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Protein

Calsequestrin-2

Gene

Casq2

Organism
Rattus norvegicus (Rat)
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 (PubMed:8042990). Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca2+ ions. Regulates the release of lumenal Ca2+ via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats (By similarity).By similarity1 Publication

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • protein homodimerization activity Source: BHF-UCL
  • protein kinase C binding Source: RGD

GO - Biological processi

  • negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  • regulation of cardiac muscle cell contraction Source: BHF-UCL
  • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calsequestrin-2
Alternative name(s):
Calsequestrin, cardiac muscle isoform
Gene namesi
Name:Casq2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2276. Casq2.

Subcellular locationi

  • Sarcoplasmic reticulum lumen By similarity

  • Note: This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells.By similarity

GO - Cellular componenti

  • sarcoplasmic reticulum Source: RGD
  • sarcoplasmic reticulum lumen Source: UniProtKB-SubCell
  • Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 413394Calsequestrin-2PRO_0000004221Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei282 – 2821PhosphotyrosineCombined sources
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence analysis
Modified residuei398 – 3981PhosphoserineCombined sources
Modified residuei405 – 4051PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation in the C-terminus, probably by CK2, moderately increases calcium buffering capacity.1 Publication
N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP51868.
PRIDEiP51868.

PTM databases

iPTMnetiP51868.
PhosphoSiteiP51868.

Expressioni

Tissue specificityi

Detected in stomach and vas deferens (at protein level).1 Publication

Interactioni

Subunit structurei

Monomer, homodimer and homooligomer. Mostly monomeric in the absence of calcium. Forms higher oligomers in a calcium-dependent manner. Dimers associate to form tetramers, that then form linear homopolymer chains. Interacts with ASPH and TRDN (By similarity).By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL
  • protein kinase C binding Source: RGD

Protein-protein interaction databases

BioGridi247887. 1 interaction.
IntActiP51868. 2 interactions.
STRINGi10116.ENSRNOP00000021846.

Structurei

3D structure databases

ProteinModelPortaliP51868.
SMRiP51868. Positions 22-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi373 – 41341Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the calsequestrin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IGY5. Eukaryota.
ENOG4111R2M. LUCA.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiP51868.
PhylomeDBiP51868.

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.

P51868-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRIYLLVVG LYLLSFSRAE EGLNFPTYDG KDRVVSLSEK NLKQVLKRYD
60 70 80 90 100
LLCLYYHEPV SSDKVAQKQF QLKEIVLELV AQVLEHKNIG FVMVDSRKEA
110 120 130 140 150
KLAKRLGFSE EGSLYVLKGG RTIEFDGEFA ADVLVEFLLD LIEDPVEIVN
160 170 180 190 200
NKLEVQAFER IEDQIKLLGF FKNEDSEYYK AFQEAAEHFQ PYIKFFATFD
210 220 230 240 250
KGVAKKLSLK MNEVGFYEPF MDEPSVIPNK PYTEEELVEF VKEHQRPTLR
260 270 280 290 300
PLRPEDMFET WEDDLNGIHI VAFAEKSDPD GYEFLEILKQ VARDNTDNPD
310 320 330 340 350
LSILWIDPDD FPLLVAYWEK TFKIDLFKPQ IGVVNVTDAD SVWMEIPDDD
360 370 380 390 400
DLPTAEELED WIEDVLSGKI NTEDDDNEDE DDDGDNDNDD DDDDDDNSDE
410
DNDDSDDDDD DDE
Length:413
Mass (Da):47,839
Last modified:October 25, 2005 - v2
Checksum:iF03B6C7C3EB19D80
GO

Sequence cautioni

The sequence AAH72547.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 523DLL → ARV in AAB58746 (Ref. 4) Curated
Sequence conflicti208 – 2114SLKM → FLEV in AAA75480 (Ref. 1) Curated
Sequence conflicti251 – 2511P → R in AAH72547 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33287 mRNA. Translation: AAA75480.1.
BC072547 mRNA. Translation: AAH72547.1. Different initiation.
AF001334 Genomic DNA. Translation: AAB58746.1.
RefSeqiNP_058827.3. NM_017131.2.
UniGeneiRn.10111.

Genome annotation databases

GeneIDi29209.
KEGGirno:29209.
UCSCiRGD:2276. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33287 mRNA. Translation: AAA75480.1.
BC072547 mRNA. Translation: AAH72547.1. Different initiation.
AF001334 Genomic DNA. Translation: AAB58746.1.
RefSeqiNP_058827.3. NM_017131.2.
UniGeneiRn.10111.

3D structure databases

ProteinModelPortaliP51868.
SMRiP51868. Positions 22-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247887. 1 interaction.
IntActiP51868. 2 interactions.
STRINGi10116.ENSRNOP00000021846.

PTM databases

iPTMnetiP51868.
PhosphoSiteiP51868.

Proteomic databases

PaxDbiP51868.
PRIDEiP51868.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29209.
KEGGirno:29209.
UCSCiRGD:2276. rat.

Organism-specific databases

CTDi845.
RGDi2276. Casq2.

Phylogenomic databases

eggNOGiENOG410IGY5. Eukaryota.
ENOG4111R2M. LUCA.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiP51868.
PhylomeDBiP51868.

Miscellaneous databases

PROiP51868.

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. Aquilla T.T., Rovner A.S.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Heart muscle.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  3. "Calsequestrin is a component of smooth muscles: the skeletal- and cardiac-muscle isoforms are both present, although in highly variable amounts and ratios."
    Volpe P., Martini A., Furlan S., Meldolesi J.
    Biochem. J. 301:465-469(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-30, TISSUE SPECIFICITY, FUNCTION.
    Strain: Wistar.
    Tissue: Vas deferens.
  4. Rodriguez M.M., Chen C., Smith B., Mochly-Rosen D.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-413.
    Strain: Sprague-Dawley.
  5. "The cytosolic protein kinase CK2 phosphorylates cardiac calsequestrin in intact cells."
    McFarland T.P., Sleiman N.H., Yaeger D.B., Cala S.E.
    Mol. Cell. Biochem. 353:81-91(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CK2.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-282; SER-398 AND SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCASQ2_RAT
AccessioniPrimary (citable) accession number: P51868
Secondary accession number(s): O09177, Q6IMX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 25, 2005
Last modified: June 8, 2016
This is version 116 of the entry and version 2 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. 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.