CASQ1_MOUSE
ID CASQ1_MOUSE Reviewed; 405 AA.
AC O09165;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Calsequestrin-1;
DE AltName: Full=Calmitine {ECO:0000303|PubMed:7945294};
DE AltName: Full=Calsequestrin, skeletal muscle isoform;
DE Flags: Precursor;
GN Name=Casq1;
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], AND TISSUE SPECIFICITY.
RX PubMed=9795116; DOI=10.1016/s0378-1119(98)00372-2;
RA Park K.-W., Goo J.H., Chung H.-S., Kim H., Kim D.-H., Park W.-J.;
RT "Cloning of the genes encoding mouse cardiac and skeletal calsequestrins:
RT expression pattern during embryogenesis.";
RL Gene 217:25-30(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PROTEIN SEQUENCE OF 35-47, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=7945294; DOI=10.1006/bbrc.1994.2351;
RA Bataille N., Schmitt N., Aumercier-Maes P., Ollivier B., Lucas-Heron B.,
RA Lestienne P.;
RT "Molecular cloning of human calmitine, a mitochondrial calcium binding
RT protein, reveals identity with calsequestrine.";
RL Biochem. Biophys. Res. Commun. 203:1477-1482(1994).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17627988; DOI=10.1113/jphysiol.2007.138024;
RA Paolini C., Quarta M., Nori A., Boncompagni S., Canato M., Volpe P.,
RA Allen P.D., Reggiani C., Protasi F.;
RT "Reorganized stores and impaired calcium handling in skeletal muscle of
RT mice lacking calsequestrin-1.";
RL J. Physiol. (Lond.) 583:767-784(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Lung;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22049211; DOI=10.1152/ajpcell.00119.2011;
RA Tomasi M., Canato M., Paolini C., Dainese M., Reggiani C., Volpe P.,
RA Protasi F., Nori A.;
RT "Calsequestrin (CASQ1) rescues function and structure of calcium release
RT units in skeletal muscles of CASQ1-null mice.";
RL Am. J. Physiol. 302:C575-C586(2012).
CC -!- FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-
CC binding protein and thus acts as an internal calcium store in muscle.
CC Calcium ions are bound by clusters of acidic residues at the protein
CC surface, often at the interface between subunits. Can bind around 80
CC Ca(2+) ions (By similarity). Regulates the release of lumenal Ca(2+)
CC via the calcium release channel RYR1; this plays an important role in
CC triggering muscle contraction. Negatively regulates store-operated
CC Ca(2+) entry (SOCE) activity (By similarity).
CC {ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:17627988,
CC ECO:0000269|PubMed:22049211, ECO:0000269|PubMed:7945294}.
CC -!- SUBUNIT: Monomer; increases in response to a depletion of intracellular
CC calcium. Homodimer. Homotetramer and homopolymer. Can form linear
CC homooligomers. Ca(2+) ions promote oligomerization. Interacts (via C-
CC terminal end and preferentially with the monomeric form) with STIM1;
CC this interaction increases in response to a depletion of intracellular
CC calcium, decreases both STIM1 aggregation and clustering, interaction
CC of STIM1 with ORAI1 and store-operated Ca(2+) entry (SOCE) activity.
CC Interacts with ASPH and TRDN. {ECO:0000250|UniProtKB:P07221,
CC ECO:0000250|UniProtKB:P31415}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum
CC {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum lumen
CC {ECO:0000269|PubMed:22049211, ECO:0000269|PubMed:7945294}. Sarcoplasmic
CC reticulum membrane; Peripheral membrane protein; Lumenal side
CC {ECO:0000250|UniProtKB:P07221}. Mitochondrion matrix
CC {ECO:0000269|PubMed:7945294}. Note=This isoform of calsequestrin occurs
CC in the sarcoplasmic reticulum's terminal cisternae luminal spaces of
CC fast skeletal muscle cells (PubMed:22049211). Preferentially forms
CC linear and round aggregates in the endoplasmic reticulum (ER) of
CC resting cells. In a minority of cells, homogeneously detected in the ER
CC lumen. Colocalizes with STIM1 at endoplasmic reticulum in response to a
CC depletion of intracellular calcium (By similarity).
CC {ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:22049211}.
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level).
CC Detected in skeletal muscle. {ECO:0000269|PubMed:17627988,
CC ECO:0000269|PubMed:22049211, ECO:0000269|PubMed:7945294,
CC ECO:0000269|PubMed:9795116}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P07221}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but have a lower
CC body weight than wild-type, due to a reduction in fast-twitch muscle
CC mass. Fast-twitch muscle from mutant mice exhibits slower contraction
CC kinetics and requires more time to achieve peak tension and to achieve
CC half-relaxation after a contraction. Fast-twitch muscle fibers from
CC mutant mice show a strikingly altered structure of the calcium release
CC units in the sarcoplasmic reticulum with a strongly increased number of
CC ryanodine receptors, plus narrower sarcoplasmic reticulum cisternae. In
CC addition, the number of mitochondria is increased in mutant muscle.
CC Mutant muscle fibers show smaller calcium transients upon electrical
CC stimulation and release less Ca(2+) in response to caffeine.
CC {ECO:0000269|PubMed:17627988}.
CC -!- SIMILARITY: Belongs to the calsequestrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC63616.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U93291; AAC63616.1; ALT_INIT; mRNA.
DR EMBL; AC074310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS35781.2; -.
DR RefSeq; NP_033943.2; NM_009813.2.
DR AlphaFoldDB; O09165; -.
DR SMR; O09165; -.
DR BioGRID; 198502; 1.
DR STRING; 10090.ENSMUSP00000003554; -.
DR GlyGen; O09165; 1 site.
DR iPTMnet; O09165; -.
DR PhosphoSitePlus; O09165; -.
DR MaxQB; O09165; -.
DR PaxDb; O09165; -.
DR PeptideAtlas; O09165; -.
DR PRIDE; O09165; -.
DR ProteomicsDB; 281218; -.
DR Antibodypedia; 1664; 159 antibodies from 26 providers.
DR DNASU; 12372; -.
DR Ensembl; ENSMUST00000003554; ENSMUSP00000003554; ENSMUSG00000007122.
DR GeneID; 12372; -.
DR KEGG; mmu:12372; -.
DR UCSC; uc007dqa.2; mouse.
DR CTD; 844; -.
DR MGI; MGI:1309468; Casq1.
DR VEuPathDB; HostDB:ENSMUSG00000007122; -.
DR eggNOG; ENOG502QQUJ; Eukaryota.
DR GeneTree; ENSGT00390000019377; -.
DR HOGENOM; CLU_036303_1_0_1; -.
DR InParanoid; O09165; -.
DR OMA; GYPELEY; -.
DR OrthoDB; 1091027at2759; -.
DR PhylomeDB; O09165; -.
DR TreeFam; TF313796; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR BioGRID-ORCS; 12372; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Casq1; mouse.
DR PRO; PR:O09165; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O09165; protein.
DR Bgee; ENSMUSG00000007122; Expressed in triceps brachii and 133 other tissues.
DR ExpressionAtlas; O09165; baseline and differential.
DR Genevisible; O09165; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0031674; C:I band; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0030016; C:myofibril; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0014802; C:terminal cisterna; ISO:MGI.
DR GO; GO:0014804; C:terminal cisterna lumen; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:1901341; P:positive regulation of store-operated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; ISS:UniProtKB.
DR GO; GO:0006937; P:regulation of muscle contraction; TAS:MGI.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0051282; P:regulation of sequestering of calcium ion; ISO:MGI.
DR GO; GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; IMP:UniProtKB.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; ISS:UniProtKB.
DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IMP:MGI.
DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IMP:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR CDD; cd03074; PDI_b'_Calsequestrin_C; 1.
DR CDD; cd03066; PDI_b_Calsequestrin_middle; 1.
DR CDD; cd03065; PDI_b_Calsequestrin_N; 1.
DR InterPro; IPR001393; Calsequestrin.
DR InterPro; IPR041860; Calsequestrin_C.
DR InterPro; IPR018233; Calsequestrin_CS.
DR InterPro; IPR041858; Calsequestrin_middle_dom.
DR InterPro; IPR041859; Calsequestrin_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF01216; Calsequestrin; 1.
DR SUPFAM; SSF52833; SSF52833; 3.
DR PROSITE; PS00863; CALSEQUESTRIN_1; 1.
DR PROSITE; PS00864; CALSEQUESTRIN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Metal-binding; Mitochondrion; Muscle protein; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:7945294"
FT CHAIN 35..405
FT /note="Calsequestrin-1"
FT /id="PRO_0000412170"
FT REGION 382..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19633"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19633"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19633"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19633"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 405 AA; 46378 MW; 813A8DD681434E59 CRC64;
MRATDRMGAR AVSELRLALL FVLVLGTPRL GVQGEDGLDF PEYDGVDRVI NVNAKNYKNV
FKKYEVLALL YHEPPEDDKA SQRQFEMEEL ILELAAQVLE DKGVGFGLVD SEKDAAVAKK
LGLTEEDSVY VFKGDEVIEY DGEFSADTLV EFLLDVLEDP VELIEGEREL QAFENIEDEI
KLIGYFKSKD SEHYKAYEDA AEEFHPYIPF FATFDSKVAK KLTLKLNEID FYEAFMEEPM
TIPDKPNSEE EIVSFVEEHR RSTLRKLKPE SMYETWEDDL DGIHIVAFAE EADPDGYEFL
ETLKAVAQDN TENPDLSIIW IDPDDFPLLV PYWEKTFDID LSAPQIGVVN VTDADSIWME
MDNEEDLPSA DELEDWLEDV LEGEINTEDD DDDDDDDDDD DDDDD
