CT0189 : CAST protein [Homo sapiens]
[ CaMP Format ]
* Basic Information
| Organism | Homo sapiens (human) |
| Protein Names | CAST protein; Calpastatin; Calpain inhibitor; Sperm BS-17 component |
| Gene Names | CAST |
| Gene Locus | Not available |
| GO Function | Not available |
* Information From OMIM
Text: Calpastatin is the natural inhibitor of calpain (OMIM:114170). In erythrocytes of patients with essential hypertension (OMIM:145500), the level of calpastatin activity has been found to be significantly lower than in the red cells of normotensive subjects. Pontremoli et al. (1988) demonstrated by Western blot analysis that the decreased inhibitor activity is the result of a decrease in the amount of the inhibitor protein. Calpastatin isolated and purified from erythrocytes of normotensive and hypertensive patients had identical specific activities. Pontremoli et al. (1988) also presented evidence indicating that the decreased level of calpastatin cannot be ascribed to accelerated decay during the red cell life span. Using a cDNA probe encoding the 5-prime terminal region of CAST for spot-blot analysis of sorted chromosomes and chromosomal in situ hybridization, Inazawa et al. (1990) assigned the CAST gene to 5q14-q22. Inazawa et al. (1991) mapped CAST to 5q15-q21 by 2 methods of in situ hybridization and confirmed the results by spot-blot analysis of sorted chromosomes. Mimori et al. (1995) demonstrated that anti-calpastatin autoantibodies are present in as many as 57% of rheumatoid arthritis patients and concluded that they may participate in pathogenic mechanisms of this and other rheumatic diseases which showed a lower frequency.
* Structure Information
1. Primary Information
Length: 667 aa
Average Mass: 71.894 kDa
Monoisotopic Mass: 71.851 kDa
2. Domain Information
Annotated Domains: interpro / pfam / smart / prosite
Computationally Assigned Domains (Pfam+HMMER):
| domain name | begin | end | score | e-value |
|---|---|---|---|---|
| Calpain_inhib 1. | 58 | 183 | 178.7 | 1.7e-50 |
| Calpain_inhib 2. | 191 | 317 | 195.4 | 1.6e-55 |
| Calpain_inhib 3. | 328 | 460 | 220.8 | 3.5e-63 |
| Calpain_inhib 4. | 471 | 597 | 227.1 | 4.4e-65 |
3. Sequence Information
Fasta Sequence: CT0189.fasta
Amino Acid Sequence and Secondary Structures (PsiPred):
4. 3D Information
Not Available.
* References
[PubMed ID: 12477932] Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA, Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11.