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Plasma membrane-associated cation-binding protein 2 (AtPCAP2) (Lysine rich protein At168) (Microtubule-associated protein 18)

 PCAP2_ARATH             Reviewed;         168 AA.
Q9LU05; C0Z2P4;
04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
30-AUG-2017, entry version 100.
RecName: Full=Plasma membrane-associated cation-binding protein 2 {ECO:0000303|PubMed:20061304};
Short=AtPCAP2 {ECO:0000303|PubMed:20061304};
AltName: Full=Lysine rich protein At168 {ECO:0000303|Ref.1};
AltName: Full=Microtubule-associated protein 18 {ECO:0000303|PubMed:17337629};
Name=PCAP2 {ECO:0000303|PubMed:20061304};
Synonyms=MAP18 {ECO:0000303|PubMed:17337629};
OrderedLocusNames=At5g44610 {ECO:0000312|Araport:AT5G44610};
ORFNames=K15C23.5 {ECO:0000312|EMBL:BAC41928.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|EMBL:BAA98114.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Zhao Q., Ou G., Yu J.;
"Cloning of cDNAs encoding a lysine rich protein At168.";
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[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=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[7]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
DISRUPTION PHENOTYPE, AND REPEATS.
PubMed=17337629; DOI=10.1105/tpc.106.048579;
Wang X., Zhu L., Liu B., Wang C., Jin L., Zhao Q., Yuan M.;
"Arabidopsis MICROTUBULE-ASSOCIATED PROTEIN18 functions in directional
cell growth by destabilizing cortical microtubules.";
Plant Cell 19:877-889(2007).
[8]
INDUCTION BY ARSENATE.
PubMed=18684332; DOI=10.1186/1471-2229-8-87;
Abercrombie J.M., Halfhill M.D., Ranjan P., Rao M.R., Saxton A.M.,
Yuan J.S., Stewart C.N. Jr.;
"Transcriptional responses of Arabidopsis thaliana plants to As (V)
stress.";
BMC Plant Biol. 8:87-87(2008).
[9]
SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, INDUCTION BY BIOTIC AND ABIOTIC STRESSES, MYRISTOYLATION AT
GLY-2, AND MUTAGENESIS OF GLY-2.
PubMed=20061304; DOI=10.1093/pcp/pcq003;
Kato M., Nagasaki-Takeuchi N., Ide Y., Maeshima M.;
"An Arabidopsis hydrophilic Ca2(+) -binding protein with a PEVK-rich
domain, PCaP2, is associated with the plasma membrane and interacts
with calmodulin and phosphatidylinositol phosphates.";
Plant Cell Physiol. 51:366-379(2010).
[10]
INDUCTION BY SENESCENCE.
PubMed=20966154; DOI=10.1104/pp.110.163402;
Keech O., Pesquet E., Gutierrez L., Ahad A., Bellini C., Smith S.M.,
Gardestroem P.;
"Leaf senescence is accompanied by an early disruption of the
microtubule network in Arabidopsis.";
Plant Physiol. 154:1710-1720(2010).
[11]
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).
-!- 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 (Probable). Binds
to microtubules and inhibits tubulin polymerization. Regulates
directional cell growth and cortical microtubule organization by
destabilizing microtubules (e.g. in cotyledon pavement cells)
(PubMed:17337629). {ECO:0000250|UniProtKB:Q96262,
ECO:0000269|PubMed:17337629, ECO:0000305|PubMed:20448467}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000250|UniProtKB:Q96262};
-!- SUBUNIT: Binds microtubules (PubMed:17337629). Interacts with
calcium ion Ca(2+), calmodulin and some phosphatidylinositol
phosphates (PtdInsPs) such as phosphatidylinositol 3,5-
bisphosphate [PtdIns(3,5)P(2)], PtdIns(4,5)P(2) and
PtdIns(3,4,5)P(3) (PubMed:20061304). {ECO:0000269|PubMed:17337629,
ECO:0000269|PubMed:20061304}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20061304};
Lipid-anchor {ECO:0000269|PubMed:20061304}. Cytoplasm,
cytoskeleton {ECO:0000269|PubMed:17337629}. Note=Localized along
cortical microtubules as patches of dot-like structures.
{ECO:0000269|PubMed:17337629}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9LU05-1; Sequence=Displayed;
Name=2;
IsoId=Q9LU05-2; Sequence=VSP_057466;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Mostly expressed in the expanding cells,
specifically in roots (except in root tips) and flowers (at
protein level). Also detected in cotyledons, hypocotyls and
trichome stalks. {ECO:0000269|PubMed:17337629,
ECO:0000269|PubMed:20061304}.
-!- DEVELOPMENTAL STAGE: Expressed in developing root hairs and
elongating pollen tubes. {ECO:0000269|PubMed:20061304}.
-!- INDUCTION: By arsenate As (V) (PubMed:18684332). Accumulates in
response to abscisic acid (ABA), gibberellic acid (GA), cold, and
drought stresses. Induced by various salt treatments such as NaCl,
KCl, MgCl(2), MnCl(2) and ZnCl(2) (PubMed:20061304). Expressed
during leaf senescence (PubMed:20966154).
{ECO:0000269|PubMed:18684332, ECO:0000269|PubMed:20061304,
ECO:0000269|PubMed:20966154}.
-!- DISRUPTION PHENOTYPE: Altered cortical microtubule arrays.
Abnormal cotyledon pavement cells with fewer extension lobes and
shorter cell length. {ECO:0000269|PubMed:17337629}.
-!- SIMILARITY: Belongs to the DREPP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; JN624857; AEO93269.1; -; mRNA.
EMBL; AB024024; BAA98114.1; -; Genomic_DNA.
EMBL; CP002688; AED95138.1; -; Genomic_DNA.
EMBL; CP002688; ANM69874.1; -; Genomic_DNA.
EMBL; CP002688; ANM69875.1; -; Genomic_DNA.
EMBL; AK117253; BAC41928.1; -; mRNA.
EMBL; BT003705; AAO39933.1; -; mRNA.
EMBL; AK318858; BAH56973.1; -; mRNA.
RefSeq; NP_001331521.1; NM_001344569.1. [Q9LU05-1]
RefSeq; NP_001331522.1; NM_001344568.1. [Q9LU05-1]
RefSeq; NP_568636.1; NM_123828.4. [Q9LU05-1]
UniGene; At.43801; -.
ProteinModelPortal; Q9LU05; -.
STRING; 3702.AT5G44610.1; -.
iPTMnet; Q9LU05; -.
PaxDb; Q9LU05; -.
EnsemblPlants; AT5G44610.1; AT5G44610.1; AT5G44610. [Q9LU05-1]
EnsemblPlants; AT5G44610.2; AT5G44610.2; AT5G44610. [Q9LU05-1]
EnsemblPlants; AT5G44610.3; AT5G44610.3; AT5G44610. [Q9LU05-1]
GeneID; 834489; -.
Gramene; AT5G44610.1; AT5G44610.1; AT5G44610.
Gramene; AT5G44610.2; AT5G44610.2; AT5G44610.
Gramene; AT5G44610.3; AT5G44610.3; AT5G44610.
KEGG; ath:AT5G44610; -.
Araport; AT5G44610; -.
TAIR; locus:2152145; AT5G44610.
HOGENOM; HOG000153113; -.
OMA; FEKSPAK; -.
PRO; PR:Q9LU05; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9LU05; baseline and differential.
Genevisible; Q9LU05; AT.
GO; GO:0046658; C:anchored component of plasma membrane; IEA:InterPro.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0090406; C:pollen tube; IDA:TAIR.
GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:TAIR.
GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
GO; GO:0008017; F:microtubule binding; IDA:TAIR.
GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:TAIR.
GO; GO:0038023; F:signaling receptor activity; IDA:TAIR.
GO; GO:0000902; P:cell morphogenesis; IMP:TAIR.
GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
GO; GO:0010150; P:leaf senescence; IEP:TAIR.
GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:TAIR.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
GO; GO:0046685; P:response to arsenic-containing substance; IEP:UniProtKB.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
GO; GO:0010038; P:response to metal ion; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0048768; P:root hair cell tip growth; IMP:TAIR.
GO; GO:0007165; P:signal transduction; TAS:TAIR.
InterPro; IPR008469; DREPP.
PANTHER; PTHR38522; PTHR38522; 1.
Pfam; PF05558; DREPP; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calmodulin-binding; Cell membrane;
Cell shape; Coiled coil; Complete proteome; Copper; Cytoplasm;
Cytoskeleton; Lipid-binding; Lipoprotein; Membrane; Microtubule;
Myristate; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:20061304}.
CHAIN 2 168 Plasma membrane-associated cation-binding
protein 2.
/FTId=PRO_0000431913.
REPEAT 26 30 1.
REPEAT 69 73 2.
REPEAT 94 99 3.
REPEAT 103 107 4.
REPEAT 110 115 5.
REPEAT 118 122 6.
REPEAT 124 129 7.
REGION 26 129 7 X 5 AA approximate repeats of V-E-E-K-
K.
COILED 56 77 {ECO:0000255}.
COMPBIAS 24 130 Glu-rich. {ECO:0000255|PROSITE-
ProRule:PRU00007}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:20061304}.
VAR_SEQ 69 117 Missing (in isoform 2).
/FTId=VSP_057466.
MUTAGEN 2 2 G->A: Loss of plasma membrane
localization, but accumulates into the
cytoplasm. {ECO:0000269|PubMed:20061304}.
SEQUENCE 168 AA; 18549 MW; 84CD08788D7914D1 CRC64;
MGYWKSKVVP RMKKLFEKSP AKKEVVEEEK PREVEVVEEV VVKTEEPAKE GETKPEEIIA
TGEKEIEIVE EKKEEAKPVE VPVLAAAEEK KPAVEEEKKT APVEEKKPAV EEEKKPAVEE
KKPVEEEKKE VVAAVPVAET PSTKAPETPV VETPAKAPET PAAAPQKA


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