UniProt ID | CAS_ARATH | |
---|---|---|
UniProt AC | Q9FN48 | |
Protein Name | Calcium sensing receptor, chloroplastic | |
Gene Name | CAS | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 387 | |
Subcellular Localization |
Plastid, chloroplast thylakoid membrane Single-pass membrane protein Stromal side . |
|
Protein Description | Modulates cytoplasmic Ca(2+) concentration and is crucial for proper stomatal regulation in response to elevated levels of external Ca(2+). May function by regulating concentrations of inositol 1,4,5-trisphosphate (IP3), which in turn triggers release of Ca(2+) from internal stores. May play a role in de-etiolation.. | |
Protein Sequence | MAMAEMATKSSLSAKLTLPSSSTKKTLSLRQVSVSLPTSTSISLLSLFASPPHEAKAAVSIPKDQIVSSLTEVEKTINQVQETGSSVFDATQRVFQVVGDALKPALDTALPIAKQAGEEAMKLASPAFSEASKKAQEAMQSSGFDSEPVFNAAKTVTDVAQQTSKAIEDAKPIASSTMDTISSADPSVIVVAAGAAFLAYLLLPPVFSAISFNFRGYKGDLTPAQTLDLLCTKNYLMVDIRSEKDKEKAGIPRLPSNAKNRVISIPLEELPNKVKGIVRNSKRVEAEIAALKISYLKKINKGSNIIILDSYTDSAKIVAKTLKVLGYKNCYIVTDGFSGGRGWLQSRLGTDSYNFSFAQVLSPSRIIPAASRSFGTRSGTKFLPSSD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
76 | Phosphorylation | SLTEVEKTINQVQET HHHHHHHHHHHHHHH | 16.20 | 29797451 | |
264 | Phosphorylation | NAKNRVISIPLEELP CCCCCEEEEEHHHCC | 18.46 | 19880383 | |
350 | Phosphorylation | WLQSRLGTDSYNFSF HHHHHHCCCCCCEEH | 26.77 | 19376835 | |
352 | Phosphorylation | QSRLGTDSYNFSFAQ HHHHCCCCCCEEHHH | 23.09 | 19376835 | |
353 | Phosphorylation | SRLGTDSYNFSFAQV HHHCCCCCCEEHHHH | 24.04 | 19376835 | |
356 | Phosphorylation | GTDSYNFSFAQVLSP CCCCCCEEHHHHCCH | 18.94 | 30291188 | |
362 | Phosphorylation | FSFAQVLSPSRIIPA EEHHHHCCHHHEEEH | 23.21 | 19376835 | |
364 | Phosphorylation | FAQVLSPSRIIPAAS HHHHCCHHHEEEHHH | 32.51 | 19376835 | |
371 | Phosphorylation | SRIIPAASRSFGTRS HHEEEHHHHCCCCCC | 30.48 | 19376835 | |
373 | Phosphorylation | IIPAASRSFGTRSGT EEEHHHHCCCCCCCC | 26.07 | 19376835 | |
376 | Phosphorylation | AASRSFGTRSGTKFL HHHHCCCCCCCCCCC | 21.46 | 19376835 | |
378 | Phosphorylation | SRSFGTRSGTKFLPS HHCCCCCCCCCCCCC | 51.13 | 23111157 | |
380 | Phosphorylation | SFGTRSGTKFLPSSD CCCCCCCCCCCCCCC | 21.62 | 30291188 | |
385 | Phosphorylation | SGTKFLPSSD----- CCCCCCCCCC----- | 49.65 | 27545962 | |
386 | Phosphorylation | GTKFLPSSD------ CCCCCCCCC------ | 45.45 | 19376835 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CAS_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CAS_ARATH !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CAS_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of CAS_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-378 ANDTHR-380, AND IDENTIFICATION BY MASS SPECTROMETRY. | |
"Light regulation of CaS, a novel phosphoprotein in the thylakoidmembrane of Arabidopsis thaliana."; Vainonen J.P., Sakuragi Y., Stael S., Tikkanen M., Allahverdiyeva Y.,Paakkarinen V., Aro E., Suorsa M., Scheller H.V., Vener A.V.,Aro E.M.; FEBS J. 275:1767-1777(2008). Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-380, AND DISRUPTIONPHENOTYPE. |