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P07221

- CASQ1_RABIT

UniProt

P07221 - CASQ1_RABIT

Protein

Calsequestrin-1

Gene

CASQ1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    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.By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    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

    Keywords - Cellular componenti

    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
    Modified residuei381 – 3811Phosphothreonine; by CK21 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Interactioni

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07221.

    Family & Domainsi

    Region

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

    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.

    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

    Experimental Info

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

    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...
    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.

    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 1, 2014
    This is version 103 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