Calpastatin

Details

Name
Calpastatin
Synonyms
  • Calpain inhibitor
  • Sperm BS-17 component
Gene Name
CAST
Organism
Humans
Amino acid sequence
>lcl|BSEQ0001801|Calpastatin
MNPTETKAIPVSQQMEGPHLPNKKKHKKQAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEH
TEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAI
SGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGP
EVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFT
CGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGT
RQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKP
KPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPP
EPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPD
YRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAIS
EVVSQTPASTTQAGAPPRDTSQSDKDLDDALDKLSDSLGQRQPDPDENKPMEDKVKEKAK
AEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDS
CPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD
Number of residues
708
Molecular Weight
76572.035
Theoretical pI
4.7
GO Classification
Functions
calcium-dependent cysteine-type endopeptidase inhibitor activity / endopeptidase inhibitor activity / poly(A) RNA binding
Processes
aging / brain development / egg activation / liver development / myoblast differentiation / myoblast fusion / negative regulation of cell cycle arrest / negative regulation of type B pancreatic cell apoptotic process / organ regeneration
Components
cytoplasm / cytosol / endoplasmic reticulum / membrane / nucleus
General Function
Poly(a) rna binding
Specific Function
Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0019027|Calpastatin (CAST)
ATGTCCCAGCCCGGCCAGAAGCCCGCCGCCTCCCCGCGGCCCCGGCGAGCAGCCGCCGCC
CGCCGCACCCATGAGCATGTCAGTGAAAAAACCAGTGAATCGCCTTCCAAACCAGGAGAA
AAGAAAGGATCAGATGAGAAAAAAGCAGCAAGCCTCGGCAGCAGTCAATCCTCCAGAACC
TATGCTGGTGGAACAGCCTCGGCCACCAAGGTGTCAGCTTCCTCTGGTGCAACCAGCAAG
TCTTCCAGTATGAATCCCACAGAAACCAAGGCTGTAAAAACAGAACCTGAGAAGAAGTCA
CAGTCAACCAAGCCAAAAAGCCTACCCAAGCAGGCATCAGATACAGGAAGTAACGATGCT
CACAATAAAAAAGCAGTTTCCAGATCAGCTGAACAGCAGCCATCAGAGAAATCAACAGAA
CCAAAGACTAAACCACAAGACATGATTTCTGCTGGTGGAGAGAGTGTTGCTGGTATCACT
GCAATATCTGGCAAGCCGGGTGACAAGAAAAAAGAAAAGAAATCATTAACCCCAGCTGTG
CCAGTTGAATCTAAACCGGATAAACCATCGGGAAAGTCAGGCATGGATGCTGCTTTGGAT
GACTTAATAGATACTTTAGGAGGACCTGAAGAAACTGAAGAAGAAAATACAACGTATACT
GGACCAGAAGTTTCAGATCCAATGAGTTCCACCTACATAGAGGAATTGGGTAAAAGAGAA
GTCACAATTCCTCCAAAATATAGGGAACTATTGGCTAAAAAGGAAGGGATCACAGGGCCT
CCTGCAGACTCTTCGAAACCCATAGGGCCAGATGATGCTATAGACGCCTTGTCATCTGAC
TTCACCTGTGGGTCGCCTACAGCTGCTGGAAAGAAAACTGAAAAAGAGGAATCTACAGAA
GTTTTAAAAGCTCAGTCAGCAGGGACAGTCAGAAGTGCTGCTCCACCCCAAGAGAAGAAA
AGAAAGGTGGAGAAGGATACAATGAGTGATCAAGCACTCGAGGCTCTGTCGGCTTCACTG
GGCACCCGGCAAGCAGAACCTGAGCTCGACCTCCGCTCAATTAAGGAAGTCGATGAGGCA
AAAGCTAAAGAAGAAAAACTAGAGAAGTGTGGTGAGGATGATGAAACAATCCCATCTGAG
TACAGATTAAAACCAGCCACGGATAAAGATGGAAAACCACTATTGCCAGAGCCTGAAGAA
AAACCCAAGCCTCGGAGTGAATCAGAACTCATTGATGAACTTTCAGAAGATTTTGACCGG
TCTGAATGTAAAGAGAAACCATCTAAGCCAACTGAAAAGACAGAAGAATCTAAGGCCGCT
GCTCCAGCTCCTGTGTCGGAGGCTGTGTGTCGGACCTCCATGTGTAGTATACAGTCAGCA
CCCCCTGAGCCGGCTACCTTGAAGGGCACAGTGCCAGATGATGCTGTAGAAGCCTTGGCT
GATAGCCTGGGGAAAAAGGAAGCAGATCCAGAAGATGGAAAACCTGTGATGGATAAAGTC
AAGGAGAAGGCCAAAGAAGAAGACCGTGAAAAGCTTGGTGAAAAAGAAGAAACAATTCCT
CCTGATTATAGATTAGAAGAGGTCAAGGATAAAGATGGAAAGCCACTCCTGCCAAAAGAG
TCTAAGGAACAGCTTCCACCCATGAGTGAAGACTTCCTTCTGGATGCTTTGTCTGAGGAC
TTCTCTGGTCCACAAAATGCTTCATCTCTTAAATTTGAAGATGCTAAACTTGCTGCTGCC
ATCTCTGAAGTGGTTTCCCAAACCCCAGCTTCAACGACCCAAGCTGGAGCCCCACCCCGT
GATACCTCGCAGAGTGACAAAGACCTCGATGATGCCTTGGATAAACTCTCTGACAGTCTA
GGACAAAGGCAGCCTGACCCAGATGAGAACAAACCAATGGAAGATAAAGTAAAGGAAAAA
GCTAAAGCTGAACATAGAGACAAGCTTGGAGAAAGAGATGACACTATCCCACCTGAATAC
AGACATCTCCTGGATGATAATGGACAGGACAAACCAGTGAAGCCACCTACAAAGAAATCA
GAGGATTCAAAGAAACCTGCAGATGACCAAGACCCCATTGATGCTCTCTCAGGAGATCTG
GACAGCTGTCCCTCCACTACAGAAACCTCACAGAACACAGCAAAGGATAAGTGCAAGAAG
GCTGCTTCCAGCTCCAAAGCACCTAAGAATGGAGGTAAAGCGAAGGATTCAGCAAAGACA
ACAGAGGAAACTTCCAAGCCAAAAGATGACTAA
Chromosome Location
5
Locus
5q15
External Identifiers
ResourceLink
UniProtKB IDP20810
UniProtKB Entry NameICAL_HUMAN
GenBank Protein ID303599
GenBank Gene IDD16217
GenAtlas IDCAST
HGNC IDHGNC:1515
General References
  1. Asada K, Ishino Y, Shimada M, Shimojo T, Endo M, Kimizuka F, Kato I, Maki M, Hatanaka M, Murachi T: cDNA cloning of human calpastatin: sequence homology among human, pig, and rabbit calpastatins. J Enzyme Inhib. 1989;3(1):49-56. [Article]
  2. Zhu H, Zhou ZM, Li JM, Zhu H, Cheng LJ, Shan YX, Yin LL, Sha JH: Cloning and characterization of a novel isoform of calpastatin in human adult testis. Acta Pharmacol Sin. 2002 May;23(5):450-4. [Article]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  4. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [Article]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  6. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [Article]
  7. Lee WJ, Ma H, Takano E, Yang HQ, Hatanaka M, Maki M: Molecular diversity in amino-terminal domains of human calpastatin by exon skipping. J Biol Chem. 1992 Apr 25;267(12):8437-42. [Article]
  8. Maki M, Bagci H, Hamaguchi K, Ueda M, Murachi T, Hatanaka M: Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. J Biol Chem. 1989 Nov 15;264(32):18866-9. [Article]
  9. Uemori T, Shimojo T, Asada K, Asano T, Kimizuka F, Kato I, Maki M, Hatanaka M, Murachi T, Hanzawa H, et al.: Characterization of a functional domain of human calpastatin. Biochem Biophys Res Commun. 1990 Feb 14;166(3):1485-93. [Article]
  10. Wang LF, Wei SG, Miao SY, Liu QY, Koide SS: Calpastatin gene in human testis. Biochem Mol Biol Int. 1994 May;33(2):245-51. [Article]
  11. Despres N, Talbot G, Plouffe B, Boire G, Menard HA: Detection and expression of a cDNA clone that encodes a polypeptide containing two inhibitory domains of human calpastatin and its recognition by rheumatoid arthritis sera. J Clin Invest. 1995 Apr;95(4):1891-6. [Article]
  12. Adachi Y, Ishida-Takahashi A, Takahashi C, Takano E, Murachi T, Hatanaka M: Phosphorylation and subcellular distribution of calpastatin in human hematopoietic system cells. J Biol Chem. 1991 Feb 25;266(6):3968-72. [Article]
  13. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [Article]
  14. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  15. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  16. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  17. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  18. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  19. Hendriks IA, D'Souza RC, Yang B, Verlaan-de Vries M, Mann M, Vertegaal AC: Uncovering global SUMOylation signaling networks in a site-specific manner. Nat Struct Mol Biol. 2014 Oct;21(10):927-36. doi: 10.1038/nsmb.2890. Epub 2014 Sep 14. [Article]
  20. Lin Z, Zhao J, Nitoiu D, Scott CA, Plagnol V, Smith FJ, Wilson NJ, Cole C, Schwartz ME, McLean WH, Wang H, Feng C, Duo L, Zhou EY, Ren Y, Dai L, Chen Y, Zhang J, Xu X, O'Toole EA, Kelsell DP, Yang Y: Loss-of-function mutations in CAST cause peeling skin, leukonychia, acral punctate keratoses, cheilitis, and knuckle pads. Am J Hum Genet. 2015 Mar 5;96(3):440-7. doi: 10.1016/j.ajhg.2014.12.026. Epub 2015 Feb 12. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01373CalciumnutraceuticalunknownDetails
DB11638Artenimolapproved, experimental, investigationalunknownligandDetails