CASQ2_RAT
ID CASQ2_RAT Reviewed; 413 AA.
AC P51868; O09177; Q6IMX1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Calsequestrin-2;
DE AltName: Full=Calsequestrin, cardiac muscle isoform;
DE Flags: Precursor;
GN Name=Casq2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart muscle;
RA Aquilla T.T., Rovner A.S.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 20-30, TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=Wistar; TISSUE=Vas deferens;
RX PubMed=8042990; DOI=10.1042/bj3010465;
RA Volpe P., Martini A., Furlan S., Meldolesi J.;
RT "Calsequestrin is a component of smooth muscles: the skeletal- and cardiac-
RT muscle isoforms are both present, although in highly variable amounts and
RT ratios.";
RL Biochem. J. 301:465-469(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-413.
RC STRAIN=Sprague-Dawley;
RA Rodriguez M.M., Chen C., Smith B., Mochly-Rosen D.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION BY CK2.
RX PubMed=21431367; DOI=10.1007/s11010-011-0777-6;
RA McFarland T.P., Sleiman N.H., Yaeger D.B., Cala S.E.;
RT "The cytosolic protein kinase CK2 phosphorylates cardiac calsequestrin in
RT intact cells.";
RL Mol. Cell. Biochem. 353:81-91(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-282; SER-398 AND SER-405, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:8042990). Calcium ions are bound by clusters of acidic residues
CC at the protein surface, especially at the interface between subunits.
CC Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+)
CC via the calcium release channel RYR2; this plays an important role in
CC triggering muscle contraction. Plays a role in excitation-contraction
CC coupling in the heart and in regulating the rate of heart beats (By
CC similarity). {ECO:0000250|UniProtKB:O14958,
CC ECO:0000269|PubMed:8042990}.
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 -!- TISSUE SPECIFICITY: Detected in stomach and vas deferens (at protein
CC level). {ECO:0000269|PubMed:8042990}.
CC -!- PTM: Phosphorylation in the C-terminus, probably by CK2, moderately
CC increases calcium buffering capacity. {ECO:0000269|PubMed:21431367}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O14958}.
CC -!- SIMILARITY: Belongs to the calsequestrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72547.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U33287; AAA75480.1; -; mRNA.
DR EMBL; BC072547; AAH72547.1; ALT_INIT; mRNA.
DR EMBL; AF001334; AAB58746.1; -; Genomic_DNA.
DR RefSeq; NP_058827.3; NM_017131.2.
DR AlphaFoldDB; P51868; -.
DR SMR; P51868; -.
DR BioGRID; 247887; 2.
DR IntAct; P51868; 5.
DR MINT; P51868; -.
DR STRING; 10116.ENSRNOP00000021846; -.
DR GlyGen; P51868; 1 site.
DR iPTMnet; P51868; -.
DR PhosphoSitePlus; P51868; -.
DR PaxDb; P51868; -.
DR PRIDE; P51868; -.
DR GeneID; 29209; -.
DR KEGG; rno:29209; -.
DR UCSC; RGD:2276; rat.
DR CTD; 845; -.
DR RGD; 2276; Casq2.
DR eggNOG; ENOG502QU4Q; Eukaryota.
DR InParanoid; P51868; -.
DR OrthoDB; 1091027at2759; -.
DR PhylomeDB; P51868; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR PRO; PR:P51868; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030314; C:junctional membrane complex; ISO:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; ISO:RGD.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0140314; F:calcium ion sequestering activity; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0005080; F:protein kinase C binding; IDA:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0071313; P:cellular response to caffeine; ISO:RGD.
DR GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; ISO:RGD.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IMP:BHF-UCL.
DR GO; GO:0051258; P:protein polymerization; ISO:RGD.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IMP:BHF-UCL.
DR GO; GO:0010649; P:regulation of cell communication by electrical coupling; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0060306; P:regulation of membrane repolarization; ISO:RGD.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR GO; GO:0051208; P:sequestering of calcium ion; ISO:RGD.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Glycoprotein; Metal-binding;
KW Muscle protein; Phosphoprotein; Reference proteome; Sarcoplasmic reticulum;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8042990"
FT CHAIN 20..413
FT /note="Calsequestrin-2"
FT /id="PRO_0000004221"
FT REGION 365..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..413
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 50..52
FT /note="DLL -> ARV (in Ref. 4; AAB58746)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..211
FT /note="SLKM -> FLEV (in Ref. 1; AAA75480)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="P -> R (in Ref. 2; AAH72547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 47839 MW; F03B6C7C3EB19D80 CRC64;
MKRIYLLVVG LYLLSFSRAE EGLNFPTYDG KDRVVSLSEK NLKQVLKRYD LLCLYYHEPV
SSDKVAQKQF QLKEIVLELV AQVLEHKNIG FVMVDSRKEA KLAKRLGFSE EGSLYVLKGG
RTIEFDGEFA ADVLVEFLLD LIEDPVEIVN NKLEVQAFER IEDQIKLLGF FKNEDSEYYK
AFQEAAEHFQ PYIKFFATFD KGVAKKLSLK MNEVGFYEPF MDEPSVIPNK PYTEEELVEF
VKEHQRPTLR PLRPEDMFET WEDDLNGIHI VAFAEKSDPD GYEFLEILKQ VARDNTDNPD
LSILWIDPDD FPLLVAYWEK TFKIDLFKPQ IGVVNVTDAD SVWMEIPDDD DLPTAEELED
WIEDVLSGKI NTEDDDNEDE DDDGDNDNDD DDDDDDNSDE DNDDSDDDDD DDE
