CASQ1_PELLE
ID CASQ1_PELLE Reviewed; 420 AA.
AC P31231;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Calsequestrin-1;
DE AltName: Full=Calsequestrin, skeletal muscle isoform;
DE Flags: Precursor;
OS Pelophylax lessonae (Pool frog) (Rana lessonae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=45623;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=1375450; DOI=10.1042/bj2830767;
RA Treves S., Vilsen B., Chiozzi P., Andersen J.P., Zorzato F.;
RT "Molecular cloning, functional expression and tissue distribution of the
RT cDNA encoding frog skeletal muscle calsequestrin.";
RL Biochem. J. 283:767-772(1992).
RN [2]
RP PROTEIN SEQUENCE OF 23-57.
RC TISSUE=Skeletal muscle;
RX PubMed=2018493; DOI=10.1016/0006-291x(91)91584-y;
RA Treveso S., Zorzato F., Chiozzi P., Melandri P., Volpe P., Pozzan T.;
RT "Frog brain expresses a 60 KDa Ca2+ binding protein similar to mammalian
RT calreticulin.";
RL Biochem. Biophys. Res. Commun. 175:444-450(1991).
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:1375450). Calcium ions are bound by clusters of acidic residues
CC at the protein surface, often at the interface between subunits. Can
CC bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via
CC the calcium release channel RYR1; this plays an important role in
CC triggering muscle contraction. Negatively regulates store-operated
CC Ca(2+) entry (SOCE) activity (By similarity).
CC {ECO:0000250|UniProtKB:O09165, ECO:0000250|UniProtKB:P07221,
CC ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:1375450}.
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.
CC {ECO:0000250|UniProtKB:P07221, 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 -!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level).
CC Detected in skeletal muscle. {ECO:0000269|PubMed:1375450}.
CC -!- SIMILARITY: Belongs to the calsequestrin family. {ECO:0000305}.
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DR EMBL; X64324; CAA45609.1; -; mRNA.
DR PIR; S22418; S22418.
DR AlphaFoldDB; P31231; -.
DR SMR; P31231; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:2001256; P:regulation of store-operated calcium entry; 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 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; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Metal-binding; Mitochondrion; Muscle protein;
KW Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:2018493"
FT CHAIN 23..420
FT /note="Calsequestrin-1"
FT /id="PRO_0000004216"
FT REGION 369..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 420 AA; 48205 MW; 5589676478E09DF0 CRC64;
MKGPWLVLAA LCLSLANLGP RGEDGLDFPE YDGEDRVIHI SLKNYKAALK KYEVLALLYH
EPIGDDKASQ RQFEMEELIL ELAAQVLEDK GVGFGLVDSE DDAAVAKKLG LDEEDSIYVF
KDDEMIEYDG EFSADTLVEF LLDVLEDPVE FIDGSHELAA FENLDDEPKL IGYFKNEDSE
HYKAYEDAAE EFHPYIPFFA TFDAKVAKTL TLKLNEIDYY EPFHDEPITI PSKPNSEKEI
VDFLHQHKRP TLRKLRPDSM YETWEDDLNG IHIVAFAEED DPDGYEFLQI IKEVAEDNTD
NPDLSIIWID PEDFPLLIPY WEEKFGIDLS RPHIGVVNVT DADSVWMDMD DEEDLPTVDE
LEDWIEDVLE GEVNTEDDDD DDDDDDDDDD DDDDDDDDDD DDDDDDDDDD DDDDDDDDDD
