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P12637

- CASQ2_CANFA

UniProt

P12637 - CASQ2_CANFA

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Protein

Calsequestrin-2

Gene

CASQ2

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - 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

  1. calcium ion binding Source: Ensembl

GO - Biological processi

  1. cardiac muscle contraction Source: Ensembl
  2. cellular response to caffeine Source: Ensembl
  3. negative regulation of potassium ion transmembrane transporter activity Source: Ensembl
  4. negative regulation of potassium ion transport Source: Ensembl
  5. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  6. protein polymerization Source: Ensembl
  7. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: Ensembl
  8. regulation of cell communication by electrical coupling Source: Ensembl
  9. regulation of heart rate Source: Ensembl
  10. regulation of membrane repolarization Source: Ensembl
  11. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  12. sequestering of calcium ion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_219568. 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: 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

  1. sarcoplasmic reticulum Source: BHF-UCL
  2. 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 – 373
Helixi39 – 468
Beta strandi50 – 578
Beta strandi62 – 643
Helixi68 – 8316
Helixi84 – 863
Beta strandi87 – 959
Turni96 – 994
Helixi100 – 1067
Beta strandi113 – 1186
Beta strandi121 – 1255
Helixi131 – 1399
Beta strandi145 – 1484
Helixi152 – 1609
Beta strandi166 – 1705
Helixi177 – 18812
Turni189 – 1924
Beta strandi193 – 1986
Helixi201 – 2077
Beta strandi214 – 2174
Beta strandi228 – 2314
Helixi234 – 24411
Beta strandi248 – 2514
Turni254 – 2563
Helixi257 – 2626
Beta strandi265 – 2739
Helixi279 – 29416
Helixi295 – 2973
Beta strandi303 – 3064
Helixi308 – 3103
Helixi312 – 32110
Beta strandi330 – 33910
Beta strandi341 – 3444
Helixi355 – 36612

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 [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:
EMBL
GenBank
DDBJ
Links Updated
J03766 mRNA. Translation: AAA30833.1.
PIRiA28071.
A39040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03766 mRNA. Translation: AAA30833.1 .
PIRi A28071.
A39040.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SJI X-ray 2.40 A/B 22-371 [» ]
ProteinModelPortali P12637.
SMRi P12637. Positions 22-370.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000014348.

Proteomic databases

PaxDbi P12637.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG77804.
HOGENOMi HOG000049047.
HOVERGENi HBG050805.
InParanoidi P12637.
OrthoDBi EOG725DHM.

Enzyme and pathway databases

Reactomei REACT_219568. Stimuli-sensing channels.

Miscellaneous databases

EvolutionaryTracei P12637.
NextBioi 20857578.

Family and domain databases

Gene3Di 3.40.30.10. 3 hits.
InterProi IPR001393. Calsequestrin.
IPR018233. Calsequestrin_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF01216. Calsequestrin. 1 hit.
[Graphical view ]
PRINTSi PR00312. CALSEQUESTRN.
SUPFAMi SSF52833. SSF52833. 3 hits.
PROSITEi PS00863. CALSEQUESTRIN_1. 1 hit.
PS00864. CALSEQUESTRIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 119 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