Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0014809 | biological_process | regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion |
| A | 0016529 | cellular_component | sarcoplasmic reticulum |
| A | 0030018 | cellular_component | Z disc |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| A | 0033018 | cellular_component | sarcoplasmic reticulum lumen |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0045214 | biological_process | sarcomere organization |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051258 | biological_process | protein polymerization |
| A | 0051279 | biological_process | regulation of release of sequestered calcium ion into cytosol |
| A | 0051281 | biological_process | positive regulation of release of sequestered calcium ion into cytosol |
| A | 1901341 | biological_process | positive regulation of store-operated calcium channel activity |
| A | 2001256 | biological_process | regulation of store-operated calcium entry |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 368 |
| Chain | Residue |
| A | PHE6 |
| A | PRO7 |
| A | TRP242 |
| A | TYR298 |
| A | TRP299 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD A 369 |
| Chain | Residue |
| A | HOH493 |
| A | GLN63 |
| A | LEU294 |
| A | LEU295 |
| A | HOH462 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 370 |
| Chain | Residue |
| A | ASN279 |
| A | GLU344 |
| A | HOH413 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 371 |
| Chain | Residue |
| A | VAL314 |
| A | ASN316 |
| A | ASP321 |
| A | VAL346 |
| A | GLY349 |
| A | GLU350 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 372 |
| Chain | Residue |
| A | ASN17 |
| A | VAL18 |
| A | LEU74 |
| A | ASP80 |
| A | HOH490 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 373 |
| Chain | Residue |
| A | GLU199 |
| A | THR229 |
| A | THR277 |
| A | HOH756 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 374 |
| Chain | Residue |
| A | ASP210 |
| A | PRO212 |
| A | GLU217 |
| A | HOH391 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 375 |
| Chain | Residue |
| A | THR189 |
| A | HOH474 |
| A | HOH565 |
| A | HOH684 |
| A | HOH801 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 376 |
| Chain | Residue |
| A | PRO172 |
| A | HOH629 |
| A | HOH771 |
Functional Information from PROSITE/UniProt
| site_id | PS00863 |
| Number of Residues | 15 |
| Details | CALSEQUESTRIN_1 Calsequestrin signature 1. EEGLDFPeYDGvDRV |
| Chain | Residue | Details |
| A | GLU1-VAL15 | |
| site_id | PS00864 |
| Number of Residues | 20 |
| Details | CALSEQUESTRIN_2 Calsequestrin signature 2. ELEDWLEDVLeGeINTEDDD |
| Chain | Residue | Details |
| A | GLU338-ASP357 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22170046","evidenceCode":"ECO:0000269"}]} |
