CASQ1_RABIT
ID CASQ1_RABIT Reviewed; 395 AA.
AC P07221;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Calsequestrin-1;
DE AltName: Full=Aspartactin;
DE AltName: Full=Calsequestrin, skeletal muscle isoform;
DE AltName: Full=Laminin-binding protein;
DE Flags: Precursor;
GN Name=CASQ1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RX PubMed=3469659; DOI=10.1073/pnas.84.5.1167;
RA Fliegel L., Ohnishi M., Carpenter M.R., Khanna V.K., Reithmeier R.A.F.,
RA McLennan D.H.;
RT "Amino acid sequence of rabbit fast-twitch skeletal muscle calsequestrin
RT deduced from cDNA and peptide sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1167-1171(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2832408; DOI=10.1016/s0021-9258(18)68857-x;
RA Zarain-Herzberg A., Fliegel L., Maclennan D.H.;
RT "Structure of the rabbit fast-twitch skeletal muscle calsequestrin gene.";
RL J. Biol. Chem. 263:4807-4812(1988).
RN [3]
RP PROTEIN SEQUENCE OF 29-87.
RC TISSUE=Skeletal muscle;
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 [4]
RP PROTEIN SEQUENCE OF 330-388, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=3427087; DOI=10.1021/bi00397a039;
RA Ohnishi M., Reithmeier R.A.F.;
RT "Fragmentation of rabbit skeletal muscle calsequestrin: spectral and ion
RT binding properties of the carboxyl-terminal region.";
RL Biochemistry 26:7458-7465(1987).
RN [5]
RP LACK OF PHOSPHORYLATION.
RX PubMed=1985907; DOI=10.1016/s0021-9258(18)52447-9;
RA Cala S.E., Jones L.R.;
RT "Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by
RT casein kinase II. Demonstration of a cluster of unique rapidly
RT phosphorylated sites in cardiac calsequestrin.";
RL J. Biol. Chem. 266:391-398(1991).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=8227022; DOI=10.1016/s0021-9258(19)74513-x;
RA He Z., Dunker A.K., Wesson C.R., Trumble W.R.;
RT "Ca(2+)-induced folding and aggregation of skeletal muscle sarcoplasmic
RT reticulum calsequestrin. The involvement of the trifluoperazine-binding
RT site.";
RL J. Biol. Chem. 268:24635-24641(1993).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TRDN AND ASPH.
RX PubMed=15731387; DOI=10.1529/biophysj.104.051441;
RA Beard N.A., Casarotto M.G., Wei L., Varsanyi M., Laver D.R., Dulhunty A.F.;
RT "Regulation of ryanodine receptors by calsequestrin: effect of high luminal
RT Ca2+ and phosphorylation.";
RL Biophys. J. 88:3444-3454(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH TRDN AND
RP ASPH.
RX PubMed=19230141; DOI=10.1016/j.ceca.2008.01.005;
RA Beard N.A., Wei L., Cheung S.N., Kimura T., Varsanyi M., Dulhunty A.F.;
RT "Phosphorylation of skeletal muscle calsequestrin enhances its Ca2+ binding
RT capacity and promotes its association with junctin.";
RL Cell Calcium 44:363-373(2008).
RN [9]
RP INTERACTION WITH TRDN AND ASPH, AND FUNCTION.
RX PubMed=19398037; DOI=10.1016/j.biocel.2009.04.017;
RA Wei L., Gallant E.M., Dulhunty A.F., Beard N.A.;
RT "Junctin and triadin each activate skeletal ryanodine receptors but junctin
RT alone mediates functional interactions with calsequestrin.";
RL Int. J. Biochem. Cell Biol. 41:2214-2224(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 31-375, AND SUBUNIT.
RC TISSUE=Skeletal muscle;
RX PubMed=9628486; DOI=10.1038/nsb0698-476;
RA Wang S., Trumble W.R., Liao H., Wesson C.R., Dunker A.K., Kang C.H.;
RT "Crystal structure of calsequestrin from rabbit skeletal muscle
RT sarcoplasmic reticulum.";
RL Nat. Struct. Biol. 5:476-483(1998).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 29-395 IN COMPLEX WITH CALCIUM,
RP FUNCTION, SUBUNIT, LACK OF PHOSPHORYLATION AT THR-381, AND GLYCOSYLATION AT
RP ASN-344.
RX PubMed=22170046; DOI=10.1074/jbc.m111.326363;
RA Sanchez E.J., Lewis K.M., Munske G.R., Nissen M.S., Kang C.;
RT "Glycosylation of skeletal calsequestrin: implications for its function.";
RL J. Biol. Chem. 287:3042-3050(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 29-381 IN COMPLEX WITH CALCIUM,
RP FUNCTION, AND SUBUNIT.
RX PubMed=22337878; DOI=10.1074/jbc.m111.335075;
RA Sanchez E.J., Lewis K.M., Danna B.R., Kang C.;
RT "High-capacity Ca2+ binding of human skeletal calsequestrin.";
RL J. Biol. Chem. 287:11592-11601(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 Calcium ions are bound by clusters of acidic residues at the protein
CC surface, often at the interface between subunits. Can bind around 80
CC Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium
CC release channel RYR1; this plays an important role in triggering muscle
CC contraction. Negatively regulates store-operated Ca(2+) entry (SOCE)
CC activity (By similarity). {ECO:0000250|UniProtKB:P31415,
CC ECO:0000269|PubMed:15731387, ECO:0000269|PubMed:19230141,
CC ECO:0000269|PubMed:19398037, ECO:0000269|PubMed:22170046,
CC ECO:0000269|PubMed:3427087, ECO:0000269|PubMed:8227022,
CC ECO:0000303|PubMed:22337878}.
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 (By
CC similarity). Interacts with ASPH and TRDN (PubMed:15731387,
CC PubMed:19230141, PubMed:19398037). {ECO:0000250|UniProtKB:P31415,
CC ECO:0000269|PubMed:15731387, ECO:0000269|PubMed:19230141,
CC ECO:0000269|PubMed:19398037, ECO:0000269|PubMed:22170046,
CC ECO:0000269|PubMed:22337878, ECO:0000269|PubMed:8227022,
CC ECO:0000269|PubMed:9628486}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum
CC {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum lumen
CC {ECO:0000269|PubMed:15731387, ECO:0000269|PubMed:19230141,
CC ECO:0000269|PubMed:8227022}. Mitochondrion matrix
CC {ECO:0000250|UniProtKB:O09165}. Sarcoplasmic reticulum membrane;
CC Peripheral membrane protein; Lumenal side
CC {ECO:0000269|PubMed:15731387}. Note=This isoform of calsequestrin
CC occurs in the sarcoplasmic reticulum's terminal cisternae luminal
CC spaces of fast skeletal muscle cells (PubMed:15731387). Preferentially
CC forms linear and round aggregates in the endoplasmic reticulum (ER) of
CC resting cells. In a minority of cells, homogeneously detected in the ER
CC lumen. Colocalizes with STIM1 at endoplasmic reticulum in response to a
CC depletion of intracellular calcium (By similarity).
CC {ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:15731387}.
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level).
CC Detected in skeletal muscle. {ECO:0000269|PubMed:3427087,
CC ECO:0000269|PubMed:3469659, ECO:0000269|PubMed:8227022}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:22170046}.
CC -!- SIMILARITY: Belongs to the calsequestrin family. {ECO:0000305}.
CC -!- CAUTION: Phosphorylated at very low, substoichiometric levels when
CC isolated from skeletal muscle sarcoplasmic reticulum (PubMed:1985907).
CC Can be phosphorylated by CK2 at Thr-381 (in vitro), albeit with low
CC efficiency, suggesting this is not a physiological CK2 substrate
CC (PubMed:1985907). Not phosphorylated at Thr-381 (PubMed:22170046).
CC {ECO:0000269|PubMed:1985907, ECO:0000269|PubMed:22170046, ECO:0000305}.
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DR EMBL; M15747; AAA31184.1; -; mRNA.
DR EMBL; M22717; AAA31185.1; -; Genomic_DNA.
DR EMBL; M20142; AAA31185.1; JOINED; Genomic_DNA.
DR EMBL; M22712; AAA31185.1; JOINED; Genomic_DNA.
DR EMBL; M22713; AAA31185.1; JOINED; Genomic_DNA.
DR EMBL; M22714; AAA31185.1; JOINED; Genomic_DNA.
DR EMBL; M22715; AAA31185.1; JOINED; Genomic_DNA.
DR EMBL; M22716; AAA31185.1; JOINED; Genomic_DNA.
DR PIR; A28142; A25887.
DR RefSeq; NP_001075737.1; NM_001082268.1.
DR PDB; 1A8Y; X-ray; 2.40 A; A=29-395.
DR PDB; 3TRP; X-ray; 1.88 A; A=29-381.
DR PDB; 3TRQ; X-ray; 1.76 A; A=29-381.
DR PDB; 3US3; X-ray; 1.74 A; A=29-395.
DR PDB; 3V1W; X-ray; 1.91 A; A=29-395.
DR PDBsum; 1A8Y; -.
DR PDBsum; 3TRP; -.
DR PDBsum; 3TRQ; -.
DR PDBsum; 3US3; -.
DR PDBsum; 3V1W; -.
DR AlphaFoldDB; P07221; -.
DR SMR; P07221; -.
DR MINT; P07221; -.
DR STRING; 9986.ENSOCUP00000024484; -.
DR iPTMnet; P07221; -.
DR PRIDE; P07221; -.
DR GeneID; 100009095; -.
DR KEGG; ocu:100009095; -.
DR CTD; 844; -.
DR eggNOG; ENOG502QQUJ; Eukaryota.
DR InParanoid; P07221; -.
DR OrthoDB; 1091027at2759; -.
DR EvolutionaryTrace; P07221; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:CAFA.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0046872; F:metal ion binding; IDA:CAFA.
DR GO; GO:0030955; F:potassium ion binding; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
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:0051258; P:protein polymerization; IDA:UniProtKB.
DR GO; GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; ISS:UniProtKB.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; ISS:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; ISS:UniProtKB.
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 DisProt; DP00132; -.
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 3D-structure; Calcium; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Metal-binding; Mitochondrion; Muscle protein;
KW Phosphoprotein; Reference proteome; Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:3427023"
FT CHAIN 29..395
FT /note="Calsequestrin-1"
FT /id="PRO_0000004214"
FT REGION 376..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19633"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19633"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19633"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19633"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22170046"
FT CONFLICT 387..388
FT /note="ED -> DE (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 73..93
FT /evidence="ECO:0007829|PDB:3US3"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:3US3"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 186..198
FT /evidence="ECO:0007829|PDB:3US3"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1A8Y"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 288..303
FT /evidence="ECO:0007829|PDB:3US3"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3US3"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:3US3"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3US3"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:3US3"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:3TRP"
SQ SEQUENCE 395 AA; 45263 MW; E849B05AF107AFA7 CRC64;
MNAADRMGAR VALLLLLVLG SPQSGVHGEE GLDFPEYDGV DRVINVNAKN YKNVFKKYEV
LALLYHEPPE DDKASQRQFE MEELILELAA QVLEDKGVGF GLVDSEKDAA VAKKLGLTEE
DSIYVFKEDE VIEYDGEFSA DTLVEFLLDV LEDPVELIEG ERELQAFENI EDEIKLIGYF
KNKDSEHYKA FKEAAEEFHP YIPFFATFDS KVAKKLTLKL NEIDFYEAFM EEPVTIPDKP
NSEEEIVNFV EEHRRSTLRK LKPESMYETW EDDMDGIHIV AFAEEADPDG YEFLEILKSV
AQDNTDNPDL SIIWIDPDDF PLLVPYWEKT FDIDLSAPQI GVVNVTDADS VWMEMDDEED
LPSAEELEDW LEDVLEGEIN TEDDDDEDDD DDDDD
