Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calsequestrin-1

Gene

CASQ1

Organism
Oryctolagus cuniculus (Rabbit)
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. 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.1 Publication6 Publications

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB

GO - Biological processi

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
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 281 PublicationAdd BLAST28
ChainiPRO_000000421429 – 395Calsequestrin-1Add BLAST367

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei37PhosphotyrosineBy similarity1
Modified residuei75PhosphoserineBy similarity1
Modified residuei118PhosphothreonineBy similarity1
Modified residuei210PhosphoserineBy similarity1
Modified residuei291PhosphotyrosineBy similarity1
Glycosylationi344N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP07221.

PTM databases

iPTMnetiP07221.

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

1395
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni48 – 50Combined sources3
Helixi51 – 57Combined sources7
Beta strandi59 – 66Combined sources8
Helixi73 – 93Combined sources21
Turni94 – 97Combined sources4
Beta strandi98 – 104Combined sources7
Turni105 – 108Combined sources4
Helixi109 – 115Combined sources7
Beta strandi122 – 127Combined sources6
Beta strandi130 – 133Combined sources4
Helixi140 – 151Combined sources12
Beta strandi154 – 157Combined sources4
Helixi161 – 169Combined sources9
Beta strandi175 – 179Combined sources5
Helixi186 – 198Combined sources13
Turni199 – 201Combined sources3
Beta strandi204 – 207Combined sources4
Helixi210 – 216Combined sources7
Beta strandi223 – 226Combined sources4
Beta strandi231 – 235Combined sources5
Beta strandi237 – 240Combined sources4
Helixi243 – 252Combined sources10
Beta strandi257 – 260Combined sources4
Helixi263 – 265Combined sources3
Helixi266 – 271Combined sources6
Beta strandi277 – 282Combined sources6
Helixi288 – 303Combined sources16
Turni304 – 306Combined sources3
Beta strandi312 – 315Combined sources4
Helixi317 – 319Combined sources3
Turni321 – 323Combined sources3
Helixi324 – 331Combined sources8
Beta strandi339 – 344Combined sources6
Turni345 – 347Combined sources3
Beta strandi350 – 352Combined sources3
Helixi364 – 376Combined sources13
Beta strandi377 – 379Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07221.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi354 – 395Asp/Glu-rich (acidic)Add BLAST42

Sequence similaritiesi

Belongs to the calsequestrin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IGY5. Eukaryota.
ENOG4111R2M. LUCA.
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)DescriptionActionsGraphical viewLength
Sequence conflicti387 – 388ED → DE AA sequence (PubMed:3427087).Curated2

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.
KEGGiocu:100009095.

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.
PIRiA28142. A25887.
RefSeqiNP_001075737.1. NM_001082268.1.
UniGeneiOcu.6275.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-195276.
STRINGi9986.ENSOCUP00000024484.

PTM databases

iPTMnetiP07221.

Proteomic databases

PRIDEiP07221.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009095.
KEGGiocu:100009095.

Organism-specific databases

CTDi844.

Phylogenomic databases

eggNOGiENOG410IGY5. Eukaryota.
ENOG4111R2M. LUCA.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiP07221.

Miscellaneous databases

EvolutionaryTraceiP07221.

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 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 2, 2016
This is version 116 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).Curated2 Publications

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.