PCAP2_ARATH
ID PCAP2_ARATH Reviewed; 168 AA.
AC Q9LU05; C0Z2P4;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Plasma membrane-associated cation-binding protein 2 {ECO:0000303|PubMed:20061304};
DE Short=AtPCAP2 {ECO:0000303|PubMed:20061304};
DE AltName: Full=Lysine rich protein At168 {ECO:0000303|Ref.1};
DE AltName: Full=Microtubule-associated protein 18 {ECO:0000303|PubMed:17337629};
GN Name=PCAP2 {ECO:0000303|PubMed:20061304};
GN Synonyms=MAP18 {ECO:0000303|PubMed:17337629};
GN OrderedLocusNames=At5g44610 {ECO:0000312|Araport:AT5G44610};
GN ORFNames=K15C23.5 {ECO:0000312|EMBL:BAC41928.1};
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 {ECO:0000312|EMBL:BAA98114.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhao Q., Ou G., Yu J.;
RT "Cloning of cDNAs encoding a lysine rich protein At168.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND REPEATS.
RX PubMed=17337629; DOI=10.1105/tpc.106.048579;
RA Wang X., Zhu L., Liu B., Wang C., Jin L., Zhao Q., Yuan M.;
RT "Arabidopsis MICROTUBULE-ASSOCIATED PROTEIN18 functions in directional cell
RT growth by destabilizing cortical microtubules.";
RL Plant Cell 19:877-889(2007).
RN [8]
RP INDUCTION BY ARSENATE.
RX PubMed=18684332; DOI=10.1186/1471-2229-8-87;
RA Abercrombie J.M., Halfhill M.D., Ranjan P., Rao M.R., Saxton A.M.,
RA Yuan J.S., Stewart C.N. Jr.;
RT "Transcriptional responses of Arabidopsis thaliana plants to As (V)
RT stress.";
RL BMC Plant Biol. 8:87-87(2008).
RN [9]
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION BY BIOTIC AND ABIOTIC STRESSES, MYRISTOYLATION AT GLY-2, AND
RP MUTAGENESIS OF GLY-2.
RX PubMed=20061304; DOI=10.1093/pcp/pcq003;
RA Kato M., Nagasaki-Takeuchi N., Ide Y., Maeshima M.;
RT "An Arabidopsis hydrophilic Ca2(+) -binding protein with a PEVK-rich
RT domain, PCaP2, is associated with the plasma membrane and interacts with
RT calmodulin and phosphatidylinositol phosphates.";
RL Plant Cell Physiol. 51:366-379(2010).
RN [10]
RP INDUCTION BY SENESCENCE.
RX PubMed=20966154; DOI=10.1104/pp.110.163402;
RA Keech O., Pesquet E., Gutierrez L., Ahad A., Bellini C., Smith S.M.,
RA Gardestroem P.;
RT "Leaf senescence is accompanied by an early disruption of the microtubule
RT network in Arabidopsis.";
RL Plant Physiol. 154:1710-1720(2010).
RN [11]
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).
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 (Probable). Binds to microtubules and
CC inhibits tubulin polymerization. Regulates directional cell growth and
CC cortical microtubule organization by destabilizing microtubules (e.g.
CC in cotyledon pavement cells) (PubMed:17337629).
CC {ECO:0000250|UniProtKB:Q96262, ECO:0000269|PubMed:17337629,
CC ECO:0000305|PubMed:20448467}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q96262};
CC -!- SUBUNIT: Binds microtubules (PubMed:17337629). Interacts with calcium
CC ion Ca(2+), calmodulin and some phosphatidylinositol phosphates
CC (PtdInsPs) such as phosphatidylinositol 3,5-bisphosphate
CC [PtdIns(3,5)P(2)], PtdIns(4,5)P(2) and PtdIns(3,4,5)P(3)
CC (PubMed:20061304). {ECO:0000269|PubMed:17337629,
CC ECO:0000269|PubMed:20061304}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20061304};
CC Lipid-anchor {ECO:0000269|PubMed:20061304}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17337629}. Note=Localized along cortical
CC microtubules as patches of dot-like structures.
CC {ECO:0000269|PubMed:17337629}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LU05-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LU05-2; Sequence=VSP_057466;
CC -!- TISSUE SPECIFICITY: Mostly expressed in the expanding cells,
CC specifically in roots (except in root tips) and flowers (at protein
CC level). Also detected in cotyledons, hypocotyls and trichome stalks.
CC {ECO:0000269|PubMed:17337629, ECO:0000269|PubMed:20061304}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing root hairs and elongating
CC pollen tubes. {ECO:0000269|PubMed:20061304}.
CC -!- INDUCTION: By arsenate As (V) (PubMed:18684332). Accumulates in
CC response to abscisic acid (ABA), gibberellic acid (GA), cold, and
CC drought stresses. Induced by various salt treatments such as NaCl, KCl,
CC MgCl(2), MnCl(2) and ZnCl(2) (PubMed:20061304). Expressed during leaf
CC senescence (PubMed:20966154). {ECO:0000269|PubMed:18684332,
CC ECO:0000269|PubMed:20061304, ECO:0000269|PubMed:20966154}.
CC -!- DISRUPTION PHENOTYPE: Altered cortical microtubule arrays. Abnormal
CC cotyledon pavement cells with fewer extension lobes and shorter cell
CC length. {ECO:0000269|PubMed:17337629}.
CC -!- SIMILARITY: Belongs to the DREPP family. {ECO:0000305}.
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DR EMBL; JN624857; AEO93269.1; -; mRNA.
DR EMBL; AB024024; BAA98114.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95138.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69874.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69875.1; -; Genomic_DNA.
DR EMBL; AK117253; BAC41928.1; -; mRNA.
DR EMBL; BT003705; AAO39933.1; -; mRNA.
DR EMBL; AK318858; BAH56973.1; -; mRNA.
DR RefSeq; NP_001331521.1; NM_001344569.1. [Q9LU05-1]
DR RefSeq; NP_001331522.1; NM_001344568.1. [Q9LU05-1]
DR RefSeq; NP_568636.1; NM_123828.4. [Q9LU05-1]
DR AlphaFoldDB; Q9LU05; -.
DR SMR; Q9LU05; -.
DR STRING; 3702.AT5G44610.1; -.
DR iPTMnet; Q9LU05; -.
DR PaxDb; Q9LU05; -.
DR PRIDE; Q9LU05; -.
DR ProteomicsDB; 236710; -. [Q9LU05-1]
DR EnsemblPlants; AT5G44610.1; AT5G44610.1; AT5G44610. [Q9LU05-1]
DR EnsemblPlants; AT5G44610.2; AT5G44610.2; AT5G44610. [Q9LU05-1]
DR EnsemblPlants; AT5G44610.3; AT5G44610.3; AT5G44610. [Q9LU05-1]
DR GeneID; 834489; -.
DR Gramene; AT5G44610.1; AT5G44610.1; AT5G44610. [Q9LU05-1]
DR Gramene; AT5G44610.2; AT5G44610.2; AT5G44610. [Q9LU05-1]
DR Gramene; AT5G44610.3; AT5G44610.3; AT5G44610. [Q9LU05-1]
DR KEGG; ath:AT5G44610; -.
DR Araport; AT5G44610; -.
DR TAIR; locus:2152145; AT5G44610.
DR HOGENOM; CLU_1646033_0_0_1; -.
DR OMA; FSSWYIF; -.
DR PRO; PR:Q9LU05; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LU05; baseline and differential.
DR Genevisible; Q9LU05; AT.
DR GO; GO:0046658; C:anchored component of plasma membrane; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:TAIR.
DR GO; GO:0038023; F:signaling receptor activity; IDA:TAIR.
DR GO; GO:0000902; P:cell morphogenesis; IMP:TAIR.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IEP:TAIR.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:TAIR.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
DR GO; GO:0010038; P:response to metal ion; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0048768; P:root hair cell tip growth; IMP:TAIR.
DR GO; GO:0007165; P:signal transduction; TAS:TAIR.
DR InterPro; IPR008469; DREPP.
DR PANTHER; PTHR38522; PTHR38522; 3.
DR Pfam; PF05558; DREPP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calmodulin-binding; Cell membrane;
KW Cell shape; Coiled coil; Copper; Cytoplasm; Cytoskeleton; Lipid-binding;
KW Lipoprotein; Membrane; Microtubule; Myristate; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20061304"
FT CHAIN 2..168
FT /note="Plasma membrane-associated cation-binding protein 2"
FT /id="PRO_0000431913"
FT REPEAT 26..30
FT /note="1"
FT REPEAT 69..73
FT /note="2"
FT REPEAT 94..99
FT /note="3"
FT REPEAT 103..107
FT /note="4"
FT REPEAT 110..115
FT /note="5"
FT REPEAT 118..122
FT /note="6"
FT REPEAT 124..129
FT /note="7"
FT REGION 26..129
FT /note="7 X 5 AA approximate repeats of V-E-E-K-K"
FT REGION 88..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 56..77
FT /evidence="ECO:0000255"
FT COMPBIAS 89..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20061304"
FT VAR_SEQ 69..117
FT /note="Missing (in isoform 2)"
FT /id="VSP_057466"
FT MUTAGEN 2
FT /note="G->A: Loss of plasma membrane localization, but
FT accumulates into the cytoplasm."
FT /evidence="ECO:0000269|PubMed:20061304"
SQ SEQUENCE 168 AA; 18549 MW; 84CD08788D7914D1 CRC64;
MGYWKSKVVP RMKKLFEKSP AKKEVVEEEK PREVEVVEEV VVKTEEPAKE GETKPEEIIA
TGEKEIEIVE EKKEEAKPVE VPVLAAAEEK KPAVEEEKKT APVEEKKPAV EEEKKPAVEE
KKPVEEEKKE VVAAVPVAET PSTKAPETPV VETPAKAPET PAAAPQKA
