ID   CASQ1_CANLF             Reviewed;          56 AA.
AC   P31236;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Calsequestrin-1;
DE   AltName: Full=Calsequestrin, skeletal muscle isoform;
DE   Flags: Fragment;
GN   Name=CASQ1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3427023; DOI=10.1021/bi00394a038;
RA   Slupsky J.R., Ohnishi M., Carpenter M.R., Reithmeier R.A.F.;
RT   "Characterization of cardiac calsequestrin.";
RL   Biochemistry 26:6539-6544(1987).
RN   [2]
RP   FUNCTION, AND CALCIUM AFFINITY.
RX   PubMed=14871888; DOI=10.1074/jbc.m311553200;
RA   Park H., Park I.Y., Kim E., Youn B., Fields K., Dunker A.K., Kang C.;
RT   "Comparing skeletal and cardiac calsequestrin structures and their calcium
RT   binding: a proposed mechanism for coupled calcium binding and protein
RT   polymerization.";
RL   J. Biol. Chem. 279:18026-18033(2004).
CC   -!- FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-
CC       binding protein and thus acts as an internal calcium store in muscle
CC       (PubMed:14871888). Calcium ions are bound by clusters of acidic
CC       residues at the protein surface, often at the interface between
CC       subunits. Can bind around 80 Ca(2+) ions. Regulates the release of
CC       lumenal Ca(2+) via the calcium release channel RYR1; this plays an
CC       important role in triggering muscle contraction (By similarity).
CC       Negatively regulates store-operated Ca(2+) entry (SOCE) activity (By
CC       similarity). {ECO:0000250|UniProtKB:O09165,
CC       ECO:0000250|UniProtKB:P07221, ECO:0000250|UniProtKB:P31415,
CC       ECO:0000269|PubMed:14871888}.
CC   -!- SUBUNIT: Monomer; increases in response to a depletion of intracellular
CC       calcium. Homodimer. Homotetramer and homopolymer. Can form linear
CC       homooligomers. Ca(2+) ions promote oligomerization. Interacts (via C-
CC       terminal end and preferentially with the monomeric form) with STIM1;
CC       this interaction increases in response to a depletion of intracellular
CC       calcium, decreases both STIM1 aggregation and clustering, interaction
CC       of STIM1 with ORAI1 and store-operated Ca(2+) entry (SOCE) activity.
CC       Interacts with ASPH and TRDN. {ECO:0000250|UniProtKB:P07221,
CC       ECO:0000250|UniProtKB:P31415}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:P07221}. Sarcoplasmic reticulum membrane;
CC       Peripheral membrane protein; Lumenal side
CC       {ECO:0000250|UniProtKB:P07221}. Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:O09165}. Note=This isoform of calsequestrin
CC       occurs in the sarcoplasmic reticulum's terminal cisternae luminal
CC       spaces of fast skeletal muscle cells. Preferentially forms linear and
CC       round aggregates in the endoplasmic reticulum (ER) of resting cells. In
CC       a minority of cells, homogeneously detected in the ER lumen.
CC       Colocalizes with STIM1 at endoplasmic reticulum in response to a
CC       depletion of intracellular calcium. {ECO:0000250|UniProtKB:P07221,
CC       ECO:0000250|UniProtKB:P31415}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P07221}.
CC   -!- SIMILARITY: Belongs to the calsequestrin family. {ECO:0000305}.
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DR   PIR; B27499; B27499.
DR   STRING; 9612.ENSCAFP00000018363; -.
DR   eggNOG; ENOG502QQUJ; Eukaryota.
DR   InParanoid; P31236; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0033018; C:sarcoplasmic reticulum lumen; IBA:GO_Central.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR   GO; GO:1901341; P:positive regulation of store-operated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   GO; GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; IBA:GO_Central.
DR   GO; GO:2001256; P:regulation of store-operated calcium entry; ISS:UniProtKB.
DR   InterPro; IPR001393; Calsequestrin.
DR   InterPro; IPR018233; Calsequestrin_CS.
DR   Pfam; PF01216; Calsequestrin; 1.
DR   PROSITE; PS00863; CALSEQUESTRIN_1; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW   Metal-binding; Mitochondrion; Muscle protein; Phosphoprotein;
KW   Reference proteome; Sarcoplasmic reticulum.
FT   CHAIN           1..>56
FT                   /note="Calsequestrin-1"
FT                   /id="PRO_0000144071"
FT   MOD_RES         9
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P19633"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19633"
FT   NON_TER         56
SQ   SEQUENCE   56 AA;  6615 MW;  5DFF02D3CD949E96 CRC64;
     EEGLDFPEYD GVDRVVNVNA KNYKNVFKKY EVLALLYHEP PXXDKASQRQ FDMEEL