262; F4JUT4; Q56YV4; Q8H7H8; Q8LDH5;
31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
30-AUG-2017, entry version 108.
RecName: Full=Plasma membrane-associated cation-binding protein 1;
Short=AtPCAP1;
AltName: Full=Microtubule-destabilizing protein 25;
Name=PCAP1; Synonyms=MDP25; OrderedLocusNames=At4g20260;
ORFNames=F1C12.180;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Dupree P., Prime T.A., Packman L.C.;
"Sequence of novel endomembrane-associated protein of Arabidopsis
thaliana.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-167 (ISOFORM 1).
Stracke R., Palme K.;
"Signal peptide selection derived cDNAs from Arabidopsis thaliana
leaves and guard cells.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-225 (ISOFORMS 1/2).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
SUBCELLULAR LOCATION.
PubMed=12949074; DOI=10.1074/jbc.M307443200;
Nuehse T.S., Boller T., Peck S.C.;
"A plasma membrane syntaxin is phosphorylated in response to the
bacterial elicitor flagellin.";
J. Biol. Chem. 278:45248-45254(2003).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=15060130; DOI=10.1074/mcp.M400001-MCP200;
Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
Garin J., Barbier-Brygoo H., Ephritikhine G.;
"Identification of new intrinsic proteins in Arabidopsis plasma
membrane proteome.";
Mol. Cell. Proteomics 3:675-691(2004).
[11]
FUNCTION AS CALCIUM-BINDING PROTEIN, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION BY SALTS; SUGARS AND FLAGELLIN.
STRAIN=cv. Columbia;
PubMed=17264065; DOI=10.1093/jxb/erl284;
Ide Y., Nagasaki N., Tomioka R., Suito M., Kamiya T., Maeshima M.;
"Molecular properties of a novel, hydrophilic cation-binding protein
associated with the plasma membrane.";
J. Exp. Bot. 58:1173-1183(2007).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=17644812; DOI=10.1074/mcp.M700099-MCP200;
Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
Barbier-Brygoo H., Ephritikhine G.;
"A high content in lipid-modified peripheral proteins and integral
receptor kinases features in the arabidopsis plasma membrane
proteome.";
Mol. Cell. Proteomics 6:1980-1996(2007).
[13]
FUNCTION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=18397324; DOI=10.1111/j.1742-4658.2008.06379.x;
Nagasaki N., Tomioka R., Maeshima M.;
"A hydrophilic cation-binding protein of Arabidopsis thaliana,
AtPCaP1, is localized to plasma membrane via N-myristoylation and
interacts with calmodulin and the phosphatidylinositol phosphates
PtdIns(3,4,5)P(3) and PtdIns(3,5)P(2).";
FEBS J. 275:2267-2282(2008).
[14]
COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18664522; DOI=10.1093/jb/mvn092;
Nagasaki-Takeuchi N., Miyano M., Maeshima M.;
"A plasma membrane-associated protein of Arabidopsis thaliana AtPCaP1
binds copper ions and changes its higher order structure.";
J. Biochem. 144:487-497(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[16]
FUNCTION, AND REVIEW.
PubMed=20448467; DOI=10.4161/psb.5.7.11825;
Kato M., Nagasaki-Takeuchi N., Ide Y., Tomioka R., Maeshima M.;
"PCaPs, possible regulators of PtdInsP signals on plasma membrane.";
Plant Signal. Behav. 5:848-850(2010).
[17]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=22209764; DOI=10.1105/tpc.111.092684;
Li J., Wang X., Qin T., Zhang Y., Liu X., Sun J., Zhou Y., Zhu L.,
Zhang Z., Yuan M., Mao T.;
"MDP25, a novel calcium regulatory protein, mediates hypocotyl cell
elongation by destabilizing cortical microtubules in Arabidopsis.";
Plant Cell 23:4411-4427(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32; SER-107 AND THR-152,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
[19]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH VIRAL P3N-PIPO,
MUTAGENESIS OF GLY-2, AND SUBCELLULAR LOCATION.
PubMed=22511869; DOI=10.1371/journal.ppat.1002639;
Vijayapalani P., Maeshima M., Nagasaki-Takekuchi N., Miller W.A.;
"Interaction of the trans-frame potyvirus protein P3N-PIPO with host
protein PCaP1 facilitates potyvirus movement.";
PLoS Pathog. 8:E1002639-E1002639(2012).
-!- FUNCTION: May be involved in intracellular signaling through
interaction with PtdInsPs and calmodulin (CaM); may keep PtdInsPs
attached to the plasma membrane until Ca(2+)-CaM reaches a
competitive concentration subsequent to an increase triggered by a
stimulus, thus leading to PtdInsPs release and subsequent
activation of InsPs-dependent signaling cascade. Interacts
competitively at the N-terminus with calcium ions and CaM (in a
calcium-dependent manner), and with the phosphatidylinositol
phosphates PtdIns(3,4,5)P(3), PtdIns(3,4)P(2), PtdIns(4,5)P(2) and
PtdIns(3,5)P(2). Binds also weakly to PtdIns(3)P, PtdIns(4)P and
PtdIns(5)P. Negative regulator of hypocotyl cell elongation by
destabilizing cortical microtubules in a calcium-dependent manner.
Binds directly to and destabilized microtubules to enhance
microtubule depolymerization when cytoplasmic calcium increases.
In case of Turnip mosaic virus (TuMV) infection, confers
sensitivity by promoting viral cell-to-cell movement through
interaction with viral P3N-PIPO. {ECO:0000269|PubMed:17264065,
ECO:0000269|PubMed:18397324, ECO:0000269|PubMed:20448467,
ECO:0000269|PubMed:22209764, ECO:0000269|PubMed:22511869}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000269|PubMed:18664522};
Note=Binds 6 Cu(2+) ions per subunit. Decreased of the heat
stability in the presence of metal ions (e.g. K(+), Ca(2+),
Cu(2+), Sr(2+) and Mg(2+)). {ECO:0000269|PubMed:18664522};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=345 nm {ECO:0000269|PubMed:18664522};
Note=Results were obtained when excited at 277 nm. In the
presence of copper ions, the maximum absorption peak
disappears.;
-!- SUBUNIT: Interacts with Turnip mosaic virus (TuMV) P3N-PIPO.
{ECO:0000269|PubMed:22511869}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130};
Lipid-anchor. Cytoplasm. Cytoplasm, cytoskeleton. Cell junction,
plasmodesma. Note=Shuttles from plasma membrane to cytoplasm (e.g.
colocalizes with cortical microtubules) upon calcium levels
increase. Co-localizes with Turnip mosaic virus (TuMV) P3N-PIPO at
the plasmodesmata.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q96262-1; Sequence=Displayed;
Name=2;
IsoId=Q96262-2; Sequence=VSP_044347;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Mostly expressed in the basal region of
hypocotyls. Expressed in seedlings, roots, shoots, stems, leaves
(e.g. in epidermis and vascular tissues), flowers (e.g. in pistils
and anthers) and siliques (at protein level).
{ECO:0000269|PubMed:17264065, ECO:0000269|PubMed:18397324,
ECO:0000269|PubMed:22209764}.
-!- INDUCTION: Accumulates in response to CuCl(2), mannitol, sorbitol,
and flagellin oligopeptide (e.g. flg22) treatments. Induced after
long treatment (2 days) with NaCl, KCl, MgCl(2) and FeCl(3).
Slight induction in Mg(2+) deprivation. Slightly repressed by
dehydration. {ECO:0000269|PubMed:17264065}.
-!- DISRUPTION PHENOTYPE: Long etiolated hypocotyls. Reduced
accumulation and cell-to-cell movement of Turnip mosaic virus
(TuMV) leading to an enhanced plant resistance.
{ECO:0000269|PubMed:22209764, ECO:0000269|PubMed:22511869}.
-!- SIMILARITY: Belongs to the DREPP family. {ECO:0000305}.
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EMBL; Y08061; CAA69300.1; -; mRNA.
EMBL; AL022224; CAA18251.1; -; Genomic_DNA.
EMBL; AL161552; CAB79026.1; -; Genomic_DNA.
EMBL; CP002687; AEE84291.1; -; Genomic_DNA.
EMBL; CP002687; AEE84292.1; -; Genomic_DNA.
EMBL; CP002687; AEE84293.1; -; Genomic_DNA.
EMBL; CP002687; AEE84294.1; -; Genomic_DNA.
EMBL; CP002687; ANM67675.1; -; Genomic_DNA.
EMBL; CP002687; ANM67676.1; -; Genomic_DNA.
EMBL; CP002687; ANM67677.1; -; Genomic_DNA.
EMBL; CP002687; ANM67678.1; -; Genomic_DNA.
EMBL; AY093084; AAM13083.1; -; mRNA.
EMBL; AY128768; AAM91168.1; -; mRNA.
EMBL; AK317524; BAH20189.1; -; mRNA.
EMBL; AY086004; AAM63213.1; -; mRNA.
EMBL; AF083669; AAN60228.1; -; mRNA.
EMBL; AK221216; BAD93780.1; -; mRNA.
PIR; T05334; T05334.
RefSeq; NP_001031676.1; NM_001036599.2. [Q96262-1]
RefSeq; NP_001031677.1; NM_001036600.2. [Q96262-2]
RefSeq; NP_001320005.1; NM_001341407.1. [Q96262-1]
RefSeq; NP_001329492.1; NM_001341410.1. [Q96262-1]
RefSeq; NP_001329493.1; NM_001341409.1. [Q96262-1]
RefSeq; NP_001329494.1; NM_001341408.1. [Q96262-1]
RefSeq; NP_193759.1; NM_118145.4. [Q96262-1]
RefSeq; NP_849412.1; NM_179081.5. [Q96262-1]
UniGene; At.21638; -.
UniGene; At.24152; -.
ProteinModelPortal; Q96262; -.
BioGrid; 13065; 4.
STRING; 3702.AT4G20260.4; -.
iPTMnet; Q96262; -.
SwissPalm; Q96262; -.
PaxDb; Q96262; -.
PRIDE; Q96262; -.
ProMEX; Q96262; -.
EnsemblPlants; AT4G20260.1; AT4G20260.1; AT4G20260. [Q96262-1]
EnsemblPlants; AT4G20260.10; AT4G20260.10; AT4G20260. [Q96262-1]
EnsemblPlants; AT4G20260.2; AT4G20260.2; AT4G20260. [Q96262-1]
EnsemblPlants; AT4G20260.3; AT4G20260.3; AT4G20260. [Q96262-1]
EnsemblPlants; AT4G20260.4; AT4G20260.4; AT4G20260. [Q96262-2]
EnsemblPlants; AT4G20260.7; AT4G20260.7; AT4G20260. [Q96262-1]
EnsemblPlants; AT4G20260.8; AT4G20260.8; AT4G20260. [Q96262-1]
EnsemblPlants; AT4G20260.9; AT4G20260.9; AT4G20260. [Q96262-1]
GeneID; 827773; -.
Gramene; AT4G20260.1; AT4G20260.1; AT4G20260.
Gramene; AT4G20260.10; AT4G20260.10; AT4G20260.
Gramene; AT4G20260.2; AT4G20260.2; AT4G20260.
Gramene; AT4G20260.3; AT4G20260.3; AT4G20260.
Gramene; AT4G20260.4; AT4G20260.4; AT4G20260.
Gramene; AT4G20260.7; AT4G20260.7; AT4G20260.
Gramene; AT4G20260.8; AT4G20260.8; AT4G20260.
Gramene; AT4G20260.9; AT4G20260.9; AT4G20260.
KEGG; ath:AT4G20260; -.
Araport; AT4G20260; -.
TAIR; locus:2120402; AT4G20260.
eggNOG; ENOG410IYJB; Eukaryota.
eggNOG; ENOG410YIYH; LUCA.
HOGENOM; HOG000070951; -.
InParanoid; Q96262; -.
OMA; KVVPKFK; -.
PhylomeDB; Q96262; -.
PRO; PR:Q96262; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q96262; baseline and differential.
Genevisible; Q96262; AT.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0009506; C:plasmodesma; IDA:UniProtKB.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0071280; P:cellular response to copper ion; IEP:UniProtKB.
GO; GO:0071281; P:cellular response to iron ion; IEP:UniProtKB.
GO; GO:0071286; P:cellular response to magnesium ion; IEP:UniProtKB.
GO; GO:0010350; P:cellular response to magnesium starvation; IEP:UniProtKB.
GO; GO:0071325; P:cellular response to mannitol stimulus; IEP:UniProtKB.
GO; GO:0071219; P:cellular response to molecule of bacterial origin; IEP:UniProtKB.
GO; GO:0035865; P:cellular response to potassium ion; IEP:UniProtKB.
GO; GO:0071472; P:cellular response to salt stress; IEP:UniProtKB.
GO; GO:0072709; P:cellular response to sorbitol; IEP:UniProtKB.
GO; GO:0043622; P:cortical microtubule organization; IDA:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0075733; P:intracellular transport of virus; IMP:TAIR.
GO; GO:0006499; P:N-terminal protein myristoylation; IMP:UniProtKB.
GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:TAIR.
GO; GO:0051511; P:negative regulation of unidimensional cell growth; IMP:UniProtKB.
GO; GO:0031117; P:positive regulation of microtubule depolymerization; IDA:UniProtKB.
GO; GO:0051592; P:response to calcium ion; IDA:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
GO; GO:0090332; P:stomatal closure; IMP:TAIR.
InterPro; IPR008469; DREPP.
PANTHER; PTHR38522; PTHR38522; 1.
Pfam; PF05558; DREPP; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calmodulin-binding; Cell junction;
Cell membrane; Complete proteome; Copper; Cytoplasm; Cytoskeleton;
Host-virus interaction; Lipid-binding; Lipoprotein; Membrane;
Microtubule; Myristate; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 225 Plasma membrane-associated cation-binding
protein 1.
/FTId=PRO_0000419768.
COMPBIAS 132 212 Glu-rich.
MOD_RES 32 32 Phosphothreonine.
{ECO:0000244|PubMed:22092075}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
MOD_RES 152 152 Phosphothreonine.
{ECO:0000244|PubMed:22092075}.
MOD_RES 177 177 Phosphothreonine.
{ECO:0000244|PubMed:19376835}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:18397324}.
VAR_SEQ 67 67 K -> KQ (in isoform 2). {ECO:0000305}.
/FTId=VSP_044347.
MUTAGEN 2 2 G->A: No N-myristoylation leading to
cytoplasmic location, but normal
interaction with Turnip mosaic virus
(TuMV) P3N-PIPO.
{ECO:0000269|PubMed:18397324,
ECO:0000269|PubMed:22511869}.
CONFLICT 175 175 G -> D (in Ref. 6; AAM63213).
{ECO:0000305}.
CONFLICT 213 213 Missing (in Ref. 6; AAM63213).
{ECO:0000305}.
SEQUENCE 225 AA; 24584 MW; 4E11D1C1DEA493C9 CRC64;
MGYWNSKVVP KFKKLFEKNS AKKAAAAEAT KTFDESKETI NKEIEEKKTE LQPKVVETYE
ATSAEVKALV RDPKVAGLKK NSAAVQKYLE ELVKIEFPGS KAVSEASSSF GAGYVAGPVT
FIFEKVSVFL PEEVKTKEIP VEEVKAEEPA KTEEPAKTEG TSGEKEEIVE ETKKGETPET
AVVEEKKPEV EEKKEEATPA PAVVETPVKE PETTTTAPVA EPPKP


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