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Protein

Calsequestrin-1

Gene

Casq1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca2+ ions (By similarity). Regulates the release of lumenal Ca2+ via the calcium release channel RYR1; this plays an important role in triggering muscle contraction.By similarity3 Publications

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB

GO - Biological processi

  • endoplasmic reticulum organization Source: MGI
  • protein polymerization Source: UniProtKB
  • regulation of muscle contraction Source: MGI
  • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: MGI
  • regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion Source: UniProtKB
  • response to denervation involved in regulation of muscle adaptation Source: Ensembl
  • response to heat Source: MGI
  • response to organic substance Source: Ensembl
  • sarcomere organization Source: UniProtKB
  • skeletal muscle tissue development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-2672351. Stimuli-sensing channels.
R-MMU-5578775. Ion homeostasis.

Names & Taxonomyi

Protein namesi
Recommended name:
Calsequestrin-1
Alternative name(s):
Calmitine1 Publication
Calsequestrin, skeletal muscle isoform
Gene namesi
Name:Casq1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1309468. Casq1.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: Ensembl
  • I band Source: Ensembl
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: MGI
  • sarcoplasmic reticulum Source: UniProtKB
  • sarcoplasmic reticulum lumen Source: UniProtKB
  • sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
  • terminal cisterna lumen Source: Ensembl
  • T-tubule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Sarcoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile, but have a lower body weight than wild-type, due to a reduction in fast-twitch muscle mass. Fast-twitch muscle from mutant mice exhibits slower contraction kinetics and requires more time to achieve peak tension and to achieve half-relaxation after a contraction. Fast-twitch muscle fibers from mutant mice show a strikingly altered structure of the calcium release units in the sarcoplasmic reticulum with a strongly increased number of ryanodine receptors, plus narrower sarcoplasmic reticulum cisternae. In addition, the number of mitochondria is increased in mutant muscle. Mutant muscle fibers show smaller calcium transients upon electrical stimulation and release less Ca2+ in response to caffeine.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 34341 PublicationAdd
BLAST
Chaini35 – 405371Calsequestrin-1PRO_0000412170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphotyrosineBy similarity
Modified residuei81 – 811PhosphoserineBy similarity
Modified residuei124 – 1241PhosphothreonineBy similarity
Modified residuei216 – 2161PhosphoserineBy similarity
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO09165.
PaxDbiO09165.
PRIDEiO09165.

PTM databases

iPTMnetiO09165.
PhosphoSiteiO09165.

Expressioni

Tissue specificityi

Detected in skeletal muscle (at protein level). Detected in skeletal muscle.4 Publications

Gene expression databases

BgeeiO09165.
CleanExiMM_CASQ1.
ExpressionAtlasiO09165. baseline and differential.
GenevisibleiO09165. MM.

Interactioni

Subunit structurei

Monomer, homodimer, homotetramer and homopolymer. Can form linear homooligomers. Ca2+ ions promote oligomerization. Interacts with ASPH and TRDN (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003554.

Structurei

3D structure databases

ProteinModelPortaliO09165.
SMRiO09165. Positions 37-388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi353 – 40553Asp-richAdd
BLAST

Sequence similaritiesi

Belongs to the calsequestrin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IGY5. Eukaryota.
ENOG4111R2M. LUCA.
GeneTreeiENSGT00390000019377.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiO09165.
OMAiVYVFKGD.
OrthoDBiEOG725DHM.
TreeFamiTF313796.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR001393. Calsequestrin.
IPR018233. Calsequestrin_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF01216. Calsequestrin. 1 hit.
[Graphical view]
PRINTSiPR00312. CALSEQUESTRN.
SUPFAMiSSF52833. SSF52833. 3 hits.
PROSITEiPS00863. CALSEQUESTRIN_1. 1 hit.
PS00864. CALSEQUESTRIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O09165-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRATDRMGAR AVSELRLALL FVLVLGTPRL GVQGEDGLDF PEYDGVDRVI
60 70 80 90 100
NVNAKNYKNV FKKYEVLALL YHEPPEDDKA SQRQFEMEEL ILELAAQVLE
110 120 130 140 150
DKGVGFGLVD SEKDAAVAKK LGLTEEDSVY VFKGDEVIEY DGEFSADTLV
160 170 180 190 200
EFLLDVLEDP VELIEGEREL QAFENIEDEI KLIGYFKSKD SEHYKAYEDA
210 220 230 240 250
AEEFHPYIPF FATFDSKVAK KLTLKLNEID FYEAFMEEPM TIPDKPNSEE
260 270 280 290 300
EIVSFVEEHR RSTLRKLKPE SMYETWEDDL DGIHIVAFAE EADPDGYEFL
310 320 330 340 350
ETLKAVAQDN TENPDLSIIW IDPDDFPLLV PYWEKTFDID LSAPQIGVVN
360 370 380 390 400
VTDADSIWME MDNEEDLPSA DELEDWLEDV LEGEINTEDD DDDDDDDDDD

DDDDD
Length:405
Mass (Da):46,378
Last modified:July 27, 2011 - v3
Checksum:i813A8DD681434E59
GO

Sequence cautioni

The sequence AAC63616.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93291 mRNA. Translation: AAC63616.1. Different initiation.
AC074310 Genomic DNA. No translation available.
CCDSiCCDS35781.2.
RefSeqiNP_033943.2. NM_009813.2.
UniGeneiMm.12829.

Genome annotation databases

EnsembliENSMUST00000003554; ENSMUSP00000003554; ENSMUSG00000007122.
GeneIDi12372.
KEGGimmu:12372.
UCSCiuc007dqa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93291 mRNA. Translation: AAC63616.1. Different initiation.
AC074310 Genomic DNA. No translation available.
CCDSiCCDS35781.2.
RefSeqiNP_033943.2. NM_009813.2.
UniGeneiMm.12829.

3D structure databases

ProteinModelPortaliO09165.
SMRiO09165. Positions 37-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003554.

PTM databases

iPTMnetiO09165.
PhosphoSiteiO09165.

Proteomic databases

MaxQBiO09165.
PaxDbiO09165.
PRIDEiO09165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003554; ENSMUSP00000003554; ENSMUSG00000007122.
GeneIDi12372.
KEGGimmu:12372.
UCSCiuc007dqa.2. mouse.

Organism-specific databases

CTDi844.
MGIiMGI:1309468. Casq1.

Phylogenomic databases

eggNOGiENOG410IGY5. Eukaryota.
ENOG4111R2M. LUCA.
GeneTreeiENSGT00390000019377.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiO09165.
OMAiVYVFKGD.
OrthoDBiEOG725DHM.
TreeFamiTF313796.

Enzyme and pathway databases

ReactomeiR-MMU-2672351. Stimuli-sensing channels.
R-MMU-5578775. Ion homeostasis.

Miscellaneous databases

ChiTaRSiCasq1. mouse.
NextBioi281074.
PROiO09165.
SOURCEiSearch...

Gene expression databases

BgeeiO09165.
CleanExiMM_CASQ1.
ExpressionAtlasiO09165. baseline and differential.
GenevisibleiO09165. MM.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR001393. Calsequestrin.
IPR018233. Calsequestrin_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF01216. Calsequestrin. 1 hit.
[Graphical view]
PRINTSiPR00312. CALSEQUESTRN.
SUPFAMiSSF52833. SSF52833. 3 hits.
PROSITEiPS00863. CALSEQUESTRIN_1. 1 hit.
PS00864. CALSEQUESTRIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the genes encoding mouse cardiac and skeletal calsequestrins: expression pattern during embryogenesis."
    Park K.-W., Goo J.H., Chung H.-S., Kim H., Kim D.-H., Park W.-J.
    Gene 217:25-30(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Molecular cloning of human calmitine, a mitochondrial calcium binding protein, reveals identity with calsequestrine."
    Bataille N., Schmitt N., Aumercier-Maes P., Ollivier B., Lucas-Heron B., Lestienne P.
    Biochem. Biophys. Res. Commun. 203:1477-1482(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 35-47, SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  4. "Reorganized stores and impaired calcium handling in skeletal muscle of mice lacking calsequestrin-1."
    Paolini C., Quarta M., Nori A., Boncompagni S., Canato M., Volpe P., Allen P.D., Reggiani C., Protasi F.
    J. Physiol. (Lond.) 583:767-784(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart and Lung.
  6. "Calsequestrin (CASQ1) rescues function and structure of calcium release units in skeletal muscles of CASQ1-null mice."
    Tomasi M., Canato M., Paolini C., Dainese M., Reggiani C., Volpe P., Protasi F., Nori A.
    Am. J. Physiol. 302:C575-C586(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCASQ1_MOUSE
AccessioniPrimary (citable) accession number: O09165
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: March 16, 2016
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.