Kalpastatin

CAST
Identifikatori
AlijasiCAST
Spoljašnji IDOMIM: 114090 MGI: 1098236 HomoloGene: 7658 GeneCards: CAST
Genska lokacija (miš)
Chromosome 13 (mouse)
Hr.Chromosome 13 (mouse)[1]
Chromosome 13 (mouse)
Genomska lokacija za CAST
Genomska lokacija za CAST
Band13|13 C1Start74,840,487 bp[1]
Kraj74,956,929 bp[1]
Obrazac RNK izražavanja




More reference expression data
Genska ontologija
Molecular function• peptidase inhibitor activity
• cysteine-type endopeptidase inhibitor activity
• GO:0001948, GO:0016582 везивање за протеине плазме
• endopeptidase inhibitor activity
• RNA binding
• cadherin binding
• calcium-dependent cysteine-type endopeptidase inhibitor activity
• protease binding
Cellular component• ендоплазматични ретикулум
• мембрана
• цитосол
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
Ortolozi
VrsteČovekMiš
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)n/aChr 13: 74.84 – 74.96 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Kalpastatin je protein koji je kod ljudi kodiran CAST genom.[4][5][6][7]

Protein kodiran ovim genom je endogeni inhibitor kalpaina (kalcijum-zavisne cisteinske proteaze). On se sastoji od N-terminalnog domena L i četiri ponavljajuća kalpain-inhibitorna domena (domeni 1-4). Ovaj protein učestvuje u proteolizi amiloidnog prekurzornog proteina. Kalpain/kalpastatinski sistem učestvuje u brojnim membranskim fuzionim procesima, kao što su neuralno vezikularna egzocitoza i agregacija trombocita i crvenih krvnih zrnaca. Smatra se da ovaj protein takođe utiče na nivoe izražavanja gena koji kodiraju strukturne i regulatorne proteine. Poznato je nekoliko alternativno splajsovanih transkriptnih varijanti ovog gena, mada oni nisu u potpunosti ispitani.[7]

Reference

  1. ^ а б в GRCm38: Ensembl release 89: ENSMUSG00000021585 - Ensembl, May 2017
  2. ^ „Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  3. ^ „Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  4. ^ Ma H, Yang HQ, Takano E, Lee WJ, Hatanaka M, Maki M (1993). „Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains”. J Biochem. 113 (5): 591—9. PMID 8340353. 
  5. ^ Averna M, De Tullio R, Capini P, Salamino F, Pontremoli S, Melloni E (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. PMID 14685690. doi:10.1007/s00018-003-3288-0. 
  6. ^ Raynaud P, Jayat-Vignoles C, Laforet MP, Leveziel H, Amarger V (2005). „Four promoters direct expression of the calpastatin gene”. Arch Biochem Biophys. 437 (1): 69—77. PMID 15820218. doi:10.1016/j.abb.2005.02.026. 
  7. ^ а б „Entrez Gene: CAST calpastatin”. 

Literatura

  • 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. 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. 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. PMID 2265559. doi:10.1159/000132982. 
  • 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. PMID 2407243. doi:10.1016/0006-291X(90)91035-Q. 
  • 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. 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. PMID 2577276. doi:10.3109/14756368909030363. 
  • 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. PMID 2849943. doi:10.1016/S0006-291X(88)80955-0. 
  • 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. PMC 41320 Слободан приступ. PMID 7638179. doi:10.1073/pnas.92.16.7267. 
  • 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. PMC 295733 Слободан приступ. PMID 7706496. doi:10.1172/JCI117870. 
  • 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. PMID 7710300. doi:10.3109/01485019508987826. 
  • 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. PMC 1137502 Слободан приступ. 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. PMID 9213221. doi:10.1002/(SICI)1097-4644(19970801)66:2<197::AID-JCB7>3.0.CO;2-L. 
  • 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. PMID 9705209. doi:10.1006/abbi.1998.0748. 
  • 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. PMID 9873017. doi:10.1074/jbc.274.2.787. 
  • 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. PMID 10600505. doi:10.1006/bbrc.1999.1819. 

Spoljašnje veze

  • The MEROPS online database for peptidases and their inhibitors: LI27.001[мртва веза]
  • п
  • р
  • у
3.4.11-19: Egzopeptidaza
3.4.11
Aminopeptidaza (Alanin, Arginil, Aspartil, Cistinil, Leucil, Glutamil, Metionil (1, 2), O)
3.4.13
Dipeptidaza (1, 2, 3)
3.4.14
Dipeptidil peptidaza (Katepsin C, Dipeptidil peptidaza-4) · Tripeptidil peptidaza (Tripeptidil peptidaza I, Tripeptidil peptidaza II)
3.4.15
3.4.16
Karboksipeptidaze serinskog tipa: Katepsin A · DD-transpeptidaza
3.4.17
Metalokarboksipeptidaze: Karboksipeptidaza (A, A2, B, C, E, Glutamat II)
Drugi/negrupisni
Metaloeksopeptidaza
3.4.21-24: Endopeptidaza3.4.99: Nepoznato
Stafilokinaza
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
  • п
  • р
  • у
Teme
Tipovi
  • B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
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