ID   CASQ2_PONAB             Reviewed;         400 AA.
AC   Q5RAN9;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Calsequestrin-2;
DE   AltName: Full=Calsequestrin, cardiac muscle isoform;
DE   Flags: Precursor;
GN   Name=CASQ2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR858976; CAH91171.1; -; mRNA.
DR   RefSeq; NP_001125686.1; NM_001132214.1.
DR   AlphaFoldDB; Q5RAN9; -.
DR   SMR; Q5RAN9; -.
DR   STRING; 9601.ENSPPYP00000001152; -.
DR   PRIDE; Q5RAN9; -.
DR   GeneID; 100172607; -.
DR   KEGG; pon:100172607; -.
DR   CTD; 845; -.
DR   eggNOG; ENOG502QU4Q; Eukaryota.
DR   InParanoid; Q5RAN9; -.
DR   OrthoDB; 1091027at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd03074; PDI_b'_Calsequestrin_C; 1.
DR   CDD; cd03066; PDI_b_Calsequestrin_middle; 1.
DR   CDD; cd03065; PDI_b_Calsequestrin_N; 1.
DR   InterPro; IPR001393; Calsequestrin.
DR   InterPro; IPR041860; Calsequestrin_C.
DR   InterPro; IPR018233; Calsequestrin_CS.
DR   InterPro; IPR041858; Calsequestrin_middle_dom.
DR   InterPro; IPR041859; Calsequestrin_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF01216; Calsequestrin; 1.
DR   SUPFAM; SSF52833; SSF52833; 3.
DR   PROSITE; PS00863; CALSEQUESTRIN_1; 1.
DR   PROSITE; PS00864; CALSEQUESTRIN_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Glycoprotein; Metal-binding; Muscle protein; Phosphoprotein;
KW   Reference proteome; Sarcoplasmic reticulum; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..400
FT                   /note="Calsequestrin-2"
FT                   /id="PRO_0000042644"
FT   REGION          365..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..400
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         282
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O09161"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   400 AA;  46387 MW;  3CEA67D628D63C9F CRC64;
     MKRTHLFIVG VYVLSSCRAE EGLNFPTYDG KDRVVSLSEK NFKQVLKKYD LLCLYYHEPV
     SSDKVAQKQF QLKEIVLELV AQVLEHKAIG FVMVDAKKEA KLAKKLGFDE EGSLYILKGD
     RTIEFDGEFA ADVLVEFLLD LIEDPVEIIS SKLEVQAFER IEDYIKLIGF FKSGDSEYYK
     AFEEAAEHFQ PYIKFFATFD KGVAKKLSLK MNEVDFYEPF MDEPIAIPNK PYTEEELVEF
     VKEHQRPTLR RLRPEEMFET WEDDLNGIHI VAFAEKSDPD GYEFLEILKQ VARDNTDNPD
     LSILWIDPDD FPLLVAYWEK TFKIDLFRPQ IGVVNVTDAD SVWMEIPDDD DLPTAEELED
     WIEDVLSGKI NTEDDDDEDD DDDNSDEEDN DDSDDDDDDE