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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: 4 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. 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.

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium

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

GO - Cellular componenti

  1. sarcoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi344 – 3441N-linked (GlcNAc...)1 Publication
Modified residuei381 – 3811Phosphothreonine; by CK2

Keywords - PTMi

Glycoprotein, Phosphoprotein

Interactioni

Protein-protein interaction databases

MINTiMINT-195276.
STRINGi9986.ENSOCUP00000024484.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP07221.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni231 – 26535Calcium regulated hydrophobic site
Add
BLAST
Regioni231 – 26535Trifluoperazine binding site
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the calsequestrin family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG77804.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.

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

MNAADRMGAR VALLLLLVLG SPQSGVHGEE GLDFPEYDGV DRVINVNAKN    50
YKNVFKKYEV LALLYHEPPE DDKASQRQFE MEELILELAA QVLEDKGVGF 100
GLVDSEKDAA VAKKLGLTEE DSIYVFKEDE VIEYDGEFSA DTLVEFLLDV 150
LEDPVELIEG ERELQAFENI EDEIKLIGYF KNKDSEHYKA FKEAAEEFHP 200
YIPFFATFDS KVAKKLTLKL NEIDFYEAFM EEPVTIPDKP NSEEEIVNFV 250
EEHRRSTLRK LKPESMYETW EDDMDGIHIV AFAEEADPDG YEFLEILKSV 300
AQDNTDNPDL SIIWIDPDDF PLLVPYWEKT FDIDLSAPQI GVVNVTDADS 350
VWMEMDDEED LPSAEELEDW LEDVLEGEIN TEDDDDEDDD DDDDD 395
Length:395
Mass (Da):45,263
Last modified:April 1, 1988 - v1
Checksum:iE849B05AF107AFA7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti387 – 3882ED → DE AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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...

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.

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.
  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.
    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.

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: October 16, 2013
This is version 102 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

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