Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00348
Entry Name
UniProt Accession
Theoretical PI
4.99
Molecular Weight
24583.84
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Plasma membrane-associated cation-binding protein 1
Protein Synonyms/Alias
AtPCAP1; Microtubule-destabilizing protein 25;
Gene Name
PCAP1
Gene Synonyms/Alias
MDP25; At4g20260; F1C12.180;
Created Date
31-OCT-2012
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGYWNSKVV
[1]
N-Myristoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Nagasaki N, Tomioka R, Maeshima M. A hydrophilic cation-binding protein ofArabidopsis thaliana, AtPCaP1, is localized to plasma membrane viaN-myristoylation and interacts with calmodulin and the phosphatidylinositolphosphates PtdIns(3,4,5)P(3) and PtdIns(3,5)P(2). FEBS J. 2008May;275(9):2267-82. doi: 10.1111/j.1742-4658.2008.06379.x. Epub 2008 Apr 3.[PMID:18397324]
Functional Description
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.
Sequence Annotation
Modified residue: 177 177 Phosphothreonine.
Protein Length
225 AA.
Protein Sequence
(Canonical)
MGYWNSKVVP KFKKLFEKNS AKKAAAAEAT KTFDESKETI NKEIEEKKTE LQPKVVETYE  60
ATSAEVKALV RDPKVAGLKK NSAAVQKYLE ELVKIEFPGS KAVSEASSSF GAGYVAGPVT  120
FIFEKVSVFL PEEVKTKEIP VEEVKAEEPA KTEEPAKTEG TSGEKEEIVE ETKKGETPET  180
AVVEEKKPEV EEKKEEATPA PAVVETPVKE PETTTTAPVA EPPKP                  225
FASTA
(Canonical)
>LipidDB-3702-00348|Q96262
MGYWNSKVVPKFKKLFEKNSAKKAAAAEATKTFDESKETINKEIEEKKTELQPKVVETYE
ATSAEVKALVRDPKVAGLKKNSAAVQKYLEELVKIEFPGSKAVSEASSSFGAGYVAGPVT
FIFEKVSVFLPEEVKTKEIPVEEVKAEEPAKTEEPAKTEGTSGEKEEIVEETKKGETPET
AVVEEKKPEVEEKKEEATPAPAVVETPVKEPETTTTAPVAEPPKP
Gene Ontology
GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB
GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0009506; C:plasmodesma; IDA:UniProtKB
GO:0005509; F:calcium ion binding; IDA:UniProtKB
GO:0005516; F:calmodulin binding; IDA:UniProtKB
GO:0005507; F:copper ion binding; IDA:UniProtKB
GO:0008017; F:microtubule binding; IDA:UniProtKB
GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB
GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB
GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB
GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB
GO:0071280; P:cellular response to copper ion; IEP:UniProtKB
GO:0071281; P:cellular response to iron ion; IEP:UniProtKB
GO:0071286; P:cellular response to magnesium ion; IEP:UniProtKB
GO:0010350; P:cellular response to magnesium starvation; IEP:UniProtKB
GO:0071325; P:cellular response to mannitol stimulus; IEP:UniProtKB
GO:0071219; P:cellular response to molecule of bacterial origin; IEP:UniProtKB
GO:0035865; P:cellular response to potassium ion; IEP:UniProtKB
GO:0071472; P:cellular response to salt stress; IEP:UniProtKB
GO:0072709; P:cellular response to sorbitol; IEP:UniProtKB
GO:0043622; P:cortical microtubule organization; IDA:UniProtKB
GO:0006499; P:N-terminal protein myristoylation; IMP:UniProtKB
GO:0051511; P:negative regulation of unidimensional cell growth; IMP:UniProtKB
GO:0031117; P:positive regulation of microtubule depolymerization; IDA:UniProtKB
GO:0009414; P:response to water deprivation; IEP:UniProtKB
GO:0016032; P:viral process; IEA:UniProtKB-KW
Interpro
InterPro; IPR008469; DREPP
Pfam
Pfam; PF05558; DREPP;
SMART
PROSITE
PRINTS