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P12637 (CASQ2_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calsequestrin-2
Alternative name(s):
Calsequestrin, cardiac muscle isoform
Gene names
Name:CASQ2
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 isoform (CASQ1)binds around 80 Ca2+ ions, while the cardiac isoform (CASQ2)binds approximately 60 Ca2+ ions. Ref.4

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. Interacts with ASPH and TRDN By similarity.

Subcellular location

Sarcoplasmic reticulum lumen. Note: This isoform ofcalsequestrin 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 By similarity.

Sequence similarities

Belongs to the calsequestrin family.

Ontologies

Keywords
   Cellular componentSarcoplasmic reticulum
   DomainSignal
   LigandCalcium
   Molecular functionMuscle protein
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

cellular response to caffeine

Inferred from electronic annotation. Source: Ensembl

negative regulation of potassium ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of potassium ion transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 15041652. Source: BHF-UCL

protein polymerization

Inferred from electronic annotation. Source: Ensembl

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred from electronic annotation. Source: Ensembl

regulation of cell communication by electrical coupling

Inferred from electronic annotation. Source: Ensembl

regulation of heart rate

Inferred from electronic annotation. Source: Ensembl

regulation of membrane repolarization

Inferred from electronic annotation. Source: Ensembl

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from direct assay PubMed 15041652. Source: BHF-UCL

sequestering of calcium ion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

sarcoplasmic reticulum

Inferred from direct assay PubMed 9287354. Source: BHF-UCL

sarcoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 9287354. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2
Chain20 – 410391Calsequestrin-2
PRO_0000004217

Regions

Region221 – 24222Calcium regulated hydrophobic site
Compositional bias219 – 25436Pro-rich
Compositional bias372 – 41039Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue3971Phosphoserine; by CK2
Modified residue4011Phosphoserine; by CK2
Modified residue4051Phosphoserine; by CK2
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict711Q → E AA sequence Ref.2

Secondary structure

............................................................. 410
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12637 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: FCA99A8D7E7ABB82

FASTA41047,417
        10         20         30         40         50         60 
MKRTHLFIAG LYLLASCRAE EGLNFPTYDG KDRVVSLTEK NFKQVLKKYD VLCLYYHESV 

        70         80         90        100        110        120 
SSDKVAQKQF QLKEIVLELV AQVLEHKDIG FVMVDAKKEA KLAKKLGFDE EGSLYVLKGD 

       130        140        150        160        170        180 
RTIEFDGEFA ADVLVEFLLD LIEDPVEIIN SKLEVQAFER IEDQIKLIGF FKSEESEYYK 

       190        200        210        220        230        240 
AFEEAAEHFQ PYIKFFATFD KGVAKKLSLK MNEVDFYEPF MDEPIAIPDK PYTEEELVEF 

       250        260        270        280        290        300 
VKEHQRPTLR RLRPEDMFET WEDDLNGIHI VAFAERSDPD GYEFLEILKQ VARDNTDNPD 

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

       370        380        390        400        410 
WIEDVLSGKI NTEDDDNEEG DDGDDDEDDD DDDGNNSDEE SNDDSDDDDE 

« Hide

References

[1]"Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning."
Scott B.T., Simmerman H.K.B., Collins J.H., Nadal-Ginard B., Jones L.R.
J. Biol. Chem. 263:8958-8964(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"Characterization of cardiac calsequestrin."
Slupsky J.R., Ohnishi M., Carpenter M.R., Reithmeier R.A.F.
Biochemistry 26:6539-6544(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-71.
Tissue: Heart.
[3]"Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. Demonstration of a cluster of unique rapidly phosphorylated sites in cardiac calsequestrin."
Cala S.E., Jones L.R.
J. Biol. Chem. 266:391-398(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CK2.
[4]"Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization."
Park H., Park I.Y., Kim E., Youn B., Fields K., Dunker A.K., Kang C.
J. Biol. Chem. 279:18026-18033(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-371, FUNCTION, CALCIUM AFFINITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03766 mRNA. Translation: AAA30833.1.
PIRA28071.
A39040.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJIX-ray2.40A/B22-371[»]
ProteinModelPortalP12637.
SMRP12637. Positions 22-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000014348.

Proteomic databases

PaxDbP12637.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG77804.
HOGENOMHOG000049047.
HOVERGENHBG050805.
InParanoidP12637.
OrthoDBEOG725DHM.

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR001393. Calsequestrin.
IPR018233. Calsequestrin_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF01216. Calsequestrin. 1 hit.
[Graphical view]
PRINTSPR00312. CALSEQUESTRN.
SUPFAMSSF52833. SSF52833. 3 hits.
PROSITEPS00863. CALSEQUESTRIN_1. 1 hit.
PS00864. CALSEQUESTRIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12637.
NextBio20857578.

Entry information

Entry nameCASQ2_CANFA
AccessionPrimary (citable) accession number: P12637
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: June 11, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references