CALM3

CALM3
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	2VAY, 1Y6W, 4JPZ, 3UCY, 1WRZ, 4G28, 1ZOT, 1YRT, 1IQ5, 1CDL, 2LL6, 3HR4, 4BW7, 4BW8, 1YR5, 4J9Y, 4LZX, 1L7Z, 1ZUZ, 2BE6, 2V01, 1XFV, 2M55, 1CTR, 2I08, 2MG5, 2R28, 3O77, 4UPU, 2L7L, 2K0F, 2M0K, 4V0C, 1SW8, 2WEL, 3DVK, 2M0J, 3DVM, 2KUH, 1K90, 1K93, 4G27, 1CLL, 2KUG, 1XFX, 4DJC, 2LQC, 2LQP, 4L79, 2W73, 2LV6, 1NKF, 2JZI, 3UCT, 4GOW, 1J7O, 1PK0, 4Q5U, 2V02, 3BYA, 4Q57, 2KNE, 1YRU, 2Y4V, 2L53, 2F3Y, 3O78, 1LVC, 4M1L, 2K0E, 1S26, 4DCK, 1XFW, 3SUI, 2X0G, 3EWV, 1XFY, 2LL7, 4OVN, 3J41, 2BKI, 1SK6, 3DVJ, 3UCW, 2LGF, 4UMO, 3DVE, 4JQ0, 3OXQ, 2K61, 1XFU, 3SJQ, 2K0J, 4BYF, 1J7P, 3G43, 3EWT, 4J9Z, 1XFZ, 2F3Z, 1IWQ, 2N6A, 2HF5, 2N27, 4ZLK, 5COC,%%s2HF5 Contents Context ; Clinical significance ; References ; Further reading ; External links ;
Identifiers
Aliases	CALM3 , HEL-S-72, PHKD, PHKD3, calmodulin 3 (phosphorylase kinase, delta), CaM, CaMIII, calmodulin 3, CAM1, CAMB, CALM, CAM2, CPVT6, LQT16
External IDs	OMIM: 114183 HomoloGene: 134804 GeneCards: CALM3
Gene location (Human)
Chr.	Chromosome 19 (human)
End	46,610,782 bp
RNA expression pattern
	Top expressed in
	prefrontal cortex; ; nucleus accumbens; ; amygdala; ; cingulate gyrus; ; Brodmann area 9; ; ganglionic eminence; ; caudate nucleus; ; monocyte; ; putamen; ; parietal lobe;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	calcium ion binding ; protein binding ; calcium channel inhibitor activity ; protein kinase binding ; titin binding ; protein serine/threonine kinase activator activity ; transmembrane transporter binding ; metal ion binding ; protein phosphatase activator activity ; adenylate cyclase binding ; disordered domain specific binding ; inositol-1,4,5-trisphosphate 3-kinase activity ; ligand-gated ion channel activity ; adenylate cyclase activator activity ; protein domain specific binding ; nitric-oxide synthase regulator activity ; type 3 metabotropic glutamate receptor binding ; N-terminal myristoylation domain binding ; phosphatidylinositol 3-kinase binding ; protein N-terminus binding ; calcium-dependent protein binding ; nitric-oxide synthase binding ; kinase activity ;
Cellular component	cytoplasm ; cytosol ; calcium channel complex ; extracellular region ; spindle microtubule ; neuron projection ; cytoskeleton ; nucleus ; centrosome ; voltage-gated potassium channel complex ; extracellular exosome ; spindle pole ; growth cone ; plasma membrane ; spindle ; sarcomere ; nucleoplasm ; vesicle ; postsynaptic density ; catalytic complex ; microtubule organizing center ; synaptic vesicle membrane ; mitochondrial membrane ; protein-containing complex ; myelin sheath ; intracellular anatomical structure ;
Biological process	muscle contraction ; response to amphetamine ; positive regulation of protein serine/threonine kinase activity ; detection of calcium ion ; Fc-epsilon receptor signaling pathway ; positive regulation of phosphoprotein phosphatase activity ; G2/M transition of mitotic cell cycle ; regulation of high voltage-gated calcium channel activity ; positive regulation of DNA binding ; substantia nigra development ; positive regulation of protein dephosphorylation ; inositol phosphate metabolic process ; positive regulation of nitric-oxide synthase activity ; glycogen catabolic process ; positive regulation of cyclic-nucleotide phosphodiesterase activity ; G protein-coupled receptor signaling pathway ; regulation of cytokinesis ; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion ; regulation of rhodopsin mediated signaling pathway ; response to corticosterone ; negative regulation of peptidyl-threonine phosphorylation ; activation of adenylate cyclase activity ; regulation of heart rate ; positive regulation of ryanodine-sensitive calcium-release channel activity ; response to calcium ion ; regulation of ryanodine-sensitive calcium-release channel activity ; regulation of nitric-oxide synthase activity ; platelet degranulation ; negative regulation of ryanodine-sensitive calcium-release channel activity ; MAPK cascade ; positive regulation of peptidyl-threonine phosphorylation ; positive regulation of protein autophosphorylation ; regulation of cardiac muscle contraction ; regulation of cell communication by electrical coupling involved in cardiac conduction ; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum ; calcium-mediated signaling ; ion transmembrane transport ; Wnt signaling pathway, calcium modulating pathway ; positive regulation of GTPase activity ; protein methylation ; establishment of protein localization to membrane ; establishment of protein localization to mitochondrial membrane ; regulation of synaptic vesicle endocytosis ; regulation of synaptic vesicle exocytosis ; phosphorylation ;
	Sources:Amigo / QuickGO
Orthologs
	808
	n/a
	ENSG00000160014
	n/a
	P0DP23 ; Q96HY3 ; P0DP24
	n/a
NM_001329921 ; NM_001329922 ; NM_001329923 ; NM_001329924 ; NM_001329925 ;
	NM_001329926 ; NM_005184
	n/a
NP_001292553 ; NP_001292554 ; NP_001292555 ; NP_001734 ; NP_001316850 ;
	NP_001316851 ; NP_001316852 ; NP_001316853 ; NP_001316854 ; NP_001316855 ; NP_005175 ; NP_008819 ; NP_001292554.1 ; NP_001292555.1 ; NP_001350598 ; NP_001350599 ; NP_008819 ; NP_001292553 ; NP_001292554 ; NP_001292555 ; NP_001734 ; NP_001316850 ; NP_001316851 ; NP_001316852 ; NP_001316853 ; NP_001316854 ; NP_001316855 ; NP_005175
	n/a
	Wikidata
View/Edit Human

Last updated December 04, 2023

Calmodulin 3 is a protein that in humans is encoded by the CALM3 gene.

CALM-3 is best known for contracting the heart muscles, and depending on whether this activity is consistent or not, other diseases could emerge as a downside. It is able to maintain or regulate in different types of biological systems, such as cytokinesis or the centrosome cycle.^[3]

Calmodulin-3 is able to perform different types of activities and roles, such as binding of calcium and significant activity in regulating an enzyme.^[4] The gene CALM-3 is likely to contribute to illnesses that may lead to death, such as Ventricular tachycardia which is associated with the ventricular tachycardia functioning in 2 directions and long QT syndrome which is associated with the QT interval in the electrocardiogram that is significantly longer than normal.^[4] In its structure, there are 2 helices that are observed in each of its helix-loop-helix and are then shaped into a perpendicular pattern due to the surface of the protein changing over time.^[5] Through transcription, the gene CALM-3 is able to perform the activity of a regulator for its own gene expression and has 6 exons, indicating that each exon has a specific function that takes place in the initiation stage.^[6] If there are potentially variants that could impact the calmodulin protein, it could affect the concentration of the Ca mediators that are a part of the protein.^[7]

Context

The CALM-3 gene, along with the protein of calmodulin, has been included in different types of experiments such as DNA isolation that is most common in laboratory animals such as rats. This gene can be detected in animals and humans, mainly through our genomes, and its specific polymorphisms can be found through different types of restriction enzymes.^[8] In hospital settings, a process named whole exome sequencing are used and are beneficial in determining whether CALM-3 is a cause of a certain disease.^[9] Because the protein calmodulin consists of 3 different genes, it may be difficult to determine exactly how the gene can cause a certain disease to occur and potentially worsen.^[9] However, there have been few mutations that were detected in the genes of the calmodulin protein such as in long QT syndrome.^[9]

Clinical significance

There is significant evidence that Calmodulin-3 may be associated with certain diseases, however there are few evidence that this particular gene contributes to diseases that can cause a sudden death as a result. In the lab experiment with rats, lambda rCB1 or hCE1 underwent DNA isolation as both of the genes included the CALM-3 gene, and was compared with 2 different genes that are more common among rats such as genes lambda SC4 and lambda SC8.^[8] As a result, although the lambda rCB1 or hCE1 gene may have different structures from the other genes that rats contain in their genomes, its coding strands were fairly similar.^[8] As the process of whole exome sequencing was used for patients with long QT syndrome, there was a certain criteria that had to be met in order to fully go through WES such as the patient having a stable or normal medical family history.^[9] Based on an electrocardiogram, the rhythms and waves can be detected and if irregular, it could lead to the pathway of long QT syndrome.^[9]

Related Research Articles

<span class="mw-page-title-main">Calmodulin</span> Calcium Modulated Regulatory Protein

Calmodulin (CaM) (an abbreviation for calcium-modulated protein) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. It is an intracellular target of the secondary messenger Ca²⁺, and the binding of Ca²⁺ is required for the activation of calmodulin. Once bound to Ca²⁺, calmodulin acts as part of a calcium signal transduction pathway by modifying its interactions with various target proteins such as kinases or phosphatases.

<span class="mw-page-title-main">Romano–Ward syndrome</span> Medical condition

Romano–Ward syndrome is the most common form of congenital Long QT syndrome (LQTS), a genetic heart condition that affects the electrical properties of heart muscle cells. Those affected are at risk of abnormal heart rhythms which can lead to fainting, seizures, or sudden death. Romano–Ward syndrome can be distinguished clinically from other forms of inherited LQTS as it affects only the electrical properties of the heart, while other forms of LQTS can also affect other parts of the body.

Calmodulin 1 is a protein that in humans is encoded by the CALM1 gene.

Proteasome subunit alpha type-3 also known as macropain subunit C8 and proteasome component C8 is a protein that in humans is encoded by the PSMA3 gene. This protein is one of the 17 essential subunits that contributes to the complete assembly of 20S proteasome complex.

Eukaryotic translation initiation factor 5A-1 is a protein that in humans is encoded by the EIF5A gene.

Calmodulin 2 is a protein that in humans is encoded by the CALM2 gene. A member of the calmodulin family of signaling molecules, it is an intermediary between calcium ions, which act as a second messenger, and many intracellular processes, such as the contraction of cardiac muscle.

Proteasome subunit beta type-3, also known as 20S proteasome subunit beta-3, is a protein that in humans is encoded by the PSMB3 gene. This protein is one of the 17 essential subunits that contribute to the complete assembly of the 20S proteasome complex. In particular, proteasome subunit beta type-2, along with other beta subunits, assemble into two heptameric rings and subsequently a proteolytic chamber for substrate degradation. The eukaryotic proteasome recognizes degradable proteins, including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes.

Proteasome subunit alpha type-1 is a protein that in humans is encoded by the PSMA1 gene. This protein is one of the 17 essential subunits that contributes to the complete assembly of 20S proteasome complex.

Protein S100-A1, also known as S100 calcium-binding protein A1 is a protein which in humans is encoded by the S100A1 gene. S100A1 is highly expressed in cardiac and skeletal muscle, and localizes to Z-discs and sarcoplasmic reticulum. S100A1 has shown promise as an effective candidate for gene therapy to treat post-myocardially infarcted cardiac tissue.

Plasma membrane calcium-transporting ATPase 4 is an enzyme that in humans is encoded by the ATP2B4 gene.

Proteasome subunit alpha type-2 is a protein that in humans is encoded by the PSMA2 gene. This protein is one of the 17 essential subunits that contributes to the complete assembly of 20S proteasome complex.

Proteasome subunit alpha type-5 also known as 20S proteasome subunit alpha-5 is a protein that in humans is encoded by the PSMA5 gene. This protein is one of the 17 essential subunits that contributes to the complete assembly of 20S proteasome complex.

Proteasome subunit beta type-6 also known as 20S proteasome subunit beta-1 is a protein that in humans is encoded by the PSMB6 gene.

Plasma membrane calcium-transporting ATPase 1 also known as Plasma membrane calcium pump isoform 1 is a plasma membrane Ca²⁺
ATPase, an enzyme that in humans is encoded by the ATP2B1 gene. It's a transport protein, a translocase, a calcium pump EC 7.2.2.10.

D-bifunctional protein (DBP), also known as peroxisomal multifunctional enzyme type 2 (MFP-2), as well as 17β-hydroxysteroid dehydrogenase type IV is a protein that in humans is encoded by the HSD17B4 gene. It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and steroid metabolism.

Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. AKR1A1 belongs to the aldo-keto reductase (AKR) superfamily. It catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols and catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Mutations in the AKR1A1 gene has been found associated with non-Hodgkin's lymphoma.

Calmodulin-like protein 3 is a protein that in humans is encoded by the CALML3 gene.

Alpha-mannosidase 2 is an enzyme that in humans is encoded by the MAN2A1 gene.

Neurochondrin is a protein that in humans is encoded by the NCDN gene.

Regucalcin is a protein that in humans is encoded by the RGN gene

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000160014 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "CALM3 - Calmodulin-3 - Homo sapiens (Human) - CALM3 gene & protein". www.uniprot.org. Retrieved 2022-05-18.
1 2 "CALM3 - Calmodulin-3 - Homo sapiens (Human) - CALM3 gene & protein". www.uniprot.org. Retrieved 2022-04-16.
↑ Zhang M, Yuan T (2011-01-24). "Molecular mechanisms of calmodulin's functional versatility". Biochemistry and Cell Biology. 76 (2–3): 313–323. doi:10.1139/o98-027. PMID 9923700.
↑ Koller M, Schnyder B, Strehler EE (October 1990). "Structural organization of the human CaMIII calmodulin gene". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1087 (2): 180–189. doi:10.1016/0167-4781(90)90203-E. PMID 2223880.
↑ Friedrich FW, Bausero P, Sun Y, Treszl A, Krämer E, Juhr D, et al. (July 2009). "A new polymorphism in human calmodulin III gene promoter is a potential modifier gene for familial hypertrophic cardiomyopathy". European Heart Journal. 30 (13): 1648–1655. doi: 10.1093/eurheartj/ehp153 . PMID 19429631.
1 2 3 SenGupta B, Friedberg F, Detera-Wadleigh SD (December 1987). "Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species". The Journal of Biological Chemistry. 262 (34): 16663–16670. doi: 10.1016/S0021-9258(18)49306-4 . PMID 2445749.
1 2 3 4 5 Reed GJ, Boczek NJ, Etheridge SP, Ackerman MJ (February 2015). "CALM3 mutation associated with long QT syndrome". Heart Rhythm. 12 (2): 419–422. doi:10.1016/j.hrthm.2014.10.035. PMC 4907373 . PMID 25460178.

External links

Human CALM3 genome location and CALM3 gene details page in the UCSC Genome Browser .
Overview of all the structural information available in the PDB for UniProt : P0DP23 (Calmodulin-1) at the PDBe-KB .
Overview of all the structural information available in the PDB for UniProt : P0DP24 (Calmodulin-2) at the PDBe-KB .

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000160014 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "CALM3 - Calmodulin-3 - Homo sapiens (Human) - CALM3 gene & protein". www.uniprot.org. Retrieved 2022-05-18.

[uniprot.org-4] 1 2 "CALM3 - Calmodulin-3 - Homo sapiens (Human) - CALM3 gene & protein". www.uniprot.org. Retrieved 2022-04-16.

[5] Zhang M, Yuan T (2011-01-24). "Molecular mechanisms of calmodulin's functional versatility". Biochemistry and Cell Biology. 76 (2–3): 313–323. doi:10.1139/o98-027. PMID 9923700.

[6] Koller M, Schnyder B, Strehler EE (October 1990). "Structural organization of the human CaMIII calmodulin gene". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1087 (2): 180–189. doi:10.1016/0167-4781(90)90203-E. PMID 2223880.

[7] Friedrich FW, Bausero P, Sun Y, Treszl A, Krämer E, Juhr D, et al. (July 2009). "A new polymorphism in human calmodulin III gene promoter is a potential modifier gene for familial hypertrophic cardiomyopathy". European Heart Journal. 30 (13): 1648–1655. doi: 10.1093/eurheartj/ehp153 . PMID 19429631.

[SenGupta_1987-8] 1 2 3 SenGupta B, Friedberg F, Detera-Wadleigh SD (December 1987). "Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species". The Journal of Biological Chemistry. 262 (34): 16663–16670. doi: 10.1016/S0021-9258(18)49306-4 . PMID 2445749.

[Reed_2015-9] 1 2 3 4 5 Reed GJ, Boczek NJ, Etheridge SP, Ackerman MJ (February 2015). "CALM3 mutation associated with long QT syndrome". Heart Rhythm. 12 (2): 419–422. doi:10.1016/j.hrthm.2014.10.035. PMC 4907373 . PMID 25460178.

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