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Protein

Calsequestrin-2

Gene

CASQ2

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
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:3427023). 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.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_321077. Stimuli-sensing channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Calsequestrin-2
Alternative name(s):
Calsequestrin, cardiac muscle isoform
Gene namesi
Name:CASQ2
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Unplaced

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

  • junctional membrane complex Source: Ensembl
  • sarcoplasmic reticulum Source: BHF-UCL
  • sarcoplasmic reticulum lumen Source: UniProtKB-SubCell
  • Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Sarcoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi206 – 2061K → N: Creates an additional N-glycosylation site. Decreases calcium binding and increases the rate of spontaneous Ca(2+) release from myocytes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 410391Calsequestrin-2PRO_0000004217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
Modified residuei397 – 3971Phosphoserine; by CK21 Publication
Modified residuei401 – 4011Phosphoserine; by CK21 Publication
Modified residuei405 – 4051Phosphoserine; by CK21 Publication

Post-translational modificationi

Phosphorylation in the C-terminus, probably by CK2, moderately increases calcium buffering capacity.By similarity
N-glycosylated.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP12637.

Expressioni

Tissue specificityi

Detected in heart muscle (at protein level).1 Publication

Interactioni

Subunit structurei

Interacts with ASPH (By similarity). 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 TRDN.By similarity2 Publications

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000014348.

Structurei

Secondary structure

1
410
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 373Combined sources
Helixi39 – 468Combined sources
Beta strandi50 – 578Combined sources
Beta strandi62 – 643Combined sources
Helixi68 – 8316Combined sources
Helixi84 – 863Combined sources
Beta strandi87 – 959Combined sources
Turni96 – 994Combined sources
Helixi100 – 1067Combined sources
Beta strandi113 – 1186Combined sources
Beta strandi121 – 1255Combined sources
Helixi131 – 1399Combined sources
Beta strandi145 – 1484Combined sources
Helixi152 – 1609Combined sources
Beta strandi166 – 1705Combined sources
Helixi177 – 18812Combined sources
Turni189 – 1924Combined sources
Beta strandi193 – 1986Combined sources
Helixi201 – 2077Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi228 – 2314Combined sources
Helixi234 – 24411Combined sources
Beta strandi248 – 2514Combined sources
Turni254 – 2563Combined sources
Helixi257 – 2626Combined sources
Beta strandi265 – 2739Combined sources
Helixi279 – 29416Combined sources
Helixi295 – 2973Combined sources
Beta strandi303 – 3064Combined sources
Helixi308 – 3103Combined sources
Helixi312 – 32110Combined sources
Beta strandi330 – 33910Combined sources
Beta strandi341 – 3444Combined sources
Helixi355 – 36612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJIX-ray2.40A/B22-371[»]
ProteinModelPortaliP12637.
SMRiP12637. Positions 22-370.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12637.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni221 – 24222Calcium regulated hydrophobic siteAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi219 – 25436Pro-richAdd
BLAST
Compositional biasi372 – 41039Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the calsequestrin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG77804.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiP12637.
OrthoDBiEOG725DHM.

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.

P12637-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRTHLFIAG LYLLASCRAE EGLNFPTYDG KDRVVSLTEK NFKQVLKKYD
60 70 80 90 100
VLCLYYHESV SSDKVAQKQF QLKEIVLELV AQVLEHKDIG FVMVDAKKEA
110 120 130 140 150
KLAKKLGFDE EGSLYVLKGD RTIEFDGEFA ADVLVEFLLD LIEDPVEIIN
160 170 180 190 200
SKLEVQAFER IEDQIKLIGF FKSEESEYYK AFEEAAEHFQ PYIKFFATFD
210 220 230 240 250
KGVAKKLSLK MNEVDFYEPF MDEPIAIPDK PYTEEELVEF VKEHQRPTLR
260 270 280 290 300
RLRPEDMFET WEDDLNGIHI VAFAERSDPD GYEFLEILKQ VARDNTDNPD
310 320 330 340 350
LSIVWIDPDD FPLLVAYWEK TFKIDLFKPQ IGVVNVTDAD SVWMEIPDDD
360 370 380 390 400
DLPTAEELED WIEDVLSGKI NTEDDDNEEG DDGDDDEDDD DDDGNNSDEE
410
SNDDSDDDDE
Length:410
Mass (Da):47,417
Last modified:October 1, 1989 - v1
Checksum:iFCA99A8D7E7ABB82
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711Q → E AA sequence (PubMed:3427023).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03766 mRNA. Translation: AAA30833.1.
PIRiA28071.
A39040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03766 mRNA. Translation: AAA30833.1.
PIRiA28071.
A39040.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJIX-ray2.40A/B22-371[»]
ProteinModelPortaliP12637.
SMRiP12637. Positions 22-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000014348.

Proteomic databases

PaxDbiP12637.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG77804.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiP12637.
OrthoDBiEOG725DHM.

Enzyme and pathway databases

ReactomeiREACT_321077. Stimuli-sensing channels.

Miscellaneous databases

EvolutionaryTraceiP12637.
NextBioi20857578.

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

  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. Cited for: PROTEIN SEQUENCE OF 20-71, FUNCTION, TISSUE SPECIFICITY.
    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. "The human CASQ2 mutation K206N is associated with hyperglycosylation and altered cellular calcium handling."
    Kirchhefer U., Wehrmeister D., Postma A.V., Pohlentz G., Mormann M., Kucerova D., Muller F.U., Schmitz W., Schulze-Bahr E., Wilde A.A., Neumann J.
    J. Mol. Cell. Cardiol. 49:95-105(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-206, GLYCOSYLATION, INTERACTION WITH TRDN.
  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: GLYCOSYLATION.
  6. "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, SUBUNIT, CALCIUM AFFINITY.

Entry informationi

Entry nameiCASQ2_CANFA
AccessioniPrimary (citable) accession number: P12637
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 22, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.