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Protein

Calsequestrin-2

Gene

CASQ2

Organism
Canis lupus familiaris (Dog) (Canis 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

Names & Taxonomyi

Protein namesi
Recommended name:
Calsequestrin-2
Alternative name(s):
Calsequestrin, cardiac muscle isoform
Gene namesi
Name:CASQ2
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 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

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

Keywords - Cellular componenti

Sarcoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi206K → N: Creates an additional N-glycosylation site. Decreases calcium binding and increases the rate of spontaneous Ca(2+) release from myocytes. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000000421720 – 410Calsequestrin-2Add BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei282PhosphotyrosineBy similarity1
Glycosylationi335N-linked (GlcNAc...)Sequence analysis1
Glycosylationi395N-linked (GlcNAc...)Sequence analysis1
Modified residuei397Phosphoserine; by CK21 Publication1
Modified residuei401Phosphoserine; by CK21 Publication1
Modified residuei405Phosphoserine; by CK21 Publication1

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.

PTM databases

iPTMnetiP12637.

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

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 37Combined sources3
Helixi39 – 46Combined sources8
Beta strandi50 – 57Combined sources8
Beta strandi62 – 64Combined sources3
Helixi68 – 83Combined sources16
Helixi84 – 86Combined sources3
Beta strandi87 – 95Combined sources9
Turni96 – 99Combined sources4
Helixi100 – 106Combined sources7
Beta strandi113 – 118Combined sources6
Beta strandi121 – 125Combined sources5
Helixi131 – 139Combined sources9
Beta strandi145 – 148Combined sources4
Helixi152 – 160Combined sources9
Beta strandi166 – 170Combined sources5
Helixi177 – 188Combined sources12
Turni189 – 192Combined sources4
Beta strandi193 – 198Combined sources6
Helixi201 – 207Combined sources7
Beta strandi214 – 217Combined sources4
Beta strandi228 – 231Combined sources4
Helixi234 – 244Combined sources11
Beta strandi248 – 251Combined sources4
Turni254 – 256Combined sources3
Helixi257 – 262Combined sources6
Beta strandi265 – 273Combined sources9
Helixi279 – 294Combined sources16
Helixi295 – 297Combined sources3
Beta strandi303 – 306Combined sources4
Helixi308 – 310Combined sources3
Helixi312 – 321Combined sources10
Beta strandi330 – 339Combined sources10
Beta strandi341 – 344Combined sources4
Helixi355 – 366Combined sources12

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP12637.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni221 – 242Calcium regulated hydrophobic siteAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi219 – 254Pro-richAdd BLAST36
Compositional biasi372 – 410Asp/Glu-rich (acidic)Add BLAST39

Sequence similaritiesi

Belongs to the calsequestrin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IGY5. Eukaryota.
ENOG4111R2M. LUCA.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiP12637.

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)DescriptionActionsGraphical viewLength
Sequence conflicti71Q → E AA sequence (PubMed:3427023).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03766 mRNA. Translation: AAA30833.1.
PIRiA28071.
A39040.
RefSeqiNP_001300745.1. NM_001313816.1.

Genome annotation databases

GeneIDi483134.
KEGGicfa:483134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03766 mRNA. Translation: AAA30833.1.
PIRiA28071.
A39040.
RefSeqiNP_001300745.1. NM_001313816.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000014348.

PTM databases

iPTMnetiP12637.

Proteomic databases

PaxDbiP12637.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi483134.
KEGGicfa:483134.

Organism-specific databases

CTDi845.

Phylogenomic databases

eggNOGiENOG410IGY5. Eukaryota.
ENOG4111R2M. LUCA.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiP12637.

Miscellaneous databases

EvolutionaryTraceiP12637.

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...

Entry informationi

Entry nameiCASQ2_CANLF
AccessioniPrimary (citable) accession number: P12637
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 2, 2016
This is version 134 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

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.