Calm3 (calmodulin 3) - Rat Genome Database

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Gene: Calm3 (calmodulin 3) Rattus norvegicus
Symbol: Calm3
Name: calmodulin 3
RGD ID: 2259
Description: Enables several functions, including nitric-oxide synthase binding activity; nitric-oxide synthase regulator activity; and transmembrane transporter binding activity. Involved in establishment of protein localization to mitochondrial membrane; regulation of vesicle-mediated transport; and response to amphetamine. Located in several cellular components, including growth cone; myelin sheath; and synaptic vesicle membrane. Is active in Schaffer collateral - CA1 synapse; postsynaptic cytosol; and presynaptic cytosol. Human ortholog(s) of this gene implicated in familial hypertrophic cardiomyopathy and long QT syndrome 16. Orthologous to human CALM3 (calmodulin 3); PARTICIPATES IN adenosine monophosphate-activated protein kinase (AMPK) signaling pathway; calcium/calcium-mediated signaling pathway; calcium/calmodulin dependent kinase 2 signaling pathway; INTERACTS WITH 17beta-estradiol; 2,2,2-tetramine; 2,3,7,8-tetrachlorodibenzodioxine.
Type: protein-coding
Previously known as: calmodulin; calmodulin III; calmodulin-3; caM; Cam3; Camc; CaMIII; RNCAMIII
RGD Orthologs
Green Monkey
Naked Mole-Rat
Alliance Orthologs
More Info more info ...
Latest Assembly: mRatBN7.2 - mRatBN7.2 Assembly
Rat AssemblyChrPosition (strand)SourceGenome Browsers
GRCr8186,718,761 - 86,725,869 (-)NCBIGRCr8
mRatBN7.2177,590,668 - 77,597,776 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl177,589,230 - 77,592,207 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx182,970,653 - 82,977,774 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0191,534,698 - 91,541,819 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0184,725,742 - 84,732,863 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0178,844,520 - 78,851,628 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl178,843,080 - 78,851,719 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0180,092,078 - 80,099,186 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4177,245,609 - 77,252,717 (-)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1177,322,279 - 77,330,919 (-)NCBI
Celera172,075,982 - 72,079,075 (-)NCBICelera
RH 3.4 Map1793.6RGD
Cytogenetic Map1q21NCBI
JBrowse: View Region in Genome Browser (JBrowse)

Disease Annotations     Click to see Annotation Detail View

Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(1->4)-beta-D-glucan  (ISO)
1,2-dimethylhydrazine  (ISO)
17alpha-ethynylestradiol  (ISO)
17beta-estradiol  (EXP)
2,2',4,4',5,5'-hexachlorobiphenyl  (ISO)
2,2',4,4'-Tetrabromodiphenyl ether  (ISO)
2,2',5,5'-tetrachlorobiphenyl  (ISO)
2,2,2-tetramine  (EXP)
2,3,7,8-tetrachlorodibenzodioxine  (EXP,ISO)
2,3,7,8-Tetrachlorodibenzofuran  (EXP)
3,4-methylenedioxymethamphetamine  (ISO)
4,4'-sulfonyldiphenol  (ISO)
acetylsalicylic acid  (ISO)
afimoxifene  (ISO)
amphetamine  (EXP)
antirheumatic drug  (ISO)
arsane  (EXP)
arsenic atom  (EXP)
arsenite(3-)  (ISO)
benzo[a]pyrene  (ISO)
benzo[a]pyrene diol epoxide I  (ISO)
bisphenol A  (EXP,ISO)
C60 fullerene  (EXP)
calcium dichloride  (ISO)
carbon nanotube  (ISO)
chlordecone  (ISO)
chloropicrin  (ISO)
cobalt dichloride  (ISO)
copper atom  (ISO)
copper(0)  (ISO)
coumestrol  (ISO)
cyclosporin A  (ISO)
deguelin  (ISO)
Dibutyl phosphate  (ISO)
dibutyl phthalate  (EXP,ISO)
disulfiram  (ISO)
doxorubicin  (ISO)
elemental selenium  (ISO)
Enterolactone  (ISO)
ethanol  (EXP,ISO)
fenthion  (ISO)
finasteride  (EXP)
fluoranthene  (ISO)
flutamide  (EXP)
folic acid  (ISO)
gentamycin  (EXP)
glyphosate  (ISO)
isoprenaline  (ISO)
ivermectin  (ISO)
leflunomide  (ISO)
mechlorethamine  (ISO)
mercury atom  (ISO)
mercury(0)  (ISO)
methidathion  (ISO)
methotrexate  (ISO)
microcystin-LR  (ISO)
N-methyl-4-phenylpyridinium  (ISO)
N-nitrosodimethylamine  (EXP)
nickel atom  (ISO)
ozone  (EXP,ISO)
PCB138  (ISO)
perfluorooctane-1-sulfonic acid  (ISO)
pirinixic acid  (ISO)
rotenone  (ISO)
sarin  (ISO)
selenium atom  (ISO)
serpentine asbestos  (ISO)
sodium arsenite  (EXP,ISO)
streptozocin  (EXP)
sulindac  (EXP,ISO)
tert-butyl hydroperoxide  (ISO)
tetrachloromethane  (EXP,ISO)
thimerosal  (ISO)
thiram  (ISO)
titanium dioxide  (ISO)
trichloroethene  (EXP)
tunicamycin  (ISO)
valproic acid  (ISO)
venlafaxine hydrochloride  (EXP)
vinclozolin  (EXP)
vitamin E  (ISO)
zinc atom  (EXP)
zinc sulfate  (EXP)
zinc(0)  (EXP)

Gene Ontology Annotations     Click to see Annotation Detail View


References - curated
# Reference Title Reference Citation
1. The NMDA receptor NR1 C1 region bound to calmodulin: structural insights into functional differences between homologous domains. Ataman ZA, etal., Structure. 2007 Dec;15(12):1603-17. doi: 10.1016/j.str.2007.10.012.
2. Pathogenic NPHP5 mutations impair protein interaction with Cep290, a prerequisite for ciliogenesis. Barbelanne M, etal., Hum Mol Genet. 2013 Jun 15;22(12):2482-94. doi: 10.1093/hmg/ddt100. Epub 2013 Feb 27.
3. Gene expression pattern in PC12 cells with reduced PMCA2 or PMCA3 isoform: selective up-regulation of calmodulin and neuromodulin. Boczek T, etal., Mol Cell Biochem. 2012 Jan;360(1-2):89-102. doi: 10.1007/s11010-011-1047-3. Epub 2011 Sep 13.
4. Heme oxygenase-2 is activated by calcium-calmodulin. Boehning D, etal., J Biol Chem. 2004 Jul 23;279(30):30927-30. Epub 2004 Jun 2.
5. Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure. Brushia RJ and Walsh DA, Front Biosci. 1999 Sep 15;4:D618-41.
6. Rad GTPase deficiency leads to cardiac hypertrophy. Chang L, etal., Circulation. 2007 Dec 18;116(25):2976-83. Epub 2007 Dec 3.
7. Calmodulin: a prototypical calcium sensor. Chin D and Means AR, Trends Cell Biol. 2000 Aug;10(8):322-8.
8. Calcium signaling. Clapham DE, Cell. 2007 Dec 14;131(6):1047-58.
9. FRET-based mapping of calmodulin bound to the RyR1 Ca2+ release channel. Cornea RL, etal., Proc Natl Acad Sci U S A. 2009 Apr 14;106(15):6128-33. doi: 10.1073/pnas.0813010106. Epub 2009 Mar 30.
10. CaMKII regulation in information processing and storage. Coultrap SJ and Bayer KU, Trends Neurosci. 2012 Oct;35(10):607-18. doi: 10.1016/j.tins.2012.05.003. Epub 2012 Jun 19.
11. Phospholipase C, Ca2+, and calmodulin signaling are required for 5-HT2A receptor-mediated transamidation of Rac1 by transglutaminase. Dai Y, etal., Psychopharmacology (Berl). 2011 Feb;213(2-3):403-12. doi: 10.1007/s00213-010-1984-7. Epub 2010 Aug 18.
12. Calmodulin binds to specific sequences in the cytoplasmic domain of C-CAM and down-regulates C-CAM self-association. Edlund M, etal., J Biol Chem. 1996 Jan 19;271(3):1393-9.
13. Interaction of calmodulin with Sec61alpha limits Ca2+ leakage from the endoplasmic reticulum. Erdmann F, etal., EMBO J. 2011 Jan 5;30(1):17-31. doi: 10.1038/emboj.2010.284. Epub 2010 Nov 23.
14. Sequence homology of the 3'-untranslated region of calmodulin III in mammals. Friedberg F and Rhoads AR, Mol Biol Rep 2001 Mar;28(1):27-30.
15. A new polymorphism in human calmodulin III gene promoter is a potential modifier gene for familial hypertrophic cardiomyopathy. Friedrich FW, etal., Eur Heart J. 2009 Jul;30(13):1648-55. doi: 10.1093/eurheartj/ehp153. Epub 2009 May 8.
16. Direct detection of calmodulin tuning by ryanodine receptor channel targets using a Ca2+-sensitive acrylodan-labeled calmodulin. Fruen BR, etal., Biochemistry. 2005 Jan 11;44(1):278-84.
17. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Gaudet P, etal., Brief Bioinform. 2011 Sep;12(5):449-62. doi: 10.1093/bib/bbr042. Epub 2011 Aug 27.
18. Calcium- and calmodulin-dependent inactivation of calcium channels in inner hair cells of the rat cochlea. Grant L and Fuchs P, J Neurophysiol. 2008 May;99(5):2183-93. doi: 10.1152/jn.01174.2007. Epub 2008 Mar 5.
19. Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase. Hawley SA, etal., Cell Metab. 2005 Jul;2(1):9-19.
20. The Actin Nucleator Cobl Is Controlled by Calcium and Calmodulin. Hou W, etal., PLoS Biol. 2015 Sep 3;13(9):e1002233. doi: 10.1371/journal.pbio.1002233. eCollection 2015.
21. KEGG: Kyoto Encyclopedia of Genes and Genomes KEGG
22. Coordinated signal integration at the M-type potassium channel upon muscarinic stimulation. Kosenko A, etal., EMBO J. 2012 May 29;31(14):3147-56. doi: 10.1038/emboj.2012.156.
23. IQ-motif proteins influence intracellular free Ca2+ in hippocampal neurons through their interactions with calmodulin. Kubota Y, etal., J Neurophysiol. 2008 Jan;99(1):264-76. Epub 2007 Oct 24.
24. High-density rat radiation hybrid maps containing over 24,000 SSLPs, genes, and ESTs provide a direct link to the rat genome sequence. Kwitek AE, etal., Genome Res. 2004 Apr;14(4):750-7
25. Evidence for the direct interaction between calmodulin and the human epidermal growth factor receptor. Li H and Villalobo A, Biochem J. 2002 Mar 1;362(Pt 2):499-505.
26. A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics during endocytosis. Li H, etal., Nat Cell Biol. 2013 Jul;15(7):773-85. doi: 10.1038/ncb2791. Epub 2013 Jun 23.
27. The adaptor Grb7 is a novel calmodulin-binding protein: functional implications of the interaction of calmodulin with Grb7. Li H, etal., Oncogene. 2005 Jun 16;24(26):4206-19.
28. Crystal structure of calmodulin binding domain of orai1 in complex with Ca2+ calmodulin displays a unique binding mode. Liu Y, etal., J Biol Chem. 2012 Dec 14;287(51):43030-41. doi: 10.1074/jbc.M112.380964. Epub 2012 Oct 29.
29. Separate elements within a single IQ-like motif in adenylyl cyclase type 8 impart ca2+/calmodulin binding and autoinhibition. Macdougall DA, etal., J Biol Chem. 2009 Jun 5;284(23):15573-88. doi: 10.1074/jbc.M809585200. Epub 2009 Mar 21.
30. Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. Majava V, etal., Amino Acids. 2010 Jun;39(1):59-71. doi: 10.1007/s00726-009-0364-2. Epub 2009 Oct 24.
31. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
32. Differential regulation of calmodulin content and calmodulin messenger RNA levels by acute and repeated, intermittent amphetamine in dopaminergic terminal and midbrain areas. Michelhaugh SK and Gnegy ME, Neuroscience. 2000;98(2):275-85.
33. Acute activation of hippocampal glucocorticoid receptors results in different waves of gene expression throughout time. Morsink MC, etal., J Neuroendocrinol. 2006 Apr;18(4):239-52.
34. STIM1 and calmodulin interact with Orai1 to induce Ca2+-dependent inactivation of CRAC channels. Mullins FM, etal., Proc Natl Acad Sci U S A. 2009 Sep 8;106(36):15495-500. doi: 10.1073/pnas.0906781106. Epub 2009 Aug 21.
35. Immunocytochemical localization of calmodulin in PC12 cells and its possible interaction with histones. Natsukari N, etal., Neurochem Int. 1995 May;26(5):465-76.
36. Electronic Transfer of LocusLink and RefSeq Data NCBI rat LocusLink and RefSeq merged data July 26, 2002
37. Structural organization of multiple rat calmodulin genes. Nojima H J Mol Biol 1989 Jul 20;208(2):269-82.
38. In cardiomyocytes, binding of unzipping peptide activates ryanodine receptor 2 and reciprocally inhibits calmodulin binding. Oda T, etal., Circ Res. 2013 Feb 1;112(3):487-97. doi: 10.1161/CIRCRESAHA.111.300290. Epub 2012 Dec 11.
39. KEGG Annotation Import Pipeline Pipeline to import KEGG annotations from KEGG into RGD
40. PID Annotation Import Pipeline Pipeline to import Pathway Interaction Database annotations from NCI into RGD
41. Calmodulin-dependent gating of Ca(v)1.2 calcium channels in the absence of Ca(v)beta subunits. Ravindran A, etal., Proc Natl Acad Sci U S A. 2008 Jun 10;105(23):8154-9. doi: 10.1073/pnas.0711624105. Epub 2008 Jun 5.
42. GOA pipeline RGD automated data pipeline
43. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
44. Comprehensive gene review and curation RGD comprehensive gene curation
45. New therapeutic targets in cardiology: arrhythmias and Ca2+/calmodulin-dependent kinase II (CaMKII). Rokita AG and Anderson ME, Circulation. 2012 Oct 23;126(17):2125-39. doi: 10.1161/CIRCULATIONAHA.112.124990.
46. Interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation. Russo LC, etal., FEBS J. 2009 Aug;276(16):4358-71. doi: 10.1111/j.1742-4658.2009.07144.x. Epub 2009 Jul 15.
47. Natural intracellular peptides can modulate the interactions of mouse brain proteins and thimet oligopeptidase with 14-3-3epsilon and calmodulin. Russo LC, etal., Proteomics. 2012 Aug;12(17):2641-55. doi: 10.1002/pmic.201200032. Epub 2012 Jul 26.
48. Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin. Schumacher MA, etal., Nature. 2001 Apr 26;410(6832):1120-4.
49. Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex. Schumacher MA, etal., Structure. 2004 May;12(5):849-60.
50. Rat calmodulin cDNA. Sherbany AA, etal., DNA. 1987 Jun;6(3):267-72.
51. Dissociation of protein kinase-mediated regulation of metabotropic glutamate receptor 7 (mGluR7) interactions with calmodulin and regulation of mGluR7 function. Sorensen SD, etal., Mol Pharmacol. 2002 Jun;61(6):1303-12.
52. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Strausberg RL, etal., Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11.
53. A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism. Tejero J, etal., J Biol Chem. 2010 Aug 20;285(34):25941-9. doi: 10.1074/jbc.M110.126797. Epub 2010 Jun 7.
54. Tentative Sequence Identification Numbers Tentative Sequence Data IDs. TIGR Gene Index, Rat Data
55. Identification and characterization of wolframin, the product of the wolfram syndrome gene (WFS1), as a novel calmodulin-binding protein. Yurimoto S, etal., Biochemistry. 2009 May 12;48(18):3946-55. doi: 10.1021/bi900260y.
56. Structural basis for calmodulin as a dynamic calcium sensor. Zhang M, etal., Structure. 2012 May 9;20(5):911-23. doi: 10.1016/j.str.2012.03.019.
57. Neurogranin targets calmodulin and lowers the threshold for the induction of long-term potentiation. Zhong L and Gerges NZ, PLoS One. 2012;7(7):e41275. doi: 10.1371/journal.pone.0041275. Epub 2012 Jul 25.
Additional References at PubMed
PMID:2469574   PMID:7607248   PMID:8631777   PMID:10629061   PMID:11573098   PMID:11694536   PMID:11807546   PMID:11980920   PMID:11984006   PMID:12223552   PMID:15294163   PMID:15632291  
PMID:16556866   PMID:16760425   PMID:20103772   PMID:20226167   PMID:20668654   PMID:21167176   PMID:22067155   PMID:22926577   PMID:23040497   PMID:25089838   PMID:25441029   PMID:26164367  
PMID:26969752   PMID:27165696   PMID:27516456   PMID:27564677   PMID:28153703   PMID:28765142  


Comparative Map Data
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
GRCr8186,718,761 - 86,725,869 (-)NCBIGRCr8
mRatBN7.2177,590,668 - 77,597,776 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl177,589,230 - 77,592,207 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx182,970,653 - 82,977,774 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0191,534,698 - 91,541,819 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0184,725,742 - 84,732,863 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0178,844,520 - 78,851,628 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl178,843,080 - 78,851,719 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0180,092,078 - 80,099,186 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4177,245,609 - 77,252,717 (-)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1177,322,279 - 77,330,919 (-)NCBI
Celera172,075,982 - 72,079,075 (-)NCBICelera
RH 3.4 Map1793.6RGD
Cytogenetic Map1q21NCBI
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
GRCh381946,601,074 - 46,610,782 (+)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl1946,601,074 - 46,610,782 (+)EnsemblGRCh38hg38GRCh38
GRCh371947,104,331 - 47,114,039 (+)NCBIGRCh37GRCh37hg19GRCh37
Build 361951,796,352 - 51,805,879 (+)NCBINCBI36Build 36hg18NCBI36
Build 341951,796,351 - 51,805,878NCBI
Celera1943,908,038 - 43,917,566 (+)NCBICelera
Cytogenetic Map19q13.32NCBI
HuRef1943,529,569 - 43,539,096 (+)NCBIHuRef
CHM1_11947,106,370 - 47,115,897 (+)NCBICHM1_1
T2T-CHM13v2.01949,426,688 - 49,436,397 (+)NCBIT2T-CHM13v2.0
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
GRCm39716,649,304 - 16,657,957 (-)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl716,649,304 - 16,658,039 (-)EnsemblGRCm39 Ensembl
GRCm38716,915,379 - 16,924,032 (-)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl716,915,379 - 16,924,114 (-)EnsemblGRCm38mm10GRCm38
MGSCv37717,500,728 - 17,509,381 (-)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv36716,073,901 - 16,082,476 (-)NCBIMGSCv36mm8
Celera714,121,809 - 14,130,463 (-)NCBICelera
Cytogenetic Map7A2NCBI
cM Map79.15NCBI
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
ChiLan1.0 EnsemblNW_004955574672,300 - 680,924 (+)EnsemblChiLan1.0
ChiLan1.0NW_004955574672,441 - 680,924 (+)NCBIChiLan1.0ChiLan1.0
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
NHGRI_mPanPan1-v22052,750,443 - 52,759,973 (+)NCBINHGRI_mPanPan1-v2
NHGRI_mPanPan11954,621,264 - 54,630,788 (+)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v01943,593,069 - 43,602,550 (+)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.11952,121,687 - 52,131,135 (+)NCBIpanpan1.1PanPan1.1panPan2
PanPan1.1 Ensembl1952,121,687 - 52,131,135 (+)Ensemblpanpan1.1panPan2
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
CanFam3.11109,284,729 - 109,294,491 (-)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl1109,286,155 - 109,294,391 (-)EnsemblCanFam3.1canFam3CanFam3.1
Dog10K_Boxer_Tasha1108,764,035 - 108,773,479 (-)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.01109,810,758 - 109,820,206 (-)NCBIROS_Cfam_1.0
UMICH_Zoey_3.11109,487,893 - 109,497,333 (-)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.01109,121,990 - 109,131,419 (-)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.01109,990,749 - 110,000,195 (-)NCBIUU_Cfam_GSD_1.0
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
HiC_Itri_2NW_02440934918,853,317 - 18,861,294 (+)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_004936664471,440 - 480,441 (+)EnsemblSpeTri2.0SpeTri2.0 Ensembl
SpeTri2.0NW_004936664471,446 - 480,858 (+)NCBISpeTri2.0SpeTri2.0SpeTri2.0
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
Sscrofa11.1 Ensembl652,506,674 - 52,516,703 (+)EnsemblSscrofa11.1susScr11Sscrofa11.1
Sscrofa11.1652,506,979 - 52,516,704 (+)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
Sscrofa10.2647,824,454 - 47,834,181 (+)NCBISscrofa10.2Sscrofa10.2susScr3
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
ChlSab1.1639,957,012 - 39,966,562 (+)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl639,957,320 - 39,966,581 (+)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
ChlSab1.1 Ensembl2468,133,428 - 68,145,180 (+)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
ChlSab1.1 Ensembl1460,027,801 - 60,044,951 (+)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_02366607319,668,290 - 19,677,858 (+)NCBIVero_WHO_p1.0Vero_WHO_p1.0
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
HetGla_female_1.0 EnsemblNW_0046248326,958,820 - 6,966,514 (-)EnsemblHetGla_female_1.0HetGla_female_1.0 EnsemblhetGla2
HetGla 1.0NW_0046248326,957,775 - 6,966,505 (-)NCBIHetGla_female_1.0HetGla 1.0hetGla2


Variants in Calm3
15 total Variants
miRNA Target Status

Confirmed Target Of
miRNA GeneMature miRNAMethod NameResult TypeData TypeSupport TypePMID
Mir1rno-miR-1-3pMirtarbaseexternal_infoqRT-PCRFunctional MTI (Weak)19188439

Predicted Target Of
Summary Value
Count of predictions:340
Count of miRNA genes:186
Interacting mature miRNAs:212
Prediction methods:Microtar, Miranda, Rnahybrid, Targetscan
Result types:miRGate_prediction

The detailed report is available here: Full Report CSV TAB Printer

miRNA Target Status data imported from miRGate (
For more information about miRGate, see PMID:25858286 or access the full paper here.

QTLs in Region (mRatBN7.2)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
1331732Srn4Serum renin concentration QTL 44.467renin activity (VT:0005581)plasma renin activity level (CMO:0000116)13523959878430678Rat
2313059Bss55Bone structure and strength QTL 553.20.0001tibia size trait (VT:0100001)tibia midshaft cross-sectional area (CMO:0001717)143284731118944897Rat
631688Hcas2Hepatocarcinoma susceptibility QTL 230.0001liver integrity trait (VT:0010547)liver tumorous lesion number (CMO:0001068)15925874115540829Rat
1578649Bmd8Bone mineral density QTL 84.9femur mineral mass (VT:0010011)trabecular volumetric bone mineral density (CMO:0001729)14939317294393172Rat
1358359Sradr1Stress Responsive Adrenal Weight QTL 14.74adrenal gland mass (VT:0010420)both adrenal glands wet weight (CMO:0000164)130882023123479925Rat
634314Niddm44Non-insulin dependent diabetes mellitus QTL 44blood glucose amount (VT:0000188)blood glucose level (CMO:0000046)149393289199050459Rat
4889929Bss87Bone structure and strength QTL 876.7tibia area (VT:1000281)tibia-fibula cortical bone endosteal cross-sectional area (CMO:0001722)15389511782174945Rat
1331792Rf29Renal function QTL 294.589urine potassium amount (VT:0010539)urine potassium level (CMO:0000128)13523959878430678Rat
2313062Bmd73Bone mineral density QTL 733.90.0001tibia mineral mass (VT:1000283)compact volumetric bone mineral density (CMO:0001730)11148131282174945Rat
8552900Pigfal1Plasma insulin-like growth factor 1 level QTL 17.4blood insulin-like growth factor amount (VT:0010479)plasma insulin-like growth factor 1 level (CMO:0001299)13483685879836858Rat
1578654Bss10Bone structure and strength QTL 104femur morphology trait (VT:0000559)femoral neck cortical cross-sectional area (CMO:0001702)149393172159356837Rat
1554320Bmd1Bone mineral density QTL 112.20.0001femur mineral mass (VT:0010011)volumetric bone mineral density (CMO:0001553)150910886060548Rat
1354643Foco2Food consumption QTL 27.170.0001eating behavior trait (VT:0001431)food intake rate (CMO:0000427)13344984878449848Rat
2302059Pia36Pristane induced arthritis QTL 363.80.001blood immunoglobulin amount (VT:0002460)serum immunoglobulin G1 level (CMO:0002115)14333300288333002Rat
2313065Bss67Bone structure and strength QTL 673.10.0001tibia area (VT:1000281)tibia total energy absorbed before break (CMO:0001736)11148131282174945Rat
1300121Hrtrt1Heart rate QTL 13.7heart pumping trait (VT:2000009)heart rate (CMO:0000002)165789093115540829Rat
7421628Bp361Blood pressure QTL 3610.001arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)166023617118608521Rat
2313069Bss68Bone structure and strength QTL 682.90.0001tibia size trait (VT:0100001)tibia total energy absorbed before break (CMO:0001736)11148131282174945Rat
631495Bp96Blood pressure QTL 964.52arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)122340647102268831Rat
2313075Bss66Bone structure and strength QTL 663.40.0001tibia length (VT:0004357)tibia length (CMO:0000450)11148131282174945Rat
70225Bp58Blood pressure QTL 583.3arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)132356093162846471Rat
631512Scl6Serum cholesterol level QTL 69.6blood cholesterol amount (VT:0000180)serum total cholesterol level (CMO:0000363)17219768090508767Rat
2298545Neuinf8Neuroinflammation QTL 84.6nervous system integrity trait (VT:0010566)spinal cord beta-2 microglobulin mRNA level (CMO:0002125)157336763151090257Rat
2313072Bss53Bone structure and strength QTL 534.30.0001tibia length (VT:0004357)tibia length (CMO:0000450)143284731118944897Rat
10059597Bp377Blood pressure QTL 3773.420.025arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)132737458199368955Rat
2313078Bss54Bone structure and strength QTL 543.50.0001tibia area (VT:1000281)tibia midshaft cross-sectional area (CMO:0001717)143284731118944897Rat
2313077Bss69Bone structure and strength QTL 693.50.0001tibia strength trait (VT:1000284)bone polar moment of inertia (CMO:0001558)11148131282174945Rat
1331778Rf28Renal function QTL 284.66urine potassium amount (VT:0010539)urine potassium excretion rate (CMO:0000761)14580314078430678Rat
2313402Anxrr24Anxiety related response QTL 24aggression-related behavior trait (VT:0015014)tameness/aggressiveness composite score (CMO:0002136)148963584144267916Rat
1331785Rf27Renal function QTL 274.643urine sodium amount (VT:0006274)urine sodium level (CMO:0000129)12887978078430678Rat
61342Bp27Blood pressure QTL 273.40.0006arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)15673266898773277Rat
1300172Bp172Blood pressure QTL 1723.56arterial blood pressure trait (VT:2000000)diastolic blood pressure (CMO:0000005)13273727390665040Rat
4889962Bss94Bone structure and strength QTL 943.8tibia area (VT:1000281)tibia-fibula cortical bone endosteal cross-sectional area (CMO:0001722)14936146582174945Rat
1358192Ept13Estrogen-induced pituitary tumorigenesis QTL 133.4pituitary gland mass (VT:0010496)pituitary gland wet weight (CMO:0000853)177494165122494165Rat
2313094Bss58Bone structure and strength QTL 583.70.0001tibia strength trait (VT:1000284)tibia total energy absorbed before break (CMO:0001736)143284731118944897Rat
6903308Scl36Serum cholesterol QTL 3620.0125blood cholesterol amount (VT:0000180)plasma total cholesterol level (CMO:0000585)15386304190532583Rat
2313092Bmd72Bone mineral density QTL 722.50.0001tibia mineral mass (VT:1000283)total volumetric bone mineral density (CMO:0001728)11148131282174945Rat
2300164Bmd44Bone mineral density QTL 445.40.0001lumbar vertebra mineral mass (VT:0010511)volumetric bone mineral density (CMO:0001553)156949932101949932Rat
2313099Bss56Bone structure and strength QTL 562.40.0001tibia size trait (VT:0100001)tibia midshaft endosteal cross-sectional area (CMO:0001716)143284731118944897Rat
2313098Bmd70Bone mineral density QTL 703.60.0001tibia mineral mass (VT:1000283)compact volumetric bone mineral density (CMO:0001730)143284731118944897Rat
2313097Bss70Bone structure and strength QTL 703.50.0001tibia strength trait (VT:1000284)tibia total energy absorbed before break (CMO:0001736)11148131282174945Rat
9589820Insglur3Insulin/glucose ratio QTL 310.750.001blood insulin amount (VT:0001560)calculated plasma insulin level (CMO:0002170)13483685879836858Rat
1354599Bw29Body weight QTL 293.460.001body mass (VT:0001259)body weight (CMO:0000012)13344984878449848Rat
4889919Bss86Bone structure and strength QTL 864.1tibia area (VT:1000281)tibia midshaft total cross-sectional area (CMO:0001715)15389511782174945Rat
8552948Pigfal11Plasma insulin-like growth factor 1 level QTL 114.7blood insulin-like growth factor amount (VT:0010479)plasma insulin-like growth factor 1 level (CMO:0001299)13483685879836858Rat
2313051Bss57Bone structure and strength QTL 573.70.0001tibia strength trait (VT:1000284)bone polar moment of inertia (CMO:0001558)143284731118944897Rat

Markers in Region
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2177,593,079 - 77,593,226 (+)MAPPERmRatBN7.2
Rnor_6.0178,846,932 - 78,847,078NCBIRnor6.0
Rnor_5.0180,094,490 - 80,094,636UniSTSRnor5.0
RGSC_v3.4177,248,020 - 77,248,167RGDRGSC3.4
RGSC_v3.4177,248,021 - 77,248,167UniSTSRGSC3.4
RGSC_v3.1177,326,131 - 77,326,278RGD
Celera172,078,394 - 72,078,540UniSTS
RH 3.4 Map1791.5UniSTS
RH 3.4 Map1791.5RGD
RH 2.0 Map1511.8RGD
Cytogenetic Map1q22UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2177,592,984 - 77,593,234 (+)MAPPERmRatBN7.2
Rnor_6.0178,846,837 - 78,847,086NCBIRnor6.0
Rnor_5.0180,094,395 - 80,094,644UniSTSRnor5.0
RGSC_v3.4177,247,925 - 77,248,175RGDRGSC3.4
RGSC_v3.4177,247,926 - 77,248,175UniSTSRGSC3.4
RGSC_v3.1177,326,036 - 77,326,286RGD
Celera172,078,299 - 72,078,548UniSTS
FHH x ACI Map139.05UniSTS
FHH x ACI Map139.05RGD
Cytogenetic Map1q22UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2177,598,766 - 77,598,961 (+)MAPPERmRatBN7.2
Rnor_6.0178,852,619 - 78,852,813NCBIRnor6.0
Rnor_5.0180,100,177 - 80,100,371UniSTSRnor5.0
RGSC_v3.4177,253,707 - 77,253,902RGDRGSC3.4
RGSC_v3.4177,253,708 - 77,253,902UniSTSRGSC3.4
RGSC_v3.1177,331,818 - 77,332,013RGD
Celera172,083,915 - 72,084,109UniSTS
RH 3.4 Map1790.5RGD
RH 3.4 Map1790.5UniSTS
Cytogenetic Map1q22UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2177,592,972 - 77,593,244 (+)MAPPERmRatBN7.2
Rnor_6.0178,846,825 - 78,847,096NCBIRnor6.0
Rnor_5.0180,094,383 - 80,094,654UniSTSRnor5.0
RGSC_v3.4177,247,913 - 77,248,185RGDRGSC3.4
RGSC_v3.4177,247,914 - 77,248,185UniSTSRGSC3.4
RGSC_v3.1177,326,024 - 77,326,296RGD
Celera172,078,287 - 72,078,558UniSTS
Cytogenetic Map1q22UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.25102,623,675 - 102,623,875 (+)MAPPERmRatBN7.2
mRatBN7.2177,589,281 - 77,589,472 (+)MAPPERmRatBN7.2
Rnor_6.0178,843,134 - 78,843,324NCBIRnor6.0
Rnor_6.05106,467,083 - 106,467,282NCBIRnor6.0
Rnor_5.0180,090,692 - 80,090,882UniSTSRnor5.0
Rnor_5.05110,448,523 - 110,448,722UniSTSRnor5.0
RGSC_v3.4177,244,223 - 77,244,413UniSTSRGSC3.4
Celera5100,486,767 - 100,486,966UniSTS
Celera172,074,596 - 72,074,786UniSTS
Cytogenetic Map5q32UniSTS
Cytogenetic Map1q22UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.25102,623,667 - 102,623,851 (+)MAPPERmRatBN7.2
mRatBN7.2177,589,273 - 77,589,448 (+)MAPPERmRatBN7.2
Rnor_6.0178,843,126 - 78,843,300NCBIRnor6.0
Rnor_6.05106,467,075 - 106,467,258NCBIRnor6.0
Rnor_5.0180,090,684 - 80,090,858UniSTSRnor5.0
Rnor_5.05110,448,515 - 110,448,698UniSTSRnor5.0
RGSC_v3.4177,244,215 - 77,244,389UniSTSRGSC3.4
Celera5100,486,791 - 100,486,974UniSTS
Celera172,074,588 - 72,074,762UniSTS
Cytogenetic Map5q32UniSTS
Cytogenetic Map1q22UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2177,590,696 - 77,590,999 (+)MAPPERmRatBN7.2
Rnor_6.0178,844,549 - 78,844,851NCBIRnor6.0
Rnor_5.0180,092,107 - 80,092,409UniSTSRnor5.0
RGSC_v3.4177,245,638 - 77,245,940UniSTSRGSC3.4
Celera172,076,011 - 72,076,313UniSTS
Cytogenetic Map1q22UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2177,594,298 - 77,594,557 (+)MAPPERmRatBN7.2
Rnor_6.0178,848,151 - 78,848,409NCBIRnor6.0
Rnor_5.0180,095,709 - 80,095,967UniSTSRnor5.0
RGSC_v3.4177,249,240 - 77,249,498UniSTSRGSC3.4
Celera172,079,613 - 72,079,871UniSTS
RH 3.4 Map1793.6UniSTS
Cytogenetic Map1q22UniSTS
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2177,590,677 - 77,591,018 (+)MAPPERmRatBN7.2
Rnor_6.0178,844,530 - 78,844,870NCBIRnor6.0
Rnor_5.0180,092,088 - 80,092,428UniSTSRnor5.0
RGSC_v3.4177,245,619 - 77,245,959UniSTSRGSC3.4
Celera172,075,992 - 72,076,332UniSTS
Cytogenetic Map1q22UniSTS



RefSeq Acc Id: ENSRNOT00000022603   ⟹   ENSRNOP00000022603
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl177,589,230 - 77,592,207 (-)Ensembl
Rnor_6.0 Ensembl178,843,080 - 78,851,719 (-)Ensembl
RefSeq Acc Id: NM_012518   ⟹   NP_036650
Rat AssemblyChrPosition (strand)Source
GRCr8186,718,761 - 86,725,869 (-)NCBI
mRatBN7.2177,590,668 - 77,597,776 (-)NCBI
Rnor_6.0178,844,520 - 78,851,628 (-)NCBI
Rnor_5.0180,092,078 - 80,099,186 (-)NCBI
RGSC_v3.4177,245,609 - 77,252,717 (-)RGD
Celera172,075,982 - 72,079,075 (-)RGD
RefSeq Acc Id: NP_036650   ⟸   NM_012518
- UniProtKB: P62161 (UniProtKB/Swiss-Prot),   P0DP31 (UniProtKB/Swiss-Prot),   P0DP30 (UniProtKB/Swiss-Prot),   P0DP29 (UniProtKB/Swiss-Prot),   A6JEH0 (UniProtKB/TrEMBL),   A0A8I5XV89 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: ENSRNOP00000022603   ⟸   ENSRNOT00000022603
Protein Domains

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-P0DP29-F1-model_v2 AlphaFold P0DP29 1-149 view protein structure
AF-P0DP30-F1-model_v2 AlphaFold P0DP30 1-149 view protein structure
AF-P0DP31-F1-model_v2 AlphaFold P0DP31 1-149 view protein structure


eQTL   View at Phenogen
WGCNA   View at Phenogen
Tissue/Strain Expression   View at Phenogen

RGD ID:13689745
Promoter ID:EPDNEW_R269
Type:initiation region
Description:calmodulin 2
SO ACC ID:SO:0000170
Source:EPDNEW (Eukaryotic Promoter Database,
Experiment Methods:Single-end sequencing.
Rat AssemblyChrPosition (strand)Source
Rnor_6.0178,851,694 - 78,851,754EPDNEW

Additional Information

Database Acc Id Source(s)
AGR Gene RGD:2259 AgrOrtholog
BioCyc Gene G2FUF-60587 BioCyc
Ensembl Genes ENSRNOG00000004060 UniProtKB/Swiss-Prot
  ENSRNOG00000016770 Ensembl
  ENSRNOG00000067086 UniProtKB/TrEMBL
  ENSRNOG00055015152 UniProtKB/Swiss-Prot
  ENSRNOG00055031474 UniProtKB/Swiss-Prot
  ENSRNOG00060022413 UniProtKB/Swiss-Prot
  ENSRNOG00065014668 UniProtKB/Swiss-Prot
  ENSRNOG00065032582 UniProtKB/Swiss-Prot
Ensembl Transcript ENSRNOT00000064679.3 UniProtKB/Swiss-Prot
  ENSRNOT00000118114.1 UniProtKB/TrEMBL
  ENSRNOT00055025979 UniProtKB/Swiss-Prot
  ENSRNOT00055054523 UniProtKB/Swiss-Prot
  ENSRNOT00060038843 UniProtKB/Swiss-Prot
  ENSRNOT00065024262 UniProtKB/Swiss-Prot
  ENSRNOT00065056044 UniProtKB/Swiss-Prot
Gene3D-CATH EF-hand UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
InterPro EF-hand-dom_pair UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EF_Hand_1_Ca_BS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EF_hand_dom UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
KEGG Report rno:24242 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  rno:24244 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  rno:50663 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Pfam EF-hand_1 UniProtKB/TrEMBL
  EF-hand_7 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PhenoGen Calm3 PhenoGen
PROSITE EF_HAND_1 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EF_HAND_2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
RatGTEx ENSRNOG00000004060 RatGTEx
  ENSRNOG00000016770 RatGTEx
  ENSRNOG00000067086 RatGTEx
  ENSRNOG00055015152 RatGTEx
  ENSRNOG00055031474 RatGTEx
  ENSRNOG00060022413 RatGTEx
  ENSRNOG00065014668 RatGTEx
  ENSRNOG00065032582 RatGTEx
SMART EFh UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Superfamily-SCOP EF-hand UniProtKB/TrEMBL, UniProtKB/Swiss-Prot
TIGR TC204370
  CALM1_RAT UniProtKB/Swiss-Prot
  CALM2_RAT UniProtKB/Swiss-Prot
  CALM3_RAT UniProtKB/Swiss-Prot
UniProt Secondary P02593 UniProtKB/Swiss-Prot
  P62161 UniProtKB/Swiss-Prot
  P70667 UniProtKB/Swiss-Prot
  P99014 UniProtKB/Swiss-Prot
  Q61379 UniProtKB/Swiss-Prot
  Q61380 UniProtKB/Swiss-Prot

Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2002-11-06 Calm3  calmodulin 3    Calmodulin III  Name updated 625702 APPROVED
2002-06-10 Calm3  Calmodulin III      Symbol and Name status set to approved 70586 APPROVED

RGD Curation Notes
Note Type Note Reference
gene_expression expressed mainly in skeletal muscle and brain 634687
gene_protein 2.2 and 0.75 kb mRNA 634686