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P07221 (CASQ1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 102. 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-1
Alternative name(s):
Aspartactin
Calsequestrin, skeletal muscle isoform
Laminin-binding protein
Gene names
Name:CASQ1
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length395 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 By similarity.

Subcellular location

Sarcoplasmic reticulum lumen. Note: This isoform ofcalsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells.

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)
   Cellular_componentsarcoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.3
Chain29 – 395367Calsequestrin-1
PRO_0000004214

Regions

Region231 – 26535Calcium regulated hydrophobic site
Region231 – 26535Trifluoperazine binding site
Compositional bias354 – 39542Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue3811Phosphothreonine; by CK2
Glycosylation3441N-linked (GlcNAc...) Ref.1

Experimental info

Sequence conflict387 – 3882ED → DE AA sequence Ref.4

Secondary structure

................................................................ 395
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07221 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: E849B05AF107AFA7

FASTA39545,263
        10         20         30         40         50         60 
MNAADRMGAR VALLLLLVLG SPQSGVHGEE GLDFPEYDGV DRVINVNAKN YKNVFKKYEV 

        70         80         90        100        110        120 
LALLYHEPPE DDKASQRQFE MEELILELAA QVLEDKGVGF GLVDSEKDAA VAKKLGLTEE 

       130        140        150        160        170        180 
DSIYVFKEDE VIEYDGEFSA DTLVEFLLDV LEDPVELIEG ERELQAFENI EDEIKLIGYF 

       190        200        210        220        230        240 
KNKDSEHYKA FKEAAEEFHP YIPFFATFDS KVAKKLTLKL NEIDFYEAFM EEPVTIPDKP 

       250        260        270        280        290        300 
NSEEEIVNFV EEHRRSTLRK LKPESMYETW EDDMDGIHIV AFAEEADPDG YEFLEILKSV 

       310        320        330        340        350        360 
AQDNTDNPDL SIIWIDPDDF PLLVPYWEKT FDIDLSAPQI GVVNVTDADS VWMEMDDEED 

       370        380        390 
LPSAEELEDW LEDVLEGEIN TEDDDDEDDD DDDDD 

« Hide

References

[1]"Amino acid sequence of rabbit fast-twitch skeletal muscle calsequestrin deduced from cDNA and peptide sequencing."
Fliegel L., Ohnishi M., Carpenter M.R., Khanna V.K., Reithmeier R.A.F., McLennan D.H.
Proc. Natl. Acad. Sci. U.S.A. 84:1167-1171(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Structure of the rabbit fast-twitch skeletal muscle calsequestrin gene."
Zarain-Herzberg A., Fliegel L., Maclennan D.H.
J. Biol. Chem. 263:4807-4812(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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 29-87.
Tissue: Skeletal muscle.
[4]"Fragmentation of rabbit skeletal muscle calsequestrin: spectral and ion binding properties of the carboxyl-terminal region."
Ohnishi M., Reithmeier R.A.F.
Biochemistry 26:7458-7465(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 330-388.
Tissue: Skeletal muscle.
[5]"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.
[6]"Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum."
Wang S., Trumble W.R., Liao H., Wesson C.R., Dunker A.K., Kang C.H.
Nat. Struct. Biol. 5:476-483(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 31-375.
Tissue: Skeletal muscle.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15747 mRNA. Translation: AAA31184.1.
M22717 expand/collapse EMBL AC list , M20142, M22712, M22713, M22714, M22715, M22716 Genomic DNA. Translation: AAA31185.1.
PIRA25887. A28142.
RefSeqNP_001075737.1. NM_001082268.1.
UniGeneOcu.6275.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8YX-ray2.40A29-395[»]
3TRPX-ray1.88A29-381[»]
3TRQX-ray1.76A29-381[»]
3US3X-ray1.74A29-395[»]
3V1WX-ray1.91A29-395[»]
DisProtDP00132.
ProteinModelPortalP07221.
SMRP07221. Positions 31-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-195276.
STRING9986.ENSOCUP00000024484.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009095.

Organism-specific databases

CTD844.

Phylogenomic databases

eggNOGNOG77804.
HOGENOMHOG000049047.
HOVERGENHBG050805.

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

EvolutionaryTraceP07221.

Entry information

Entry nameCASQ1_RABIT
AccessionPrimary (citable) accession number: P07221
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: October 16, 2013
This is version 102 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