P12637 (CASQ2_CANFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calsequestrin-2

Alternative name(s):
Calsequestrin, cardiac muscle isoform

Gene names

Name:

CASQ2

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis › Canis lupus

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 CASQ1) binds around 80 Ca2+ ions, while the cardiac 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 By similarity.
Subcellular location	Sarcoplasmic reticulum lumen. Note: This isoform of calsequestrin 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 component	Sarcoplasmic reticulum
Domain	Signal
Ligand	Calcium
Molecular function	Muscle protein
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to caffeine Inferred from electronic annotation. Source: Compara negative regulation of potassium ion transmembrane transporter activity Inferred from electronic annotation. Source: Compara negative regulation of potassium ion transport Inferred from electronic annotation. Source: Compara negative regulation of ryanodine-sensitive calcium-release channel activity Inferred from direct assay PubMed 15041652. Source: BHF-UCL regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Inferred from electronic annotation. Source: Compara regulation of cell communication by electrical coupling Inferred from electronic annotation. Source: Compara regulation of heart rate Inferred from electronic annotation. Source: Compara regulation of membrane repolarization Inferred from electronic annotation. Source: Compara 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: Compara
Cellular_component	Z disc Inferred from electronic annotation. Source: Compara sarcoplasmic reticulum Inferred from direct assay PubMed 9287354. Source: BHF-UCL sarcoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.2

Chain

20 – 410

391

Calsequestrin-2

PRO_0000004217

Regions

Region

221 – 242

22

Calcium regulated hydrophobic site

Compositional bias

219 – 254

36

Pro-rich

Compositional bias

372 – 410

39

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

397

1

Phosphoserine; by CK2

Modified residue

401

1

Phosphoserine; by CK2

Modified residue

405

1

Phosphoserine; by CK2

Glycosylation

335

1

N-linked (GlcNAc...) Potential

Glycosylation

395

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

71

1

Q → E AA sequence Ref.2

Secondary structure

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410

Helix Strand Turn

Details...

Beta strand

35 – 37

3

Helix

39 – 46

8

Beta strand

50 – 57

8

Beta strand

62 – 64

3

Helix

68 – 83

16

Helix

84 – 86

3

Beta strand

87 – 95

9

Turn

96 – 99

4

Helix

100 – 106

7

Beta strand

113 – 118

6

Beta strand

121 – 125

5

Helix

131 – 139

9

Beta strand

145 – 148

4

Helix

152 – 160

9

Beta strand

166 – 170

5

Helix

177 – 188

12

Turn

189 – 192

4

Beta strand

193 – 198

6

Helix

201 – 207

7

Beta strand

214 – 217

4

Beta strand

228 – 231

4

Helix

234 – 244

11

Beta strand

248 – 251

4

Turn

254 – 256

3

Helix

257 – 262

6

Beta strand

265 – 273

9

Helix

279 – 294

16

Helix

295 – 297

3

Beta strand

303 – 306

4

Helix

308 – 310

3

Helix

312 – 321

10

Beta strand

330 – 339

10

Beta strand

341 – 344

4

Helix

355 – 366

12

Sequences

	Sequence		Length	Mass (Da)
	P12637 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: FCA99A8D7E7ABB82	FASTA	410	47,417
	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

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.

PIR

A28071.
A39040.

RefSeq

XP_540252.3. XM_540252.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SJI	X-ray	2.40	A/B	22-371	[»]

ProteinModelPortal

P12637.

SMR

P12637. Positions 22-370.

ModBase

Search...

Protein-protein interaction databases

STRING

9615.ENSCAFP00000014348.

Proteomic databases

PaxDb

P12637.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

483134.

KEGG

cfa:483134.

Organism-specific databases

CTD

845.

Phylogenomic databases

eggNOG

NOG77804.

HOGENOM

HOG000049047.

HOVERGEN

HBG050805.

InParanoid

P12637.

OrthoDB

EOG4W0XD8.

Family and domain databases

Gene3D

3.40.30.10. 3 hits.

InterPro

IPR001393. Calsequestrin.
IPR018233. Calsequestrin_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

PANTHER

PTHR10033. PTHR10033. 1 hit.

Pfam

PF01216. Calsequestrin. 1 hit.
[Graphical view]

PRINTS

PR00312. CALSEQUESTRN.

SUPFAM

SSF52833. Thiordxn-like_fd. 3 hits.

PROSITE

PS00863. CALSEQUESTRIN_1. 1 hit.
PS00864. CALSEQUESTRIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P12637.

NextBio

20857578.

Entry information

Entry name

CASQ2_CANFA

Accession

Primary (citable) accession number: P12637

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	April 3, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program