PCAP1_ARATH
ID PCAP1_ARATH Reviewed; 225 AA.
AC Q96262; F4JUT4; Q56YV4; Q8H7H8; Q8LDH5;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Plasma membrane-associated cation-binding protein 1;
DE Short=AtPCAP1;
DE AltName: Full=Microtubule-destabilizing protein 25;
GN Name=PCAP1; Synonyms=MDP25; OrderedLocusNames=At4g20260;
GN ORFNames=F1C12.180;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Dupree P., Prime T.A., Packman L.C.;
RT "Sequence of novel endomembrane-associated protein of Arabidopsis
RT thaliana.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-167 (ISOFORM 1).
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-225 (ISOFORMS 1/2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12949074; DOI=10.1074/jbc.m307443200;
RA Nuehse T.S., Boller T., Peck S.C.;
RT "A plasma membrane syntaxin is phosphorylated in response to the bacterial
RT elicitor flagellin.";
RL J. Biol. Chem. 278:45248-45254(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [11]
RP FUNCTION AS CALCIUM-BINDING PROTEIN, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION BY SALTS; SUGARS AND FLAGELLIN.
RC STRAIN=cv. Columbia;
RX PubMed=17264065; DOI=10.1093/jxb/erl284;
RA Ide Y., Nagasaki N., Tomioka R., Suito M., Kamiya T., Maeshima M.;
RT "Molecular properties of a novel, hydrophilic cation-binding protein
RT associated with the plasma membrane.";
RL J. Exp. Bot. 58:1173-1183(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
RN [13]
RP FUNCTION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=18397324; DOI=10.1111/j.1742-4658.2008.06379.x;
RA Nagasaki N., Tomioka R., Maeshima M.;
RT "A hydrophilic cation-binding protein of Arabidopsis thaliana, AtPCaP1, is
RT localized to plasma membrane via N-myristoylation and interacts with
RT calmodulin and the phosphatidylinositol phosphates PtdIns(3,4,5)P(3) and
RT PtdIns(3,5)P(2).";
RL FEBS J. 275:2267-2282(2008).
RN [14]
RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18664522; DOI=10.1093/jb/mvn092;
RA Nagasaki-Takeuchi N., Miyano M., Maeshima M.;
RT "A plasma membrane-associated protein of Arabidopsis thaliana AtPCaP1 binds
RT copper ions and changes its higher order structure.";
RL J. Biochem. 144:487-497(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [16]
RP FUNCTION, AND REVIEW.
RX PubMed=20448467; DOI=10.4161/psb.5.7.11825;
RA Kato M., Nagasaki-Takeuchi N., Ide Y., Tomioka R., Maeshima M.;
RT "PCaPs, possible regulators of PtdInsP signals on plasma membrane.";
RL Plant Signal. Behav. 5:848-850(2010).
RN [17]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22209764; DOI=10.1105/tpc.111.092684;
RA Li J., Wang X., Qin T., Zhang Y., Liu X., Sun J., Zhou Y., Zhu L.,
RA Zhang Z., Yuan M., Mao T.;
RT "MDP25, a novel calcium regulatory protein, mediates hypocotyl cell
RT elongation by destabilizing cortical microtubules in Arabidopsis.";
RL Plant Cell 23:4411-4427(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32; SER-107 AND THR-152, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [19]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH VIRAL P3N-PIPO,
RP MUTAGENESIS OF GLY-2, AND SUBCELLULAR LOCATION.
RX PubMed=22511869; DOI=10.1371/journal.ppat.1002639;
RA Vijayapalani P., Maeshima M., Nagasaki-Takekuchi N., Miller W.A.;
RT "Interaction of the trans-frame potyvirus protein P3N-PIPO with host
RT protein PCaP1 facilitates potyvirus movement.";
RL PLoS Pathog. 8:E1002639-E1002639(2012).
CC -!- FUNCTION: May be involved in intracellular signaling through
CC interaction with PtdInsPs and calmodulin (CaM); may keep PtdInsPs
CC attached to the plasma membrane until Ca(2+)-CaM reaches a competitive
CC concentration subsequent to an increase triggered by a stimulus, thus
CC leading to PtdInsPs release and subsequent activation of InsPs-
CC dependent signaling cascade. Interacts competitively at the N-terminus
CC with calcium ions and CaM (in a calcium-dependent manner), and with the
CC phosphatidylinositol phosphates PtdIns(3,4,5)P(3), PtdIns(3,4)P(2),
CC PtdIns(4,5)P(2) and PtdIns(3,5)P(2). Binds also weakly to PtdIns(3)P,
CC PtdIns(4)P and PtdIns(5)P. Negative regulator of hypocotyl cell
CC elongation by destabilizing cortical microtubules in a calcium-
CC dependent manner. Binds directly to and destabilized microtubules to
CC enhance microtubule depolymerization when cytoplasmic calcium
CC increases. In case of Turnip mosaic virus (TuMV) infection, confers
CC sensitivity by promoting viral cell-to-cell movement through
CC interaction with viral P3N-PIPO. {ECO:0000269|PubMed:17264065,
CC ECO:0000269|PubMed:18397324, ECO:0000269|PubMed:20448467,
CC ECO:0000269|PubMed:22209764, ECO:0000269|PubMed:22511869}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:18664522};
CC Note=Binds 6 Cu(2+) ions per subunit. Decreased of the heat stability
CC in the presence of metal ions (e.g. K(+), Ca(2+), Cu(2+), Sr(2+) and
CC Mg(2+)). {ECO:0000269|PubMed:18664522};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=345 nm {ECO:0000269|PubMed:18664522};
CC Note=Results were obtained when excited at 277 nm. In the presence of
CC copper ions, the maximum absorption peak disappears.;
CC -!- SUBUNIT: Interacts with Turnip mosaic virus (TuMV) P3N-PIPO.
CC {ECO:0000269|PubMed:22511869}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130,
CC ECO:0000305|PubMed:17644812}; Lipid-anchor. Cytoplasm. Cytoplasm,
CC cytoskeleton. Cell junction, plasmodesma. Note=Shuttles from plasma
CC membrane to cytoplasm (e.g. colocalizes with cortical microtubules)
CC upon calcium levels increase. Co-localizes with Turnip mosaic virus
CC (TuMV) P3N-PIPO at the plasmodesmata.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q96262-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96262-2; Sequence=VSP_044347;
CC -!- TISSUE SPECIFICITY: Mostly expressed in the basal region of hypocotyls.
CC Expressed in seedlings, roots, shoots, stems, leaves (e.g. in epidermis
CC and vascular tissues), flowers (e.g. in pistils and anthers) and
CC siliques (at protein level). {ECO:0000269|PubMed:17264065,
CC ECO:0000269|PubMed:18397324, ECO:0000269|PubMed:22209764}.
CC -!- INDUCTION: Accumulates in response to CuCl(2), mannitol, sorbitol, and
CC flagellin oligopeptide (e.g. flg22) treatments. Induced after long
CC treatment (2 days) with NaCl, KCl, MgCl(2) and FeCl(3). Slight
CC induction in Mg(2+) deprivation. Slightly repressed by dehydration.
CC {ECO:0000269|PubMed:17264065}.
CC -!- DISRUPTION PHENOTYPE: Long etiolated hypocotyls. Reduced accumulation
CC and cell-to-cell movement of Turnip mosaic virus (TuMV) leading to an
CC enhanced plant resistance. {ECO:0000269|PubMed:22209764,
CC ECO:0000269|PubMed:22511869}.
CC -!- SIMILARITY: Belongs to the DREPP family. {ECO:0000305}.
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DR EMBL; Y08061; CAA69300.1; -; mRNA.
DR EMBL; AL022224; CAA18251.1; -; Genomic_DNA.
DR EMBL; AL161552; CAB79026.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84291.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84292.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84293.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84294.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67675.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67676.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67677.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67678.1; -; Genomic_DNA.
DR EMBL; AY093084; AAM13083.1; -; mRNA.
DR EMBL; AY128768; AAM91168.1; -; mRNA.
DR EMBL; AK317524; BAH20189.1; -; mRNA.
DR EMBL; AY086004; AAM63213.1; -; mRNA.
DR EMBL; AF083669; AAN60228.1; -; mRNA.
DR EMBL; AK221216; BAD93780.1; -; mRNA.
DR PIR; T05334; T05334.
DR RefSeq; NP_001031676.1; NM_001036599.2. [Q96262-1]
DR RefSeq; NP_001031677.1; NM_001036600.2. [Q96262-2]
DR RefSeq; NP_001320005.1; NM_001341407.1. [Q96262-1]
DR RefSeq; NP_001329492.1; NM_001341410.1. [Q96262-1]
DR RefSeq; NP_001329493.1; NM_001341409.1. [Q96262-1]
DR RefSeq; NP_001329494.1; NM_001341408.1. [Q96262-1]
DR RefSeq; NP_193759.1; NM_118145.4. [Q96262-1]
DR RefSeq; NP_849412.1; NM_179081.5. [Q96262-1]
DR AlphaFoldDB; Q96262; -.
DR SMR; Q96262; -.
DR BioGRID; 13065; 7.
DR STRING; 3702.AT4G20260.4; -.
DR iPTMnet; Q96262; -.
DR SwissPalm; Q96262; -.
DR PaxDb; Q96262; -.
DR PRIDE; Q96262; -.
DR ProMEX; Q96262; -.
DR ProteomicsDB; 236709; -. [Q96262-1]
DR EnsemblPlants; AT4G20260.1; AT4G20260.1; AT4G20260. [Q96262-1]
DR EnsemblPlants; AT4G20260.10; AT4G20260.10; AT4G20260. [Q96262-1]
DR EnsemblPlants; AT4G20260.2; AT4G20260.2; AT4G20260. [Q96262-1]
DR EnsemblPlants; AT4G20260.3; AT4G20260.3; AT4G20260. [Q96262-1]
DR EnsemblPlants; AT4G20260.4; AT4G20260.4; AT4G20260. [Q96262-2]
DR EnsemblPlants; AT4G20260.7; AT4G20260.7; AT4G20260. [Q96262-1]
DR EnsemblPlants; AT4G20260.8; AT4G20260.8; AT4G20260. [Q96262-1]
DR EnsemblPlants; AT4G20260.9; AT4G20260.9; AT4G20260. [Q96262-1]
DR GeneID; 827773; -.
DR Gramene; AT4G20260.1; AT4G20260.1; AT4G20260. [Q96262-1]
DR Gramene; AT4G20260.10; AT4G20260.10; AT4G20260. [Q96262-1]
DR Gramene; AT4G20260.2; AT4G20260.2; AT4G20260. [Q96262-1]
DR Gramene; AT4G20260.3; AT4G20260.3; AT4G20260. [Q96262-1]
DR Gramene; AT4G20260.4; AT4G20260.4; AT4G20260. [Q96262-2]
DR Gramene; AT4G20260.7; AT4G20260.7; AT4G20260. [Q96262-1]
DR Gramene; AT4G20260.8; AT4G20260.8; AT4G20260. [Q96262-1]
DR Gramene; AT4G20260.9; AT4G20260.9; AT4G20260. [Q96262-1]
DR KEGG; ath:AT4G20260; -.
DR Araport; AT4G20260; -.
DR TAIR; locus:2120402; AT4G20260.
DR eggNOG; ENOG502RZAR; Eukaryota.
DR InParanoid; Q96262; -.
DR OMA; PIIFVFE; -.
DR OrthoDB; 1501255at2759; -.
DR PhylomeDB; Q96262; -.
DR PRO; PR:Q96262; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q96262; baseline and differential.
DR Genevisible; Q96262; AT.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; IEP:UniProtKB.
DR GO; GO:0071281; P:cellular response to iron ion; IEP:UniProtKB.
DR GO; GO:0071286; P:cellular response to magnesium ion; IEP:UniProtKB.
DR GO; GO:0010350; P:cellular response to magnesium starvation; IEP:UniProtKB.
DR GO; GO:0071325; P:cellular response to mannitol stimulus; IEP:UniProtKB.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IEP:UniProtKB.
DR GO; GO:0035865; P:cellular response to potassium ion; IEP:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; IEP:UniProtKB.
DR GO; GO:0072709; P:cellular response to sorbitol; IEP:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; IDA:UniProtKB.
DR GO; GO:0075733; P:intracellular transport of virus; IMP:TAIR.
DR GO; GO:0006499; P:N-terminal protein myristoylation; IMP:UniProtKB.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:TAIR.
DR GO; GO:0051511; P:negative regulation of unidimensional cell growth; IMP:UniProtKB.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IDA:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0090332; P:stomatal closure; IMP:TAIR.
DR InterPro; IPR008469; DREPP.
DR PANTHER; PTHR38522; PTHR38522; 1.
DR Pfam; PF05558; DREPP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calmodulin-binding; Cell junction;
KW Cell membrane; Copper; Cytoplasm; Cytoskeleton; Host-virus interaction;
KW Lipid-binding; Lipoprotein; Membrane; Microtubule; Myristate;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..225
FT /note="Plasma membrane-associated cation-binding protein 1"
FT /id="PRO_0000419768"
FT REGION 140..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:18397324"
FT VAR_SEQ 67
FT /note="K -> KQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044347"
FT MUTAGEN 2
FT /note="G->A: No N-myristoylation leading to cytoplasmic
FT location, but normal interaction with Turnip mosaic virus
FT (TuMV) P3N-PIPO."
FT /evidence="ECO:0000269|PubMed:18397324,
FT ECO:0000269|PubMed:22511869"
FT CONFLICT 175
FT /note="G -> D (in Ref. 6; AAM63213)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="Missing (in Ref. 6; AAM63213)"
FT /evidence="ECO:0000305"
SQ 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
