Search by BoMiProt ID - Bomi4434


Primary Information

BoMiProt ID Bomi4434
Protein Name Calpastatin/Calpain inhibitor
Organism Bos taurus
Uniprot IdP20811
Milk FractionWhey
Aminoacid Length 705
Molecular Weight 75843
Fasta Sequence https://www.uniprot.org/uniprot/P20811.fasta
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.