| AT4G20260 | plasma-membrane associated cation-binding protein 1 (PCAP1); FUNCTIONS IN: calmodulin binding, copper ion binding, phosphatidylinositol-3,4,5-trisphosphate binding, phosphatidylinositol-3,5-bisphosphate binding, calcium ion binding; INVOLVED IN: response to cold, N-terminal peptidyl-glycine N-myristoylation, defense response to bacterium; LOCATED IN: plasma membrane, vacuole; EXPRESSED IN: 35 plant structures; EXPRESSED DURING: 16 growth stages; CONTAINS InterPro DOMAIN/s: DREPP plasma membrane polypeptide (InterPro:IPR008469); Has 35333 Blast hits to 34131 proteins in 2444 species: Archae - 798; Bacteria - 22429; Metazoa - 974; Fungi - 991; Plants - 531; Viruses - 0; Other Eukaryotes - 9610 (source: NCBI BLink). Encodes a Ca2+ and Cu2+ binding protein. N-terminal myristylation on glycine 2 appears to enable it to associate tightly with the plasma membrane. Recombinant PCaP1 interacts strongly with phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PtdIns (3,4,5)P3, and weakly with PtdIns(3,5)P2 and PtdIns(4,5). It also interacts with calmodulin (CaM) in a calcium-dependent manner. CaM does not interfere with PCaP1 membrane localization but does weaken interactions between it and the PtdInsPs. PCaP1 has an apparent Kd of 10 uM for Cu2+ and can bind six ions per protein. Transcript levels for PCaP1 first fall and then rise following exposure to CuCl2. Mannitol, sorbitol, and the flg22 oligopeptide also increase expression levels. plasma-membrane associated cation-binding protein 1 | 4 | + | View |
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