Calm3 (calmodulin 3) - Rat Genome Database

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Gene: Calm3 (calmodulin 3) Rattus norvegicus
Analyze
Symbol: Calm3
Name: calmodulin 3
RGD ID: 2259
Description: Enables several functions, including nitric-oxide synthase binding activity; transmembrane transporter binding activity; and type 3 metabotropic glutamate receptor binding activity. Involved in several processes, including establishment of protein localization to mitochondrial membrane; regulation of vesicle-mediated transport; and response to corticosterone. Located in several cellular components, including chromatin; growth cone; and myelin sheath. Is active in Schaffer collateral - CA1 synapse; postsynaptic cytosol; and presynaptic cytosol. Colocalizes with mitochondrial membrane and synaptic vesicle membrane. 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
RefSeq Status: PROVISIONAL
Previously known as: calmodulin; calmodulin III; calmodulin-3; caM; Cam3; Camc; CaMIII; RNCAMIII
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Naked Mole-Rat
Black Rat
Alliance Orthologs
More Info more info ...
Latest Assembly: GRCr8 - GRCr8 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr8186,718,761 - 86,725,869 (-)NCBIGRCr8GRCr8GRCr8
GRCr8 Ensembl186,717,321 - 86,725,960 (-)EnsemblGRCr8
mRatBN7.2177,590,668 - 77,597,776 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl177,589,230 - 77,592,207 (-)EnsemblmRatBN7.2
UTH_Rnor_SHR_Utx182,970,653 - 82,977,774 (-)NCBIUTH_Rnor_SHR_UtxUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0191,534,698 - 91,541,819 (-)NCBIUTH_Rnor_SHRSP_BbbUtx_1.0UTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0184,725,742 - 84,732,863 (-)NCBIUTH_Rnor_WKY_Bbb_1.0UTH_Rnor_WKY_Bbb_1.0
Rnor_6.0178,844,520 - 78,851,628 (-)NCBIRnor_6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl178,843,080 - 78,851,719 (-)Ensemblrn6Rnor6.0
Rnor_5.0180,092,078 - 80,099,186 (-)NCBIRnor_5.0Rnor_5.0rn5
RGSC_v3.4177,245,609 - 77,252,717 (-)NCBIRGSC_v3.4RGSC_v3.4rn4
Celera172,075,982 - 72,079,075 (-)NCBICelera
RGSC_v3.1177,322,279 - 77,330,919 (-)NCBI
RH 3.4 Map1793.6RGD
Cytogenetic Map1q21NCBI
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)
1,2,4-trichloro-5-(2,5-dichlorophenyl)benzene  (ISO)
1,2-dimethylhydrazine  (ISO)
17alpha-ethynylestradiol  (ISO)
17beta-estradiol  (EXP,ISO)
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)
2,4,4'-trichlorobiphenyl  (ISO)
3,4-methylenedioxymethamphetamine  (ISO)
4,4'-sulfonyldiphenol  (ISO)
acetylsalicylic acid  (ISO)
actinomycin D  (ISO)
afimoxifene  (ISO)
amphetamine  (EXP)
antirheumatic drug  (ISO)
arsane  (EXP,ISO)
arsenic atom  (EXP,ISO)
arsenite(3-)  (ISO)
benzo[a]pyrene  (ISO)
benzo[a]pyrene diol epoxide I  (ISO)
bisphenol A  (EXP,ISO)
C60 fullerene  (EXP)
cadmium atom  (ISO)
cadmium dichloride  (ISO)
calcium dichloride  (ISO)
carbon nanotube  (ISO)
chlordecone  (ISO)
chloropicrin  (ISO)
cobalt dichloride  (ISO)
copper atom  (ISO)
copper(0)  (ISO)
coumestrol  (ISO)
cyclosporin A  (ISO)
DDE  (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)
nitrates  (ISO)
Nutlin-3  (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

Biological Process
autophagosome membrane docking  (ISO,ISS)
calcineurin-mediated signaling  (IBA,IEA,ISO)
cellular response to interferon-beta  (ISO)
cellular response to type II interferon  (ISO)
detection of calcium ion  (IBA,IEA,ISO)
establishment of protein localization to membrane  (IMP)
establishment of protein localization to mitochondrial membrane  (IEA,IMP)
G2/M transition of mitotic cell cycle  (ISO)
mitochondrion-endoplasmic reticulum membrane tethering  (ISO,ISS)
negative regulation of calcium ion export across plasma membrane  (IEA)
negative regulation of high voltage-gated calcium channel activity  (ISO,ISS)
negative regulation of ryanodine-sensitive calcium-release channel activity  (ISO,ISS)
organelle localization by membrane tethering  (ISO,ISS)
positive regulation of nitric-oxide synthase activity  (IDA)
positive regulation of receptor signaling pathway via JAK-STAT  (ISO)
presynaptic endocytosis  (IEA,ISO)
regulation of cardiac muscle cell action potential  (IEA,ISO,ISS)
regulation of cardiac muscle contraction  (IEA,ISO)
regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion  (IEA,ISO)
regulation of cell communication by electrical coupling involved in cardiac conduction  (IEA,ISO)
regulation of cytokinesis  (IEA,ISO)
regulation of heart rate  (IEA,ISO)
regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum  (IBA,IEA,ISO)
regulation of ryanodine-sensitive calcium-release channel activity  (IDA,ISO,ISS)
regulation of store-operated calcium channel activity  (IC)
regulation of synaptic vesicle endocytosis  (IEA,IMP)
regulation of synaptic vesicle exocytosis  (IEA,IMP)
response to amphetamine  (IEA,IEP)
response to calcium ion  (IEA,ISO)
substantia nigra development  (ISO)

Cellular Component

References

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. Multiple calmodulin genes exhibit systematically differential responses to chronic ethanol treatment and withdrawal in several regions of the rat brain. Vizi S, etal., Brain Res Mol Brain Res. 2000 Nov 10;83(1-2):63-71. doi: 10.1016/s0169-328x(00)00185-6.
56. 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.
57. 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.
58. 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:12032157   PMID:12223552   PMID:15294163  
PMID:15632291   PMID:16556866   PMID:16760425   PMID:17482793   PMID:17492691   PMID:20103772   PMID:20226167   PMID:20668654   PMID:21167176   PMID:21855531   PMID:22067155   PMID:22926577  
PMID:23040497   PMID:25089838   PMID:25441029   PMID:26164367   PMID:26969752   PMID:27165696   PMID:27516456   PMID:27564677   PMID:28153703   PMID:28765142  


Genomics

Comparative Map Data
Calm3
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr8186,718,761 - 86,725,869 (-)NCBIGRCr8GRCr8GRCr8
GRCr8 Ensembl186,717,321 - 86,725,960 (-)EnsemblGRCr8
mRatBN7.2177,590,668 - 77,597,776 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl177,589,230 - 77,592,207 (-)EnsemblmRatBN7.2
UTH_Rnor_SHR_Utx182,970,653 - 82,977,774 (-)NCBIUTH_Rnor_SHR_UtxUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0191,534,698 - 91,541,819 (-)NCBIUTH_Rnor_SHRSP_BbbUtx_1.0UTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0184,725,742 - 84,732,863 (-)NCBIUTH_Rnor_WKY_Bbb_1.0UTH_Rnor_WKY_Bbb_1.0
Rnor_6.0178,844,520 - 78,851,628 (-)NCBIRnor_6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl178,843,080 - 78,851,719 (-)Ensemblrn6Rnor6.0
Rnor_5.0180,092,078 - 80,099,186 (-)NCBIRnor_5.0Rnor_5.0rn5
RGSC_v3.4177,245,609 - 77,252,717 (-)NCBIRGSC_v3.4RGSC_v3.4rn4
Celera172,075,982 - 72,079,075 (-)NCBICelera
RGSC_v3.1177,322,279 - 77,330,919 (-)NCBI
RH 3.4 Map1793.6RGD
Cytogenetic Map1q21NCBI
CALM3
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh381946,601,074 - 46,610,782 (+)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl1946,601,074 - 46,610,787 (+)Ensemblhg38GRCh38
GRCh371947,104,331 - 47,114,039 (+)NCBIGRCh37GRCh37hg19GRCh37
Build 361951,796,352 - 51,805,879 (+)NCBIBuild 36Build 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
Calm3
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm39716,649,304 - 16,657,957 (-)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl716,649,304 - 16,658,039 (-)EnsemblGRCm39 EnsemblGRCm39
GRCm38716,915,379 - 16,924,032 (-)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl716,915,379 - 16,924,114 (-)Ensemblmm10GRCm38
MGSCv37717,500,728 - 17,509,381 (-)NCBIMGSCv37MGSCv37mm9NCBIm37
MGSCv36716,073,901 - 16,082,476 (-)NCBIMGSCv36mm8
Celera714,121,809 - 14,130,463 (-)NCBICelera
Cytogenetic Map7A2NCBI
cM Map79.15NCBI
Calm3
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_004955574672,300 - 680,924 (+)Ensembl
ChiLan1.0NW_004955574672,441 - 680,924 (+)NCBIChiLan1.0ChiLan1.0
CALM3
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
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 (+)EnsemblpanPan2panpan1.1
CALM3
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.11109,284,729 - 109,294,491 (-)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl1109,286,155 - 109,294,391 (-)EnsemblcanFam3CanFam3.1
Dog10K_Boxer_Tasha1108,764,035 - 108,773,479 (-)NCBIDog10K_Boxer_TashaDog10K_Boxer_Tasha
ROS_Cfam_1.01109,810,758 - 109,820,206 (-)NCBIROS_Cfam_1.0ROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl1109,763,917 - 109,820,174 (-)EnsemblROS_Cfam_1.0 Ensembl
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_1.0UU_Cfam_GSD_1.0
Calm3
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2NW_02440934918,853,317 - 18,861,294 (+)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_004936664471,440 - 480,441 (+)EnsemblSpeTri2.0 Ensembl
SpeTri2.0NW_004936664471,446 - 480,858 (+)NCBISpeTri2.0SpeTri2.0SpeTri2.0
CALM3
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 Ensembl652,506,674 - 52,516,703 (+)EnsemblsusScr11Sscrofa11.1
Sscrofa11.1652,506,979 - 52,516,704 (+)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
Sscrofa10.2647,824,454 - 47,834,181 (+)NCBISscrofa10.2Sscrofa10.2susScr3
CALM3
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.1639,957,012 - 39,966,562 (+)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl639,957,320 - 39,966,581 (+)EnsemblChlSab1.1 EnsemblchlSab2Vervet-AGM
ChlSab1.1 Ensembl2468,133,428 - 68,145,180 (+)EnsemblChlSab1.1 EnsemblchlSab2Vervet-AGM
ChlSab1.1 Ensembl1460,027,801 - 60,044,951 (+)EnsemblChlSab1.1 EnsemblchlSab2Vervet-AGM
Vero_WHO_p1.0NW_02366607319,668,290 - 19,677,858 (+)NCBIVero_WHO_p1.0Vero_WHO_p1.0
Calm3
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HetGla_female_1.0 EnsemblNW_0046248326,958,820 - 6,966,514 (-)EnsemblHetGla_female_1.0 EnsemblhetGla2HetGla_female_1.0 Ensembl
HetGla 1.0NW_0046248326,957,775 - 6,966,505 (-)NCBIHetGla 1.0HetGla 1.0hetGla2
Calm3
(Rattus rattus - black rat)
Black Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Rrattus_CSIRO_v12172,166,833 - 172,173,867 (+)NCBIRrattus_CSIRO_v1

Variants

.
Variants in Calm3
35 total Variants
miRNA Target Status (No longer updated)

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
Transcripts:ENSRNOT00000022603
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 (http://mirgate.bioinfo.cnio.es/).
For more information about miRGate, see PMID:25858286 or access the full paper here.


QTLs in Region (GRCr8)
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)14345783787558729Rat
1578649Bmd8Bone mineral density QTL 84.9femur mineral mass (VT:0010011)trabecular volumetric bone mineral density (CMO:0001729)151940904101229020Rat
634314Niddm44Non-insulin dependent diabetes mellitus QTL 44blood glucose amount (VT:0000188)blood glucose level (CMO:0000046)151941022208479811Rat
1358359Sradr1Stress Responsive Adrenal Weight QTL 14.74adrenal gland mass (VT:0010420)both adrenal glands wet weight (CMO:0000164)139728272132889942Rat
4889929Bss87Bone structure and strength QTL 876.7tibia area (VT:1000281)tibia-fibula cortical bone endosteal cross-sectional area (CMO:0001722)14630261591302615Rat
1331792Rf29Renal function QTL 294.589urine potassium amount (VT:0010539)urine potassium level (CMO:0000128)14345783787558729Rat
2313062Bmd73Bone mineral density QTL 733.90.0001tibia mineral mass (VT:1000283)compact volumetric bone mineral density (CMO:0001730)14630261591302615Rat
1578654Bss10Bone structure and strength QTL 104femur morphology trait (VT:0000559)femoral neck cortical cross-sectional area (CMO:0001702)151940904168768703Rat
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)14350995288509952Rat
1354643Foco2Food consumption QTL 27.170.0001eating behavior trait (VT:0001431)food intake rate (CMO:0000427)14212296887122968Rat
2313065Bss67Bone structure and strength QTL 673.10.0001tibia area (VT:1000281)tibia total energy absorbed before break (CMO:0001736)14630261591302615Rat
7421628Bp361Blood pressure QTL 3610.001arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)183019780128019780Rat
631495Bp96Blood pressure QTL 964.52arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)166404680111404680Rat
2313069Bss68Bone structure and strength QTL 682.90.0001tibia size trait (VT:0100001)tibia total energy absorbed before break (CMO:0001736)14630261591302615Rat
70225Bp58Blood pressure QTL 583.3arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)134184556172281316Rat
2313075Bss66Bone structure and strength QTL 663.40.0001tibia length (VT:0004357)tibia length (CMO:0000450)14630261591302615Rat
631512Scl6Serum cholesterol level QTL 69.6blood cholesterol amount (VT:0000180)serum total cholesterol level (CMO:0000363)18126986099645535Rat
2298545Neuinf8Neuroinflammation QTL 84.6nervous system integrity trait (VT:0010566)spinal cord beta-2 microglobulin mRNA level (CMO:0002125)166009857160501508Rat
10059597Bp377Blood pressure QTL 3773.420.025arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)134565911208798288Rat
1331778Rf28Renal function QTL 284.66urine potassium amount (VT:0010539)urine potassium excretion rate (CMO:0000761)14345783787558729Rat
2313077Bss69Bone structure and strength QTL 693.50.0001tibia strength trait (VT:1000284)bone polar moment of inertia (CMO:0001558)14630261591302615Rat
1302788Scl19Serum cholesterol QTL 194.60.001blood cholesterol amount (VT:0000180)plasma total cholesterol level (CMO:0000585)166400974132889942Rat
1549903Bp267Blood pressure QTL 267arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)184107164115183752Rat
2313402Anxrr24Anxiety related response QTL 24aggression-related behavior trait (VT:0015014)tameness/aggressiveness composite score (CMO:0002136)151511344153680016Rat
1331785Rf27Renal function QTL 274.643urine sodium amount (VT:0006274)urine sodium level (CMO:0000129)13070837587558729Rat
61342Bp27Blood pressure QTL 273.40.0006arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)16540563796805205Rat
4889962Bss94Bone structure and strength QTL 943.8tibia area (VT:1000281)tibia-fibula cortical bone endosteal cross-sectional area (CMO:0001722)15190920691302615Rat
1358192Ept13Estrogen-induced pituitary tumorigenesis QTL 133.4pituitary gland mass (VT:0010496)pituitary gland wet weight (CMO:0000853)186622262131622262Rat
6903308Scl36Serum cholesterol QTL 3620.0125blood cholesterol amount (VT:0000180)plasma total cholesterol level (CMO:0000585)158769992103769992Rat
2300164Bmd44Bone mineral density QTL 445.40.0001lumbar vertebra mineral mass (VT:0010511)volumetric bone mineral density (CMO:0001553)166077886111077886Rat
2313092Bmd72Bone mineral density QTL 722.50.0001tibia mineral mass (VT:1000283)total volumetric bone mineral density (CMO:0001728)14630261591302615Rat
2313097Bss70Bone structure and strength QTL 703.50.0001tibia strength trait (VT:1000284)tibia total energy absorbed before break (CMO:0001736)14630261591302615Rat
9589820Insglur3Insulin/glucose ratio QTL 310.750.001blood insulin amount (VT:0001560)calculated plasma insulin level (CMO:0002170)14350995288509952Rat
152025249Scl82Serum cholesterol level QTL 824.77blood cholesterol amount (VT:0000180)152891222109116986Rat
1354599Bw29Body weight QTL 293.460.001body mass (VT:0001259)body weight (CMO:0000012)14212296887122968Rat
4889919Bss86Bone structure and strength QTL 864.1tibia area (VT:1000281)tibia midshaft total cross-sectional area (CMO:0001715)14630261591302615Rat
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)14350995288509952Rat

Markers in Region
D1Wox12  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8186,721,172 - 86,721,319 (+)Marker Load Pipeline
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
Celera172,078,394 - 72,078,540UniSTS
RGSC_v3.1177,326,131 - 77,326,278RGD
RH 3.4 Map1791.5UniSTS
RH 3.4 Map1791.5RGD
RH 2.0 Map1511.8RGD
Cytogenetic Map1q22UniSTS
D1Arb35  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8186,721,077 - 86,721,327 (+)Marker Load Pipeline
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
Celera172,078,299 - 72,078,548UniSTS
RGSC_v3.1177,326,036 - 77,326,286RGD
FHH x ACI Map139.05RGD
FHH x ACI Map139.05UniSTS
Cytogenetic Map1q22UniSTS
D1Mgh27  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8186,726,859 - 86,727,054 (+)Marker Load Pipeline
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
Celera172,083,915 - 72,084,109UniSTS
RGSC_v3.1177,331,818 - 77,332,013RGD
RH 3.4 Map1790.5UniSTS
RH 3.4 Map1790.5RGD
Cytogenetic Map1q22UniSTS
D1Mco19  
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
Celera172,078,287 - 72,078,558UniSTS
RGSC_v3.1177,326,024 - 77,326,296RGD
Cytogenetic Map1q22UniSTS
RH128262  
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
UniSTS:141218  
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
RH137447  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8186,718,789 - 86,719,092 (+)Marker Load Pipeline
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
Calm3  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8186,722,391 - 86,722,650 (+)Marker Load Pipeline
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
MARC_7076-7077:992008234:1  
Rat AssemblyChrPosition (strand)SourceJBrowse
GRCr8186,718,770 - 86,719,111 (+)Marker Load Pipeline
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


Expression

RNA-SEQ Expression

alimentary part of gastrointestinal system
appendage
circulatory system
ectoderm
hemolymphoid system
mesenchyme
mesoderm
musculoskeletal system
nervous system
renal system
reproductive system
sensory system
visual system
7 1 18 52 67 138 95 11 51 36 32 17 17

Sequence


Ensembl Acc Id: ENSRNOT00000022603   ⟹   ENSRNOP00000022603
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8 Ensembl186,717,321 - 86,725,859 (-)Ensembl
mRatBN7.2 Ensembl177,589,230 - 77,592,207 (-)Ensembl
Rnor_6.0 Ensembl178,843,080 - 78,851,719 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000124429   ⟹   ENSRNOP00000103420
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr8 Ensembl186,717,321 - 86,725,960 (-)Ensembl
RefSeq Acc Id: NM_012518   ⟹   NP_036650
RefSeq Status: PROVISIONAL
Type: CODING
Position:
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
Sequence:
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:
Ensembl Acc Id: ENSRNOP00000022603   ⟸   ENSRNOT00000022603
Ensembl Acc Id: ENSRNOP00000103420   ⟸   ENSRNOT00000124429
Protein Domains
EF-hand

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

Transcriptome

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

Promoters
RGD ID:13689745
Promoter ID:EPDNEW_R269
Type:initiation region
Name:Calm2_1
Description:calmodulin 2
SO ACC ID:SO:0000170
Source:EPDNEW (Eukaryotic Promoter Database, http://epd.vital-it.ch/)
Experiment Methods:Single-end sequencing.
Position:
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, ENTREZGENE
Ensembl Transcript ENSRNOT00000064679.3 UniProtKB/Swiss-Prot
  ENSRNOT00000124429 ENTREZGENE
Gene3D-CATH EF-hand UniProtKB/Swiss-Prot
IMAGE_CLONE IMAGE:6890866 IMAGE-MGC_LOAD
InterPro CALM/Myosin/TropC-like UniProtKB/Swiss-Prot
  EF-hand-dom_pair UniProtKB/Swiss-Prot
  EF_Hand_1_Ca_BS UniProtKB/Swiss-Prot
  EF_hand_dom UniProtKB/Swiss-Prot
KEGG Report rno:24242 UniProtKB/Swiss-Prot
  rno:24244 UniProtKB/Swiss-Prot
  rno:50663 UniProtKB/Swiss-Prot
MGC_CLONE MGC:73021 IMAGE-MGC_LOAD
NCBI Gene 24244 ENTREZGENE
PANTHER CALMODULIN LIKE 3 UniProtKB/Swiss-Prot
  MYOSIN LIGHT CHAIN 1, 3 UniProtKB/Swiss-Prot
Pfam EF-hand_7 UniProtKB/Swiss-Prot
PhenoGen Calm3 PhenoGen
PRINTS RECOVERIN UniProtKB/Swiss-Prot
PROSITE EF_HAND_1 UniProtKB/Swiss-Prot
  EF_HAND_2 UniProtKB/Swiss-Prot
RatGTEx ENSRNOG00000004060 RatGTEx
  ENSRNOG00000016770 RatGTEx
SMART EFh UniProtKB/Swiss-Prot
Superfamily-SCOP SSF47473 UniProtKB/Swiss-Prot
TIGR TC204370
UniProt A0A8I5XV89 ENTREZGENE, UniProtKB/TrEMBL
  A6J8E1_RAT UniProtKB/TrEMBL
  A6J8E2_RAT UniProtKB/TrEMBL
  A6JEH0 ENTREZGENE, UniProtKB/TrEMBL
  CALM3_RAT UniProtKB/Swiss-Prot
  P0DP29 ENTREZGENE
  P0DP30 ENTREZGENE
  P0DP31 ENTREZGENE
  P62161 ENTREZGENE
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