ID   CASQ2_PIG               Reviewed;         160 AA.
AC   O18934;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Calsequestrin-2;
DE   AltName: Full=Calsequestrin, cardiac muscle isoform;
DE   Flags: Fragment;
GN   Name=CASQ2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Canty J.M., Young R.F., Fallavollita J.A.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-
CC       binding protein and thus acts as an internal calcium store in muscle.
CC       Calcium ions are bound by clusters of acidic residues at the protein
CC       surface, especially at the interface between subunits. Can bind around
CC       60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium
CC       release channel RYR2; this plays an important role in triggering muscle
CC       contraction. Plays a role in excitation-contraction coupling in the
CC       heart and in regulating the rate of heart beats.
CC       {ECO:0000250|UniProtKB:O14958}.
CC   -!- SUBUNIT: Monomer, homodimer and homooligomer. Mostly monomeric in the
CC       absence of calcium. Forms higher oligomers in a calcium-dependent
CC       manner. Dimers associate to form tetramers, that then form linear
CC       homomer chains. Interacts with ASPH and TRDN (By similarity).
CC       {ECO:0000250|UniProtKB:O14958}.
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:O09161}. Note=This isoform of calsequestrin
CC       occurs in the sarcoplasmic reticulum's terminal cisternae luminal
CC       spaces of cardiac and slow skeletal muscle cells.
CC       {ECO:0000250|UniProtKB:O09161}.
CC   -!- PTM: Phosphorylation in the C-terminus, probably by CK2, moderately
CC       increases calcium buffering capacity. {ECO:0000250|UniProtKB:O14958}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O14958}.
CC   -!- SIMILARITY: Belongs to the calsequestrin family. {ECO:0000305}.
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DR   EMBL; AF034612; AAB87570.1; -; mRNA.
DR   AlphaFoldDB; O18934; -.
DR   SMR; O18934; -.
DR   STRING; 9823.ENSSSCP00000007195; -.
DR   PaxDb; O18934; -.
DR   PeptideAtlas; O18934; -.
DR   eggNOG; ENOG502QU4Q; Eukaryota.
DR   HOGENOM; CLU_036303_1_0_1; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; O18934; SS.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0033018; C:sarcoplasmic reticulum lumen; IBA:GO_Central.
DR   GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IBA:GO_Central.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   CDD; cd03066; PDI_b_Calsequestrin_middle; 1.
DR   InterPro; IPR001393; Calsequestrin.
DR   InterPro; IPR041858; Calsequestrin_middle_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF01216; Calsequestrin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Metal-binding; Muscle protein; Phosphoprotein; Reference proteome;
KW   Sarcoplasmic reticulum.
FT   CHAIN           <1..>160
FT                   /note="Calsequestrin-2"
FT                   /id="PRO_0000144073"
FT   NON_TER         1
FT   NON_TER         160
SQ   SEQUENCE   160 AA;  18990 MW;  0938F3ABFBA316C6 CRC64;
     FNEEGSLYIL KGDRTIEFDG EFAADVLVEF LLDLIEDPVE IINSKLEVQA FERIEDHIKL
     IGFFKSEDSE YYKAFEEAAE HFQPYIKFFA TFDKGVAKKL SLKMNEVDFY EPFMEEPIVI
     PDKPYTEEEI VEFVKEHQRP TLRRLRPEDM FETWEDNLNG