Primary Information |
|---|
| BoMiProt ID | Bomi4434 |
|---|
| Protein Name | Calpastatin/Calpain inhibitor |
|---|
| Organism | Bos taurus |
|---|
| Uniprot ID | P20811 |
|---|
| Milk Fraction | Whey |
|---|
| Aminoacid Length | 705 |
|---|
| Molecular Weight | 75843 |
|---|
| FASTA Sequence |
Download |
|---|
| Gene Name | CAST |
|---|
| Protein Existence Status | reviewed |
|---|
Secondary Information |
|---|
| Protein Function | Specific inhibition of calpain (calcium-dependent cysteine protease). endogenous inhibitor of μ-calpain and m-calpain that regulates calpain activity. Degrades non-specific cell components, including proteins and micro-organisms, via isolation membranes. |
|---|
| Biochemical Properties | Leu 612-Gly 613 dipeptide is well conserved across the four inhibitory domains of calpastatin.two unique N-terminal domains (termed dXL and dL) and four repetitive inhibitor domains (d1–d4).The N-terminal domains regulate the Ca2+ channel, 4 homologous domains d1–d4 are together capable of inhibiting calpain.33 α-helices and eight β-sheets in the sequence of calpastatin.An 11-aa short peptide on the dL (EGKPKEHTEPK) may be responsible for Ca2+ channel repriming. |
|---|
| PTMs | Phosphorylation on Ser and Thr,Ubl conjugation |
|---|
Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P20811|ICAL_BOVIN Calpastatin OS=Bos taurus OX=9913 GN=CAST PE=1 SV=2
MNPTEAKAVKTEPEKKPQSSKPSVVHEKKTQEVKPKEHTEPKSLPKHSSDTGVKHAPKEK
AVSKS*65SEQPPSEKSTKPKTKSQDKISGGGKSTVPAAAAAASAEPADKNKENKLLT*115SAVPA
ESKPSKPSGKSDMDTALDDLIDTLGEPEEMKEDNTTYTGPEVSDPMSSTYIEELGKREST
PPPKYKELLNKEEGIAGPPPDS*202LKPLGPNDAIDALSSDFTCSSLQLTTCS*230PTADGKETEK
EKSTEEALKAQSAGVIRSAAPPKEKRRKVEEDTMTEQALQALSASLGTRKPEPELDPSSI
REVDEAKAKEEKVKKCGEDEETVPSEYRLKPATDKDGKPLLPEAEEKPKPLS*352ES*354ELIDEL
S*361EDFDQSKPTEKQSKPTEKTEASPAAAPYPVAEDVPRTSMCSLQSAPPTAAPAKGMVPDD
AVEALAGS*428LPKKEADPEDGKPVEDKVKEKAKEEDRENFGEKEETIPPDYRLEEAKDKDGK
PLLPKEVKEPLPPLSEDVLLDALS*504KDFTVPSDTSS*515PQFEDAKLSAVVSEVVSQTPAPTTQ
AAGPPPDCARDNKELDDALDQLS*563DTLGQRQPDPDENKPVEDKVKEKAKAEHRDKLGERDD
TIPPKYQHLLDDNKEGTPGKPKDQRAQGIRNCGEKPAGAQDPIDALSGDFDSCPSTTETS
TDTPKDKDKKPASVPKHLGNGGKAKDSTKAKEETSKPKADGKSTS
|
|---|
| Predicted Disorder Regions | 12-91, 120-131, 147-243, 247-271, 290-390, 421-459, 504-582,635-637,666-705 |
|---|
| DisProt Annotation | |
|---|
| TM Helix Prediction | No TM helices |
|---|
| Significance of PTMs | Calpastatin I phosphorylation is promoted by PKA or PKC,as a result of which there is a decrease in its inhibitory efficiency. |
|---|
| Bibliography | 1.Hanna RA, Campbell RL, Davies PL. Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin. Nature. 2008 Nov 20;456(7220):409-12. doi: 10.1038/nature07451. PMID: 19020623. 2.Salamino F, Averna M, Tedesco I, De Tullio R, Melloni E, Pontremoli S. Modulation of rat brain calpastatin efficiency by post-translational modifications. FEBS Lett. 1997 Aug 4;412(3):433-8. doi: 10.1016/s0014-5793(97)00819-3. PMID: 9276442. |
|---|
