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P07221

- CASQ1_RABIT

UniProt

P07221 - CASQ1_RABIT

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Protein

Calsequestrin-1

Gene

CASQ1

Organism
Oryctolagus cuniculus (Rabbit)
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. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca2+ ions. Regulates the release of lumenal Ca2+ via the calcium release channel RYR1; this plays an important role in triggering muscle contraction.6 Publications1 Publication

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB

GO - Biological processi

  1. protein polymerization Source: UniProtKB
  2. regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion Source: UniProtKB
  3. sarcomere organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calsequestrin-1
Alternative name(s):
Aspartactin
Calsequestrin, skeletal muscle isoform
Laminin-binding protein
Gene namesi
Name:CASQ1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Sarcoplasmic reticulum lumen 3 Publications. Mitochondrion matrix By similarity. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side 1 Publication
Note: This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells.1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB
  2. sarcoplasmic reticulum Source: UniProtKB
  3. sarcoplasmic reticulum lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 395367Calsequestrin-1PRO_0000004214Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi344 – 3441N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

Detected in skeletal muscle (at protein level). Detected in skeletal muscle.3 Publications

Interactioni

Subunit structurei

Monomer, homodimer, homotetramer and homopolymer. Can form linear homooligomers. Ca2+ ions promote oligomerization. Interacts with ASPH and TRDN.7 Publications

Protein-protein interaction databases

MINTiMINT-195276.
STRINGi9986.ENSOCUP00000024484.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni48 – 503Combined sources
Helixi51 – 577Combined sources
Beta strandi59 – 668Combined sources
Helixi73 – 9321Combined sources
Turni94 – 974Combined sources
Beta strandi98 – 1047Combined sources
Turni105 – 1084Combined sources
Helixi109 – 1157Combined sources
Beta strandi122 – 1276Combined sources
Beta strandi130 – 1334Combined sources
Helixi140 – 15112Combined sources
Beta strandi154 – 1574Combined sources
Helixi161 – 1699Combined sources
Beta strandi175 – 1795Combined sources
Helixi186 – 19813Combined sources
Turni199 – 2013Combined sources
Beta strandi204 – 2074Combined sources
Helixi210 – 2167Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi231 – 2355Combined sources
Beta strandi237 – 2404Combined sources
Helixi243 – 25210Combined sources
Beta strandi257 – 2604Combined sources
Helixi263 – 2653Combined sources
Helixi266 – 2716Combined sources
Beta strandi277 – 2826Combined sources
Helixi288 – 30316Combined sources
Turni304 – 3063Combined sources
Beta strandi312 – 3154Combined sources
Helixi317 – 3193Combined sources
Turni321 – 3233Combined sources
Helixi324 – 3318Combined sources
Beta strandi339 – 3446Combined sources
Turni345 – 3473Combined sources
Beta strandi350 – 3523Combined sources
Helixi364 – 37613Combined sources
Beta strandi377 – 3793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8YX-ray2.40A29-395[»]
3TRPX-ray1.88A29-381[»]
3TRQX-ray1.76A29-381[»]
3US3X-ray1.74A29-395[»]
3V1WX-ray1.91A29-395[»]
DisProtiDP00132.
ProteinModelPortaliP07221.
SMRiP07221. Positions 31-375.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07221.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi354 – 39542Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the calsequestrin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG77804.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiP07221.

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.

P07221-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNAADRMGAR VALLLLLVLG SPQSGVHGEE GLDFPEYDGV DRVINVNAKN
60 70 80 90 100
YKNVFKKYEV LALLYHEPPE DDKASQRQFE MEELILELAA QVLEDKGVGF
110 120 130 140 150
GLVDSEKDAA VAKKLGLTEE DSIYVFKEDE VIEYDGEFSA DTLVEFLLDV
160 170 180 190 200
LEDPVELIEG ERELQAFENI EDEIKLIGYF KNKDSEHYKA FKEAAEEFHP
210 220 230 240 250
YIPFFATFDS KVAKKLTLKL NEIDFYEAFM EEPVTIPDKP NSEEEIVNFV
260 270 280 290 300
EEHRRSTLRK LKPESMYETW EDDMDGIHIV AFAEEADPDG YEFLEILKSV
310 320 330 340 350
AQDNTDNPDL SIIWIDPDDF PLLVPYWEKT FDIDLSAPQI GVVNVTDADS
360 370 380 390
VWMEMDDEED LPSAEELEDW LEDVLEGEIN TEDDDDEDDD DDDDD
Length:395
Mass (Da):45,263
Last modified:April 1, 1988 - v1
Checksum:iE849B05AF107AFA7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti387 – 3882ED → DE AA sequence (PubMed:3427087)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15747 mRNA. Translation: AAA31184.1.
M22717
, M20142, M22712, M22713, M22714, M22715, M22716 Genomic DNA. Translation: AAA31185.1.
PIRiA28142. A25887.
RefSeqiNP_001075737.1. NM_001082268.1.
UniGeneiOcu.6275.

Genome annotation databases

GeneIDi100009095.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15747 mRNA. Translation: AAA31184.1 .
M22717
, M20142 , M22712 , M22713 , M22714 , M22715 , M22716 Genomic DNA. Translation: AAA31185.1 .
PIRi A28142. A25887.
RefSeqi NP_001075737.1. NM_001082268.1.
UniGenei Ocu.6275.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A8Y X-ray 2.40 A 29-395 [» ]
3TRP X-ray 1.88 A 29-381 [» ]
3TRQ X-ray 1.76 A 29-381 [» ]
3US3 X-ray 1.74 A 29-395 [» ]
3V1W X-ray 1.91 A 29-395 [» ]
DisProti DP00132.
ProteinModelPortali P07221.
SMRi P07221. Positions 31-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-195276.
STRINGi 9986.ENSOCUP00000024484.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009095.

Organism-specific databases

CTDi 844.

Phylogenomic databases

eggNOGi NOG77804.
HOGENOMi HOG000049047.
HOVERGENi HBG050805.
InParanoidi P07221.

Miscellaneous databases

EvolutionaryTracei P07221.

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. "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, TISSUE SPECIFICITY.
  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. 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, FUNCTION, TISSUE SPECIFICITY.
    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: LACK OF PHOSPHORYLATION.
  6. "Ca(2+)-induced folding and aggregation of skeletal muscle sarcoplasmic reticulum calsequestrin. The involvement of the trifluoperazine-binding site."
    He Z., Dunker A.K., Wesson C.R., Trumble W.R.
    J. Biol. Chem. 268:24635-24641(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.
  7. "Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation."
    Beard N.A., Casarotto M.G., Wei L., Varsanyi M., Laver D.R., Dulhunty A.F.
    Biophys. J. 88:3444-3454(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TRDN AND ASPH.
  8. "Phosphorylation of skeletal muscle calsequestrin enhances its Ca2+ binding capacity and promotes its association with junctin."
    Beard N.A., Wei L., Cheung S.N., Kimura T., Varsanyi M., Dulhunty A.F.
    Cell Calcium 44:363-373(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TRDN AND ASPH.
  9. "Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin."
    Wei L., Gallant E.M., Dulhunty A.F., Beard N.A.
    Int. J. Biochem. Cell Biol. 41:2214-2224(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRDN AND ASPH, FUNCTION.
  10. "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, SUBUNIT.
    Tissue: Skeletal muscle.
  11. "Glycosylation of skeletal calsequestrin: implications for its function."
    Sanchez E.J., Lewis K.M., Munske G.R., Nissen M.S., Kang C.
    J. Biol. Chem. 287:3042-3050(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 29-395 IN COMPLEX WITH CALCIUM, FUNCTION, SUBUNIT, LACK OF PHOSPHORYLATION AT THR-381, GLYCOSYLATION AT ASN-344.
  12. "High-capacity Ca2+ binding of human skeletal calsequestrin."
    Sanchez E.J., Lewis K.M., Danna B.R., Kang C.
    J. Biol. Chem. 287:11592-11601(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 29-381 IN COMPLEX WITH CALCIUM, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiCASQ1_RABIT
AccessioniPrimary (citable) accession number: P07221
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 26, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Phosphorylated at very low, substoichiometric levels when isolated from skeletal muscle sarcoplasmic reticulum (PubMed:1985907). Can be phosphorylated by CK2 at Thr-381 (in vitro), albeit with low efficiency, suggesting this is not a physiological CK2 substrate (PubMed:1985907). Not phosphorylated at Thr-381 (PubMed:22170046).2 PublicationsCurated

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