CALM1_MOUSE
ID CALM1_MOUSE Reviewed; 149 AA.
AC P0DP26; P02593; P62204; P70667; P99014; Q3TEH7; Q3THK5; Q3U6Z5; Q3U7C7;
AC Q498A3; Q61379; Q61380; Q8BNC9; Q91VQ9; Q9D6G4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Calmodulin-1 {ECO:0000250|UniProtKB:P0DP23};
GN Name=Calm1 {ECO:0000312|MGI:MGI:88251}; Synonyms=Calm, Cam, Cam1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3384819; DOI=10.1016/s0021-9258(19)81579-x;
RA Bender P.K., Dedman J.R., Emerson C.P. Jr.;
RT "The abundance of calmodulin mRNAs is regulated in phosphorylase kinase-
RT deficient skeletal muscle.";
RL J. Biol. Chem. 263:9733-9737(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA Kato K.;
RT "A collection of cDNA clones with specific expression patterns in mouse
RT brain.";
RL Eur. J. Neurosci. 2:704-711(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Amnion, Bone marrow, Colon, Hippocampus, Kidney, Liver, Lung,
RC Mammary gland, Ovary, Placenta, Stomach, Testis, Thymus, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, C57BL/6J, and Czech II;
RC TISSUE=Brain, Mammary tumor, Placenta, and Spinal ganglion;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP INTERACTION WITH GIMAP4.
RX PubMed=16569770; DOI=10.1182/blood-2005-11-4616;
RA Schnell S., Demolliere C., van den Berk P., Jacobs H.;
RT "Gimap4 accelerates T-cell death.";
RL Blood 108:591-599(2006).
RN [8]
RP INTERACTION WITH RYR1 AND RYR2.
RX PubMed=18650434; DOI=10.1074/jbc.m804432200;
RA Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F.,
RA Weber D.J.;
RT "S100A1 and calmodulin compete for the same binding site on ryanodine
RT receptor.";
RL J. Biol. Chem. 283:26676-26683(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND SER-102, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP INTERACTION WITH IQCF1.
RX PubMed=25380116; DOI=10.1111/andr.296;
RA Fang P., Xu W., Li D., Zhao X., Dai J., Wang Z., Yan X., Qin M., Zhang Y.,
RA Xu C., Wang L., Qiao Z.;
RT "A novel acrosomal protein, IQCF1, involved in sperm capacitation and the
RT acrosome reaction.";
RL Andrology 3:332-344(2015).
RN [13]
RP INTERACTION WITH SYT7.
RX PubMed=24569478; DOI=10.7554/elife.01524;
RA Liu H., Bai H., Hui E., Yang L., Evans C.S., Wang Z., Kwon S.E.,
RA Chapman E.R.;
RT "Synaptotagmin 7 functions as a Ca2+-sensor for synaptic vesicle
RT replenishment.";
RL Elife 3:E01524-E01524(2014).
RN [14]
RP INTERACTION WITH HINT1 AND HINT3.
RX PubMed=31088288; DOI=10.1089/ars.2019.7724;
RA Cortes-Montero E., Rodriguez-Munoz M., Sanchez-Blazquez P., Garzon J.;
RT "The Axonal Motor Neuropathy-Related HINT1 Protein Is a Zinc- and
RT Calmodulin-Regulated Cysteine SUMO Protease.";
RL Antioxid. Redox Signal. 31:503-520(2019).
RN [15]
RP INTERACTION WITH GARIN2, AND SUBCELLULAR LOCATION.
RX PubMed=29025071; DOI=10.1093/humrep/dex290;
RA Ma Q., Li Y., Luo M., Guo H., Lin S., Chen J., Du Y., Jiang Z., Gui Y.;
RT "The expression characteristics of FAM71D and its association with sperm
RT motility.";
RL Hum. Reprod. 32:2178-2187(2017).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-147 IN COMPLEX WITH MYO5A.
RX PubMed=17151196; DOI=10.1073/pnas.0609436103;
RA Houdusse A., Gaucher J.F., Krementsova E., Mui S., Trybus K.M., Cohen C.;
RT "Crystal structure of apo-calmodulin bound to the first two IQ motifs of
RT myosin V reveals essential recognition features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19326-19331(2006).
RN [17] {ECO:0007744|PDB:3WFN}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1893-1914 IN COMPLEX WITH SCN8A,
RP INTERACTION WITH SCN8A, AND MUTAGENESIS OF GLU-115; GLU-121; GLU-124 AND
RP GLU-128.
RX PubMed=23942337; DOI=10.1038/srep02435;
RA Reddy Chichili V.P., Xiao Y., Seetharaman J., Cummins T.R., Sivaraman J.;
RT "Structural basis for the modulation of the neuronal voltage-gated sodium
RT channel NaV1.6 by calmodulin.";
RL Sci. Rep. 3:2435-2435(2013).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels, aquaporins and other proteins through calcium-binding.
CC Among the enzymes to be stimulated by the calmodulin-calcium complex
CC are a number of protein kinases and phosphatases. Together with CCP110
CC and centrin, is involved in a genetic pathway that regulates the
CC centrosome cycle and progression through cytokinesis. Is a regulator of
CC voltage-dependent L-type calcium channels. Mediates calcium-dependent
CC inactivation of CACNA1C. Positively regulates calcium-activated
CC potassium channel activity of KCNN2. Forms a potassium channel complex
CC with KCNQ1 and regulates electrophysiological activity of the channel
CC via calcium-binding. Acts as a sensor to modulate the endoplasmic
CC reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By
CC similarity). {ECO:0000250|UniProtKB:P0DP23}.
CC -!- SUBUNIT: Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY.
CC Interacts with MYO10. Interacts with RRAD (By similarity). Interacts
CC with USP6; the interaction is calcium dependent (By similarity).
CC Interacts with CDK5RAP2. Interacts with SCN5A (By similarity).
CC Interacts with FCHO1. Interacts with MIP in a 1:2 stoichiometry; the
CC interaction with the cytoplasmic domains from two MIP subunits promotes
CC MIP water channel closure. Interacts with ORAI1; this may play a role
CC in the regulation of ORAI1-mediated calcium transport (By similarity).
CC Interacts with RYR1 (PubMed:18650434). Interacts with MYO5A
CC (PubMed:17151196). Interacts with IQCF1 (PubMed:25380116). Interacts
CC with SYT7 (PubMed:24569478). Interacts with CEACAM1 (via cytoplasmic
CC domain); this interaction is in a calcium dependent manner and reduces
CC homophilic cell adhesion through dissociation of dimer (By similarity).
CC Interacts with RYR2; regulates RYR2 calcium-release channel activity
CC (PubMed:18650434). Interacts with PCP4; regulates calmodulin calcium-
CC binding (By similarity). Interacts with the heterotetrameric KCNQ2 and
CC KCNQ3 channel; the interaction is calcium-independent, constitutive and
CC participates in the proper assembly of a functional heterotetrameric M
CC channel (By similarity). Interacts with alpha-synuclein/SNCA (By
CC similarity). Interacts with SLC9A1 in a calcium-dependent manner (By
CC similarity). In the absence of Ca(+2), interacts with GIMAP4 (via IQ
CC domain) (PubMed:16569770). Interacts with SCN8A; the interaction
CC modulates the inactivation rate of SCN8A (PubMed:23942337). Interaction
CC with KIF1A; the interaction is increased in presence of calcium and
CC increases neuronal dense core vesicles motility (By similarity).
CC Interacts with KCNN3 (By similarity). Interacts with KCNQ1 (via C-
CC terminus); forms a heterooctameric structure (with 4:4 KCNQ1:CALM
CC stoichiometry) in a calcium-independent manner (By similarity).
CC Interacts with PIK3C3; the interaction modulates PIK3C3 kinase activity
CC (By similarity). Interacts with HINT1; interaction increases in the
CC presence of calcium ions (PubMed:31088288). Interacts with HINT3
CC (PubMed:31088288). Interacts with GARIN2; in mature sperm flagella
CC (PubMed:29025071). {ECO:0000250, ECO:0000250|UniProtKB:P0DP23,
CC ECO:0000250|UniProtKB:P62161, ECO:0000269|PubMed:16569770,
CC ECO:0000269|PubMed:17151196, ECO:0000269|PubMed:18650434,
CC ECO:0000269|PubMed:23942337, ECO:0000269|PubMed:24569478,
CC ECO:0000269|PubMed:25380116, ECO:0000269|PubMed:29025071,
CC ECO:0000269|PubMed:31088288}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P0DP23}. Cell
CC projection, cilium, flagellum {ECO:0000269|PubMed:29025071}.
CC Note=Distributed throughout the cell during interphase, but during
CC mitosis becomes dramatically localized to the spindle poles and the
CC spindle microtubules. {ECO:0000250|UniProtKB:P0DP23}.
CC -!- DOMAIN: The N-terminal and C-terminal lobes of CALM bind to the C-
CC terminus of KCNQ1 in a clamp-like conformation. Binding of CALM C-
CC terminus to KCNQ1 is calcium-independent but is essential for assembly
CC of the structure. Binding of CALM N-terminus to KCNQ1 is calcium-
CC dependent and regulates electrophysiological activity of the channel.
CC {ECO:0000250|UniProtKB:P0DP23}.
CC -!- PTM: Ubiquitination results in a strongly decreased activity.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation results in a decreased activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC {ECO:0000250|UniProtKB:P0DP23}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; M19381; AAA66182.1; -; mRNA.
DR EMBL; X61432; CAA43674.1; -; mRNA.
DR EMBL; AK004673; BAB23462.1; -; mRNA.
DR EMBL; AK013695; BAB28959.1; -; mRNA.
DR EMBL; AK088141; BAC40168.1; -; mRNA.
DR EMBL; AK150288; BAE29443.1; -; mRNA.
DR EMBL; AK150978; BAE30007.1; -; mRNA.
DR EMBL; AK151001; BAE30025.1; -; mRNA.
DR EMBL; AK151552; BAE30497.1; -; mRNA.
DR EMBL; AK151784; BAE30686.1; -; mRNA.
DR EMBL; AK151923; BAE30801.1; -; mRNA.
DR EMBL; AK151992; BAE30856.1; -; mRNA.
DR EMBL; AK152148; BAE30984.1; -; mRNA.
DR EMBL; AK152715; BAE31439.1; -; mRNA.
DR EMBL; AK152719; BAE31442.1; -; mRNA.
DR EMBL; AK152850; BAE31543.1; -; mRNA.
DR EMBL; AK152897; BAE31579.1; -; mRNA.
DR EMBL; AK153004; BAE31644.1; -; mRNA.
DR EMBL; AK153348; BAE31924.1; -; mRNA.
DR EMBL; AK153426; BAE31985.1; -; mRNA.
DR EMBL; AK153546; BAE32083.1; -; mRNA.
DR EMBL; AK159762; BAE35353.1; -; mRNA.
DR EMBL; AK160057; BAE35595.1; -; mRNA.
DR EMBL; AK160508; BAE35832.1; -; mRNA.
DR EMBL; AK161302; BAE36309.1; -; mRNA.
DR EMBL; AK162314; BAE36849.1; -; mRNA.
DR EMBL; AK166308; BAE38695.1; -; mRNA.
DR EMBL; AK167353; BAE39452.1; -; mRNA.
DR EMBL; AK168002; BAE39990.1; -; mRNA.
DR EMBL; AK168241; BAE40191.1; -; mRNA.
DR EMBL; AK168663; BAE40516.1; -; mRNA.
DR EMBL; AK168803; BAE40633.1; -; mRNA.
DR EMBL; AK169027; BAE40819.1; -; mRNA.
DR EMBL; AK169055; BAE40843.1; -; mRNA.
DR EMBL; AK169640; BAE41271.1; -; mRNA.
DR EMBL; BC054805; AAH54805.1; -; mRNA.
DR CCDS; CCDS36523.1; -.
DR PIR; I49567; I49567.
DR RefSeq; NP_001300863.1; NM_001313934.1.
DR RefSeq; NP_031615.1; NM_007589.5.
DR RefSeq; NP_031616.1; NM_007590.3.
DR RefSeq; NP_033920.1; NM_009790.5.
DR PDB; 1UP5; X-ray; 1.90 A; A/B=2-149.
DR PDB; 2DFS; EM; 24.00 A; B/C/D/E/F/G/N/O/P/Q/R/S=2-149.
DR PDB; 2IX7; X-ray; 2.50 A; A/B=3-147.
DR PDB; 3WFN; X-ray; 1.95 A; B/C/D/E=1-149.
DR PDB; 4E50; X-ray; 2.70 A; A=1-149.
DR PDB; 4E53; X-ray; 2.69 A; A/B=1-149.
DR PDB; 4HEX; X-ray; 2.00 A; A/B=1-149.
DR PDB; 4ZLK; X-ray; 2.50 A; B=1-149.
DR PDB; 7B1G; EM; 3.60 A; E=1-149.
DR PDB; 7CQP; X-ray; 1.90 A; B=1-78.
DR PDBsum; 1UP5; -.
DR PDBsum; 2DFS; -.
DR PDBsum; 2IX7; -.
DR PDBsum; 3WFN; -.
DR PDBsum; 4E50; -.
DR PDBsum; 4E53; -.
DR PDBsum; 4HEX; -.
DR PDBsum; 4ZLK; -.
DR PDBsum; 7B1G; -.
DR PDBsum; 7CQP; -.
DR AlphaFoldDB; P0DP26; -.
DR SMR; P0DP26; -.
DR STRING; 10090.ENSMUSP00000019514; -.
DR ChEMBL; CHEMBL3562176; -.
DR iPTMnet; P0DP26; -.
DR MetOSite; P0DP26; -.
DR PhosphoSitePlus; P0DP26; -.
DR jPOST; P0DP26; -.
DR PRIDE; P0DP26; -.
DR Antibodypedia; 39411; 188 antibodies from 17 providers.
DR Antibodypedia; 4344; 533 antibodies from 34 providers.
DR Antibodypedia; 53945; 72 antibodies from 14 providers.
DR DNASU; 12313; -.
DR Ensembl; ENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370.
DR Ensembl; ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438.
DR Ensembl; ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175.
DR GeneID; 12313; -.
DR GeneID; 12314; -.
DR GeneID; 12315; -.
DR KEGG; mmu:12313; -.
DR KEGG; mmu:12314; -.
DR KEGG; mmu:12315; -.
DR CTD; 801; -.
DR CTD; 805; -.
DR CTD; 808; -.
DR MGI; MGI:88251; Calm1.
DR VEuPathDB; HostDB:ENSMUSG00000001175; -.
DR VEuPathDB; HostDB:ENSMUSG00000019370; -.
DR VEuPathDB; HostDB:ENSMUSG00000036438; -.
DR eggNOG; KOG0027; Eukaryota.
DR OMA; SCDRHPP; -.
DR OrthoDB; 1386217at2759; -.
DR Reactome; R-MMU-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-MMU-111933; Calmodulin induced events.
DR Reactome; R-MMU-111957; Cam-PDE 1 activation.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-MMU-163615; PKA activation.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-MMU-2025928; Calcineurin activates NFAT.
DR Reactome; R-MMU-203615; eNOS activation.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-MMU-425561; Sodium/Calcium exchangers.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-MMU-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR Reactome; R-MMU-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR Reactome; R-MMU-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR Reactome; R-MMU-8876725; Protein methylation.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR Reactome; R-MMU-9619229; Activation of RAC1 downstream of NMDARs.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 12313; 6 hits in 76 CRISPR screens.
DR BioGRID-ORCS; 12314; 4 hits in 69 CRISPR screens.
DR BioGRID-ORCS; 12315; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Calm1; mouse.
DR PRO; PR:P0DP26; -.
DR Proteomes; UP000000589; Chromosome 12.
DR Proteomes; UP000000589; Chromosome 17.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P0DP26; protein.
DR Bgee; ENSMUSG00000001175; Expressed in ureter smooth muscle and 281 other tissues.
DR ExpressionAtlas; P0DP26; baseline and differential.
DR GO; GO:0034704; C:calcium channel complex; ISO:MGI.
DR GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; IDA:CAFA.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; ISO:MGI.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI.
DR GO; GO:0010856; F:adenylate cyclase activator activity; ISO:MGI.
DR GO; GO:0008179; F:adenylate cyclase binding; ISO:MGI.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0031997; F:N-terminal myristoylation domain binding; ISO:MGI.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISO:MGI.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0072542; F:protein phosphatase activator activity; ISO:MGI.
DR GO; GO:0031432; F:titin binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0031800; F:type 3 metabotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IEA:Ensembl.
DR GO; GO:0016240; P:autophagosome membrane docking; ISS:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0005513; P:detection of calcium ion; ISO:MGI.
DR GO; GO:0090151; P:establishment of protein localization to mitochondrial membrane; IEA:Ensembl.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; ISS:UniProtKB.
DR GO; GO:1901842; P:negative regulation of high voltage-gated calcium channel activity; IEA:Ensembl.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0140056; P:organelle localization by membrane tethering; ISS:UniProtKB.
DR GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; ISO:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:MGI.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI.
DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IEA:Ensembl.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
DR GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Flagellum; Isopeptide bond;
KW Metal-binding; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 2..149
FT /note="Calmodulin-1"
FT /id="PRO_0000439935"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 117..149
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 77..149
FT /note="Necessary and sufficient for interaction with PCP4"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5"
FT MOD_RES 22
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 45
FT /note="Phosphothreonine; by CaMK4"
FT /evidence="ECO:0000250|UniProtKB:P0DP29"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 100
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 116
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62157"
FT MUTAGEN 115
FT /note="E->A: Decreases interaction with SCN8A in the
FT absence of calcium."
FT /evidence="ECO:0000269|PubMed:23942337"
FT MUTAGEN 121
FT /note="E->A: Decreases interaction with SCN8A in the
FT absence of calcium."
FT /evidence="ECO:0000269|PubMed:23942337"
FT MUTAGEN 124
FT /note="E->A: Decreases interaction with SCN8A in the
FT absence of calcium."
FT /evidence="ECO:0000269|PubMed:23942337"
FT MUTAGEN 128
FT /note="E->A: Decreases interaction with SCN8A in the
FT absence of calcium."
FT /evidence="ECO:0000269|PubMed:23942337"
FT CONFLICT 26
FT /note="G -> N (in Ref. 1; AAA66182)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="E -> V (in Ref. 3; BAE41271)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="F -> L (in Ref. 3; BAE40191)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="S -> G (in Ref. 3; BAE31439/BAE31644/BAE31442)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="I -> T (in Ref. 3; BAE31579)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="V -> L (in Ref. 3; BAB28959)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:3WFN"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:7CQP"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:7CQP"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:7CQP"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:7CQP"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:7CQP"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:7CQP"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:4HEX"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:3WFN"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:3WFN"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3WFN"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:3WFN"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4E53"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3WFN"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:3WFN"
SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK
