Calpastatin

Protein found in humans
CAST
Identifiers
AliasesCAST, BS-17, PLACK, calpastatin
External IDsOMIM: 114090; MGI: 1098236; HomoloGene: 7658; GeneCards: CAST; OMA:CAST - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for CAST
Genomic location for CAST
Band5q15Start96,525,267 bp[1]
End96,779,595 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for CAST
Genomic location for CAST
Band13|13 C1Start74,840,487 bp[2]
End74,956,929 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • bronchial epithelial cell

  • epithelium of colon

  • human penis

  • synovial joint

  • oral cavity

  • urethra

  • skin of thigh

  • mucosa of pharynx

  • skin of hip
Top expressed in
  • spermatid

  • skin of external ear

  • granulocyte

  • seminiferous tubule

  • lip

  • esophagus

  • transitional epithelium of urinary bladder

  • muscle of thigh

  • stroma of bone marrow

  • triceps brachii muscle
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • peptidase inhibitor activity
  • cysteine-type endopeptidase inhibitor activity
  • protein binding
  • endopeptidase inhibitor activity
  • RNA binding
  • cadherin binding
  • calcium-dependent cysteine-type endopeptidase inhibitor activity
  • protease binding
Cellular component
  • endoplasmic reticulum
  • membrane
  • cytosol
Biological process
  • negative regulation of peptidase activity
  • negative regulation of type B pancreatic cell apoptotic process
  • inhibition of cysteine-type endopeptidase activity
  • presynaptic active zone organization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

831

12380

Ensembl

ENSG00000153113

ENSMUSG00000021585

UniProt

P20810

P51125

RefSeq (mRNA)
NM_001042440
NM_001042441
NM_001042442
NM_001042443
NM_001042444

NM_001042445
NM_001042446
NM_001190442
NM_001284212
NM_001284213
NM_001750
NM_173060
NM_173061
NM_173062
NM_173063
NM_001330626
NM_001330627
NM_001330628
NM_001330629
NM_001330630
NM_001330631
NM_001330632
NM_001330633
NM_001330634
NM_001375317

NM_001301153
NM_001301155
NM_001301156
NM_001301157
NM_001301158

NM_001301160
NM_001301181
NM_009817

RefSeq (protein)
NP_001035905
NP_001035906
NP_001035907
NP_001035908
NP_001035909

NP_001035910
NP_001035911
NP_001177371
NP_001271141
NP_001271142
NP_001317555
NP_001317556
NP_001317557
NP_001317558
NP_001317559
NP_001317560
NP_001317561
NP_001317562
NP_001317563
NP_001741
NP_775083
NP_001362246

NP_001288082
NP_001288084
NP_001288085
NP_001288086
NP_001288087

NP_001288089
NP_001288110
NP_033947

Location (UCSC)Chr 5: 96.53 – 96.78 MbChr 13: 74.84 – 74.96 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Calpastatin is a protein that in humans is encoded by the CAST gene.[5][6][7][8]

The protein encoded by this gene is an endogenous calpain (calcium-dependent cysteine protease) inhibitor. It consists of an N-terminal domain L and four repetitive calpain-inhibition domains (domains 1–4), and it is involved in the proteolysis of amyloid precursor protein.[citation needed] The calpain/calpastatin system is involved in numerous membrane fusion events, such as neural vesicle exocytosis and platelet and red-cell aggregation. The encoded protein is also thought to affect the expression levels of genes encoding structural or regulatory proteins. Several alternatively spliced transcript variants of this gene have been described, but the full-length natures of only some have been determined.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000153113 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021585 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Ma H, Yang HQ, Takano E, Lee WJ, Hatanaka M, Maki M (Sep 1993). "Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains". J Biochem. 113 (5): 591–9. doi:10.1093/oxfordjournals.jbchem.a124088. PMID 8340353.
  6. ^ Averna M, De Tullio R, Capini P, Salamino F, Pontremoli S, Melloni E (Dec 2003). "Changes in calpastatin localization and expression during calpain activation: a new mechanism for the regulation of intracellular Ca(2+)-dependent proteolysis". Cell Mol Life Sci. 60 (12): 2669–78. doi:10.1007/s00018-003-3288-0. PMC 11138551. PMID 14685690. S2CID 23794801.
  7. ^ Raynaud P, Jayat-Vignoles C, Laforet MP, Leveziel H, Amarger V (Apr 2005). "Four promoters direct expression of the calpastatin gene". Arch Biochem Biophys. 437 (1): 69–77. doi:10.1016/j.abb.2005.02.026. PMID 15820218.
  8. ^ a b "Entrez Gene: CAST calpastatin".

Further reading

  • Murachi T (1989). "Intracellular regulatory system involving calpain and calpastatin". Biochem. Int. 18 (2): 263–94. PMID 2548504.
  • Lee WJ, Ma H, Takano E, et al. (1992). "Molecular diversity in amino-terminal domains of human calpastatin by exon skipping". J. Biol. Chem. 267 (12): 8437–42. doi:10.1016/S0021-9258(18)42463-5. hdl:2433/168719. PMID 1569094.
  • Adachi Y, Ishida-Takahashi A, Takahashi C, et al. (1991). "Phosphorylation and subcellular distribution of calpastatin in human hematopoietic system cells". J. Biol. Chem. 266 (6): 3968–72. doi:10.1016/S0021-9258(19)67888-9. PMID 1995645.
  • Inazawa J, Nakagawa H, Misawa S, et al. (1991). "Assignment of the human calpastatin gene (CAST) to chromosome 5 at region q14----q22". Cytogenet. Cell Genet. 54 (3–4): 156–8. doi:10.1159/000132982. PMID 2265559.
  • Uemori T, Shimojo T, Asada K, et al. (1990). "Characterization of a functional domain of human calpastatin". Biochem. Biophys. Res. Commun. 166 (3): 1485–93. doi:10.1016/0006-291X(90)91035-Q. PMID 2407243.
  • Maki M, Bagci H, Hamaguchi K, et al. (1989). "Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene". J. Biol. Chem. 264 (32): 18866–9. doi:10.1016/S0021-9258(19)47235-9. PMID 2553724.
  • Murachi T, Takano E, Maki M, et al. (1990). "Cloning and expression of the genes for calpains and calpastatins". Biochem. Soc. Symp. 55: 29–44. PMID 2559735.
  • Asada K, Ishino Y, Shimada M, et al. (1991). "cDNA cloning of human calpastatin: sequence homology among human, pig, and rabbit calpastatins". J. Enzym. Inhib. 3 (1): 49–56. doi:10.3109/14756368909030363. PMID 2577276.
  • Pontremoli S, Salamino F, Sparatore B, et al. (1989). "Characterization of the calpastatin defect in erythrocytes from patients with essential hypertension". Biochem. Biophys. Res. Commun. 157 (3): 867–74. doi:10.1016/S0006-291X(88)80955-0. PMID 2849943.
  • Mimori T, Suganuma K, Tanami Y, et al. (1995). "Autoantibodies to calpastatin (an endogenous inhibitor for calcium-dependent neutral protease, calpain) in systemic rheumatic diseases". Proc. Natl. Acad. Sci. U.S.A. 92 (16): 7267–71. Bibcode:1995PNAS...92.7267M. doi:10.1073/pnas.92.16.7267. PMC 41320. PMID 7638179.
  • Després N, Talbot G, Plouffe B, et al. (1995). "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. 95 (4): 1891–6. doi:10.1172/JCI117870. PMC 295733. PMID 7706496.
  • Wei SG, Wang LF, Miao SY, et al. (1995). "Expression of the calpastatin gene segment during spermiogenesis in human testis: an in situ hybridization study". Arch. Androl. 34 (1): 9–12. doi:10.3109/01485019508987826. PMID 7710300.
  • Wang LF, Wei SG, Miao SY, et al. (1994). "Calpastatin gene in human testis". Biochem. Mol. Biol. Int. 33 (2): 245–51. PMID 7951045.
  • Schwarz-Benmeir N, Glaser T, Barnoy S, Kosower NS (1995). "Calpastatin in erythrocytes of young and old individuals". Biochem. J. 304 (2): 365–70. doi:10.1042/bj3040365. PMC 1137502. PMID 7998969.
  • Fujitani K, Kambayashi J, Sakon M, et al. (1997). "Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells". J. Cell. Biochem. 66 (2): 197–209. doi:10.1002/(SICI)1097-4644(19970801)66:2<197::AID-JCB7>3.0.CO;2-L. PMID 9213221. S2CID 85163404.
  • Wang KK, Posmantur R, Nadimpalli R, et al. (1998). "Caspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis". Arch. Biochem. Biophys. 356 (2): 187–96. doi:10.1006/abbi.1998.0748. PMID 9705209. S2CID 11593624.
  • Han Y, Weinman S, Boldogh I, et al. (1999). "Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation". J. Biol. Chem. 274 (2): 787–94. doi:10.1074/jbc.274.2.787. PMID 9873017.
  • Ishikawa H, Nakagawa Y, Shimizu K, et al. (2000). "Inflammatory cytokines induced down-regulation of m-calpain mRNA expression in fibroblastic synoviocytes from patients with osteoarthritis and rheumatoid arthritis". Biochem. Biophys. Res. Commun. 266 (2): 341–6. doi:10.1006/bbrc.1999.1819. hdl:2433/180881. PMID 10600505.
  • The MEROPS online database for peptidases and their inhibitors: LI27.001[permanent dead link]
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3.4.11-19: Exopeptidase
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Other/ungrouped
3.4.21-25: Endopeptidase3.4.99: Unknown
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