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P12637

- CASQ2_CANFA

UniProt

P12637 - CASQ2_CANFA

Protein

Calsequestrin-2

Gene

CASQ2

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      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.1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: Ensembl
    2. protein binding Source: BHF-UCL

    GO - Biological processi

    1. cardiac muscle contraction Source: Ensembl
    2. cellular response to caffeine Source: Ensembl
    3. negative regulation of potassium ion transmembrane transporter activity Source: Ensembl
    4. negative regulation of potassium ion transport Source: Ensembl
    5. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    6. protein polymerization Source: Ensembl
    7. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: Ensembl
    8. regulation of cell communication by electrical coupling Source: Ensembl
    9. regulation of heart rate Source: Ensembl
    10. regulation of membrane repolarization Source: Ensembl
    11. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    12. sequestering of calcium ion Source: Ensembl

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_219568. Stimuli-sensing channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calsequestrin-2
    Alternative name(s):
    Calsequestrin, cardiac muscle isoform
    Gene namesi
    Name:CASQ2
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. sarcoplasmic reticulum Source: BHF-UCL
    2. sarcoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Sarcoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 410391Calsequestrin-2PRO_0000004217Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
    Modified residuei397 – 3971Phosphoserine; by CK21 Publication
    Modified residuei401 – 4011Phosphoserine; by CK21 Publication
    Modified residuei405 – 4051Phosphoserine; by CK21 Publication

    Post-translational modificationi

    Phosphorylation in the C-terminus, probably by CK2, moderately increases calcium buffering capacity.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP12637.

    Interactioni

    Subunit structurei

    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. Interacts with ASPH and TRDN By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000014348.

    Structurei

    Secondary structure

    1
    410
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 373
    Helixi39 – 468
    Beta strandi50 – 578
    Beta strandi62 – 643
    Helixi68 – 8316
    Helixi84 – 863
    Beta strandi87 – 959
    Turni96 – 994
    Helixi100 – 1067
    Beta strandi113 – 1186
    Beta strandi121 – 1255
    Helixi131 – 1399
    Beta strandi145 – 1484
    Helixi152 – 1609
    Beta strandi166 – 1705
    Helixi177 – 18812
    Turni189 – 1924
    Beta strandi193 – 1986
    Helixi201 – 2077
    Beta strandi214 – 2174
    Beta strandi228 – 2314
    Helixi234 – 24411
    Beta strandi248 – 2514
    Turni254 – 2563
    Helixi257 – 2626
    Beta strandi265 – 2739
    Helixi279 – 29416
    Helixi295 – 2973
    Beta strandi303 – 3064
    Helixi308 – 3103
    Helixi312 – 32110
    Beta strandi330 – 33910
    Beta strandi341 – 3444
    Helixi355 – 36612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SJIX-ray2.40A/B22-371[»]
    ProteinModelPortaliP12637.
    SMRiP12637. Positions 22-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12637.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni221 – 24222Calcium regulated hydrophobic siteAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi219 – 25436Pro-richAdd
    BLAST
    Compositional biasi372 – 41039Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the calsequestrin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG77804.
    HOGENOMiHOG000049047.
    HOVERGENiHBG050805.
    InParanoidiP12637.
    OrthoDBiEOG725DHM.

    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.

    P12637-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRTHLFIAG LYLLASCRAE EGLNFPTYDG KDRVVSLTEK NFKQVLKKYD    50
    VLCLYYHESV SSDKVAQKQF QLKEIVLELV AQVLEHKDIG FVMVDAKKEA 100
    KLAKKLGFDE EGSLYVLKGD RTIEFDGEFA ADVLVEFLLD LIEDPVEIIN 150
    SKLEVQAFER IEDQIKLIGF FKSEESEYYK AFEEAAEHFQ PYIKFFATFD 200
    KGVAKKLSLK MNEVDFYEPF MDEPIAIPDK PYTEEELVEF VKEHQRPTLR 250
    RLRPEDMFET WEDDLNGIHI VAFAERSDPD GYEFLEILKQ VARDNTDNPD 300
    LSIVWIDPDD FPLLVAYWEK TFKIDLFKPQ IGVVNVTDAD SVWMEIPDDD 350
    DLPTAEELED WIEDVLSGKI NTEDDDNEEG DDGDDDEDDD DDDGNNSDEE 400
    SNDDSDDDDE 410
    Length:410
    Mass (Da):47,417
    Last modified:October 1, 1989 - v1
    Checksum:iFCA99A8D7E7ABB82
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711Q → E AA sequence (PubMed:3427023)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03766 mRNA. Translation: AAA30833.1.
    PIRiA28071.
    A39040.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03766 mRNA. Translation: AAA30833.1 .
    PIRi A28071.
    A39040.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SJI X-ray 2.40 A/B 22-371 [» ]
    ProteinModelPortali P12637.
    SMRi P12637. Positions 22-370.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000014348.

    Proteomic databases

    PaxDbi P12637.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG77804.
    HOGENOMi HOG000049047.
    HOVERGENi HBG050805.
    InParanoidi P12637.
    OrthoDBi EOG725DHM.

    Enzyme and pathway databases

    Reactomei REACT_219568. Stimuli-sensing channels.

    Miscellaneous databases

    EvolutionaryTracei P12637.
    NextBioi 20857578.

    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. "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. 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.

    Entry informationi

    Entry nameiCASQ2_CANFA
    AccessioniPrimary (citable) accession number: P12637
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 118 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