Calsequestrin-2 precursor - Rattus norvegicus (Rat)

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P51868 (CASQ2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Calsequestrin-2

Alternative name(s):
Calsequestrin, cardiac muscle isoform

Gene names

Name:

Casq2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. The release of calcium bound to calsequestrin through a calcium release channel triggers muscle contraction. The skeletal muscle CASQ1) binds around 80 Ca²⁺ ions, while the cardiac CASQ2) binds approximately 60 Ca²⁺ ions By similarity.
Subunit structure	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 By similarity.
Subcellular location	Sarcoplasmic reticulum lumen. Note: This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells.
Post-translational modification	Phosphorylation in the C-terminus, probably by CK2, moderately increases calcium buffering capacity.
Sequence similarities	Belongs to the calsequestrin family.
Sequence caution	The sequence AAH72547.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Sarcoplasmic reticulum
Domain	Signal
Ligand	Calcium
Molecular function	Muscle protein
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity Inferred from mutant phenotype PubMed 17569730. Source: BHF-UCL regulation of cardiac muscle cell contraction Inferred from mutant phenotype PubMed 17569730. Source: BHF-UCL regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Inferred from mutant phenotype PubMed 17569730. Source: BHF-UCL
Cellular_component	Z disc Inferred from direct assay PubMed 11053140. Source: BHF-UCL sarcoplasmic reticulum Inferred from direct assay PubMed 17569730. Source: RGD sarcoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from direct assay PubMed 20353949. Source: BHF-UCL protein kinase C binding Inferred from direct assay PubMed 10431815. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

By similarity

Chain

20 – 413

394

Calsequestrin-2

PRO_0000004221

Regions

Compositional bias

373 – 413

Asp/Glu-rich (acidic)

Amino acid modifications

Glycosylation

335

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

50 – 52

DLL → ARV in AAB58746. Ref.4

Sequence conflict

208 – 211

SLKM → FLEV in AAA75480. Ref.1

Sequence conflict

251

P → R in AAH72547. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P51868 [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: F03B6C7C3EB19D80
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FASTA

413

47,839

        10         20         30         40         50         60 
MKRIYLLVVG LYLLSFSRAE EGLNFPTYDG KDRVVSLSEK NLKQVLKRYD LLCLYYHEPV 

        70         80         90        100        110        120 
SSDKVAQKQF QLKEIVLELV AQVLEHKNIG FVMVDSRKEA KLAKRLGFSE EGSLYVLKGG 

       130        140        150        160        170        180 
RTIEFDGEFA ADVLVEFLLD LIEDPVEIVN NKLEVQAFER IEDQIKLLGF FKNEDSEYYK 

       190        200        210        220        230        240 
AFQEAAEHFQ PYIKFFATFD KGVAKKLSLK MNEVGFYEPF MDEPSVIPNK PYTEEELVEF 

       250        260        270        280        290        300 
VKEHQRPTLR PLRPEDMFET WEDDLNGIHI VAFAEKSDPD GYEFLEILKQ VARDNTDNPD 

       310        320        330        340        350        360 
LSILWIDPDD FPLLVAYWEK TFKIDLFKPQ IGVVNVTDAD SVWMEIPDDD DLPTAEELED 

       370        380        390        400        410 
WIEDVLSGKI NTEDDDNEDE DDDGDNDNDD DDDDDDNSDE DNDDSDDDDD DDE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U33287 mRNA. Translation: AAA75480.1. BC072547 mRNA. Translation: AAH72547.1. Different initiation. AF001334 Genomic DNA. Translation: AAB58746.1.
IPI	IPI00231901.
RefSeq	NP_058827.3. NM_017131.2.
UniGene	Rn.10111. Rn.226914.
3D structure databases
ProteinModelPortal	P51868.
SMR	P51868. Positions 22-370.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51868. 1 interaction.
STRING	10116.ENSRNOP00000021846.
PTM databases
PhosphoSite	P51868.
Proteomic databases
PRIDE	P51868.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	29209.
KEGG	rno:29209.
UCSC	RGD:2276. rat.
Organism-specific databases
CTD	845.
RGD	2276. Casq2.
Phylogenomic databases
eggNOG	NOG77804.
HOGENOM	HOG000049047.
HOVERGEN	HBG050805.
InParanoid	P51868.
OrthoDB	EOG4W0XD8.
Gene expression databases
ArrayExpress	P51868.
Genevestigator	P51868.
GermOnline	ENSRNOG00000016243. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.30.10. 3 hits.
InterPro	IPR001393. Calsequestrin. IPR018233. Calsequestrin_CS. IPR012336. Thioredoxin-like_fold. [Graphical view]
PANTHER	PTHR10033. PTHR10033. 1 hit.
Pfam	PF01216. Calsequestrin. 1 hit. [Graphical view]
PRINTS	PR00312. CALSEQUESTRN.
SUPFAM	SSF52833. Thiordxn-like_fd. 3 hits.
PROSITE	PS00863. CALSEQUESTRIN_1. 1 hit. PS00864. CALSEQUESTRIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	608376.

Entry information

Entry name

CASQ2_RAT

Accession

Primary (citable) accession number: P51868
Secondary accession number(s): O09177, Q6IMX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 25, 2005
Last modified:	April 3, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents