P12637
Gene name |
CASQ2 |
Protein name |
Calsequestrin-2 |
Names |
Calsequestrin, cardiac muscle isoform |
Species |
Canis lupus familiaris (Dog) (Canis familiaris) |
KEGG Pathway |
cfa:483134 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
2 structures for P12637
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1SJI | X-ray | 240 A | A/B | 22-371 | PDB |
| AF-P12637-F1 | Predicted | AlphaFoldDB |
No variants for P12637
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P12637 | |||||
No associated diseases with P12637
5 regional properties for P12637
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Calsequestrin, conserved site | 20 - 34 | IPR018233-1 |
| conserved_site | Calsequestrin, conserved site | 357 - 376 | IPR018233-2 |
| domain | Calsequestrin, middle TRX-fold domain | 145 - 246 | IPR041858 |
| domain | Calsequestrin, N-terminal TRX-fold domain | 24 - 143 | IPR041859 |
| domain | Calsequestrin, C-terminal TRX-fold domain | 247 - 366 | IPR041860 |
Functions
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| sarcoplasmic reticulum | A fine reticular network of membrane-limited elements that pervades the sarcoplasm of a muscle cell; continuous over large portions of the cell and with the nuclear envelope; that part of the endoplasmic reticulum specialized for calcium release, uptake and storage. |
| sarcoplasmic reticulum lumen | The volume enclosed by the membranes of the sarcoplasmic reticulum. |
| Z disc | Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| negative regulation of ryanodine-sensitive calcium-release channel activity | Any process that decreases the activity of a ryanodine-sensitive calcium-release channel. The ryanodine-sensitive calcium-release channel catalyzes the transmembrane transfer of a calcium ion by a channel that opens when a ryanodine class ligand has been bound by the channel complex or one of its constituent parts. |
| regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion | Any process that modulates the frequency, rate or extent of cardiac muscle contraction via the regulation of the release of sequestered calcium ion by sarcoplasmic reticulum into cytosol. The sarcoplasmic reticulum is the endoplasmic reticulum of striated muscle, specialised for the sequestration of calcium ions that are released upon receipt of a signal relayed by the T tubules from the neuromuscular junction. |
| regulation of release of sequestered calcium ion into cytosol | Any process that modulates the frequency, rate or extent of the release into the cytosolic compartment of calcium ions sequestered in the endoplasmic reticulum or mitochondria. |
| regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum | Any process that modulates the rate, frequency or extent of release of sequestered calcium ion into cytosol by the sarcoplasmic reticulum, the process in which the release of sequestered calcium ion by sarcoplasmic reticulum into cytosol occurs via calcium release channels. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKRTHLFIAG | LYLLASCRAE | EGLNFPTYDG | KDRVVSLTEK | NFKQVLKKYD | VLCLYYHESV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SSDKVAQKQF | QLKEIVLELV | AQVLEHKDIG | FVMVDAKKEA | KLAKKLGFDE | EGSLYVLKGD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RTIEFDGEFA | ADVLVEFLLD | LIEDPVEIIN | SKLEVQAFER | IEDQIKLIGF | FKSEESEYYK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AFEEAAEHFQ | PYIKFFATFD | KGVAKKLSLK | MNEVDFYEPF | MDEPIAIPDK | PYTEEELVEF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VKEHQRPTLR | RLRPEDMFET | WEDDLNGIHI | VAFAERSDPD | GYEFLEILKQ | VARDNTDNPD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSIVWIDPDD | FPLLVAYWEK | TFKIDLFKPQ | IGVVNVTDAD | SVWMEIPDDD | DLPTAEELED |
| 370 | 380 | 390 | 400 | ||
| WIEDVLSGKI | NTEDDDNEEG | DDGDDDEDDD | DDDGNNSDEE | SNDDSDDDDE |