(平滑筋のアクチン結合タンパク質)カルポニン
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/01/14 16:27:28」(JST)
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Calponin Homology Domain |
|
CH domain from H.Sapiends Calponin 1. PDB 1wyp |
Identifiers |
Symbol |
CH |
Pfam |
PF00307 |
Pfam clan |
CL0188 |
InterPro |
IPR001715 |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe |
PDBsum |
structure summary |
|
calponin 1, basic, smooth muscle |
|
Solution structure of the CH domain of human Calponin 1. Rainbow colored cartoon (N-terminus = blue, C-terminus = red).[1] |
Identifiers |
Symbol |
CNN1 |
Entrez |
1264 |
HUGO |
2155 |
OMIM |
600806 |
PDB |
1WYP |
RefSeq |
NM_001299 |
UniProt |
P51911 |
Other data |
Locus |
Chr. 19 p13.2-13.1 |
calponin 2 |
Identifiers |
Symbol |
CNN2 |
Entrez |
1265 |
HUGO |
2156 |
OMIM |
602373 |
RefSeq |
NM_004368 |
UniProt |
Q99439 |
Other data |
Locus |
Chr. 21 q11.1 |
calponin 3, acidic |
Identifiers |
Symbol |
CNN3 |
Entrez |
1266 |
HUGO |
2157 |
OMIM |
602374 |
RefSeq |
NM_001839 |
UniProt |
Q6FHA7 |
Other data |
Locus |
Chr. 1 p22-p21 |
Calponin is a calcium binding protein. Calponin tonically inhibits the ATPase activity of myosin in smooth muscle. Phosphorylation of calponin by a protein kinase, which is dependent upon calcium binding to calmodulin, releases the calponin's inhibition of the smooth muscle ATPase.
Structure and function
Calponin is mainly made up of α-helices with hydrogen bond turns. It is a binding protein and is made up of three domains. These domains in order of appearance are Calponin Homology (CH), regulatory domain (RD), and Click-23, domain that contains the calponin repeats. At the CH domain calponin binds to α-actin and filamin and binds to actin within the RD domain. Calponin does not bind to actin in the CH domain as generally described due to the fact that the CH domain is known to bind calcium to calmodulin which then inhibits actin binding. Calponin is responsible for binding many actin binding proteins, phospholipids, and regulates the actin/myosin interaction. Calponin is also thought to negatively affect the bone making process due to being expressed in high amounts in osteoblasts.[2]
References
- ^ PDB 1WYP; Tomizawa T, Kigawa T, Koshiba S, Inoue M, Yokoyama S. "RCSB PDB - 1WYP Structure Summary". RCSB Protein Data Bank. doi:10.2210/pdb1wyp/pdb. http://www.pdb.org/pdb/explore/explore.do?structureId=1WYP.
- ^ Maciver S. "The Calponin Family". Department of Biomedical Sciences, University of Edinburgh. http://www.bms.ed.ac.uk/research/others/smaciver/Cyto-Topics/Calponin_Family.htm. Retrieved 2011-04-25.
External links
- Calponin at the US National Library of Medicine Medical Subject Headings (MeSH)
UpToDate Contents
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English Journal
- mRNA and miRNA expression patterns associated to pathways linked to metal mixture health effects.
- Martínez-Pacheco M, Hidalgo-Miranda A, Romero-Córdoba S, Valverde M, Rojas E.SourceUniversidad Nacional Autónoma de México, Instituto de Investigaciones Biomédicas, Departamento de Medicina Genómica y Toxicología Ambiental, C.U., 04510 México, México.
- Gene.Gene.2014 Jan 10;533(2):508-14. doi: 10.1016/j.gene.2013.09.049. Epub 2013 Sep 27.
- Metals are a threat to human health by increasing disease risk. Experimental data have linked altered miRNA expression with exposure to some metals. MiRNAs comprise a large family of non-coding single-stranded molecules that primarily function to negatively regulate gene expression post-transcriptio
- PMID 24080485
- Linking phospholipase C isoforms with differentiation function in human vascular smooth muscle cells.
- Mackenzie LS, Lymn JS, Hughes AD.SourceDepartment of Pharmacology, School of Life and Medical Sciences, University of Hertfordshire, College Lane, Hatfield AL10 9AB, UK; Department of Clinical Pharmacology, National Heart & Lung Institute, Imperial College London, QEQM Wing, St. Mary's Hospital, Paddington, London W2 1NY, UK. Electronic address: l.mackenzie2@herts.ac.uk.
- Biochimica et biophysica acta.Biochim Biophys Acta.2013 Dec;1833(12):3006-12. doi: 10.1016/j.bbamcr.2013.08.005. Epub 2013 Aug 14.
- The phosphoinositol-phospholipase C (PLC) family of enzymes consists of a number of isoforms, each of which has different cellular functions. PLCγ1 is primarily linked to tyrosine kinase transduction pathways, whereas PLCδ1 has been associated with a number of regulatory proteins, including those
- PMID 23954266
- Changes in the Expression of Smooth Muscle Contractile Proteins in TNBS- and DSS-Induced Colitis in Mice.
- Alkahtani R, Mahavadi S, Al-Shboul O, Alsharari S, Grider JR, Murthy KS.SourceDepartment of Physiology, VCU Program in Enteric Neuromuscular Sciences, Virginia Commonwealth University, Richmond, VA, 23298-0551, USA.
- Inflammation.Inflammation.2013 Dec;36(6):1304-15. doi: 10.1007/s10753-013-9669-0.
- Thin filament-associated proteins such as calponin, caldesmon, tropomyosin, and smoothelin are thought to regulate acto-myosin interaction and thus, muscle contraction. However, the effect of inflammation on the expression of thin filament-associated proteins is not known. The aim of the present stu
- PMID 23794034
Japanese Journal
- A mutation of the fission yeast EB1 overcomes negative regulation by phosphorylation and stabilizes microtubules.
- Iimori Makoto,Ozaki Kanako,Chikashige Yuji,Habu Toshiyuki,Hiraoka Yasushi,Maki Takahisa,Hayashi Ikuko,Obuse Chikashi,Matsumoto Tomohiro
- Experimental cell research 318(3), 262-275, 2012-02-01
- … We have generated a mutation (89R) replacing glutamine with arginine in the calponin homology (CH) domain of Mal3. …
- NAID 120003874262
- Characterization of a novel rice kinesin O12 with a calponin homology domain
- Umezu Nozomi,Umeki Nobuhisa,Mitsui Toshiaki [他]
- Journal of Biochemistry 149(1), 91-101, 2011-01
- NAID 40017664419
Related Links
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- Fibroadenoma (FFPE) stained with Anti-Calponin, Code M3556. Disclaimer: Due to variances among color computer monitors, the colors you see on your screen may not be the exact colors of the stain. The image you see should ...
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