CASQ1_RAT
ID CASQ1_RAT Reviewed; 406 AA.
AC P19633;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 132.
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 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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-163.
RC TISSUE=Prostate;
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 35-54, AND TISSUE SPECIFICITY.
RX PubMed=3417768; DOI=10.1083/jcb.107.2.687;
RA Hall D.E., Frazer K.A., Hann B.C., Reichardt L.F.;
RT "Isolation and characterization of a laminin-binding protein from rat and
RT chick muscle.";
RL J. Cell Biol. 107:687-697(1988).
RN [4]
RP PROTEIN SEQUENCE OF 35-54, TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=Wistar; TISSUE=Aorta, Stomach, and 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43; SER-81; THR-124 AND
RP SER-216, AND 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, 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 (By similarity). Negatively regulates
CC store-operated Ca(2+) entry (SOCE) activity (By similarity).
CC {ECO:0000250|UniProtKB:O09165, ECO:0000250|UniProtKB:P07221,
CC ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:8042990}.
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.
CC Interacts with ASPH and TRDN. {ECO:0000250|UniProtKB:P07221,
CC 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 and in smooth muscle
CC from vas deferens, aorta and stomach (at protein level).
CC {ECO:0000269|PubMed:3417768, ECO:0000269|PubMed:8042990}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P07221}.
CC -!- SIMILARITY: Belongs to the calsequestrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CA334109; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AABR03085534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03087242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CA334109; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A31049; A31049.
DR RefSeq; NP_001153066.1; NM_001159594.1.
DR AlphaFoldDB; P19633; -.
DR SMR; P19633; -.
DR STRING; 10116.ENSRNOP00000009344; -.
DR GlyGen; P19633; 1 site.
DR iPTMnet; P19633; -.
DR PhosphoSitePlus; P19633; -.
DR PaxDb; P19633; -.
DR Ensembl; ENSRNOT00000009344; ENSRNOP00000009344; ENSRNOG00000006930.
DR GeneID; 686019; -.
DR KEGG; rno:686019; -.
DR UCSC; RGD:1586677; rat.
DR CTD; 844; -.
DR RGD; 1586677; Casq1.
DR eggNOG; ENOG502QQUJ; Eukaryota.
DR GeneTree; ENSGT00390000019377; -.
DR HOGENOM; CLU_036303_1_0_1; -.
DR InParanoid; P19633; -.
DR OMA; GYPELEY; -.
DR OrthoDB; 1091027at2759; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR PRO; PR:P19633; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000006930; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; P19633; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0031674; C:I band; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0030016; C:myofibril; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0014802; C:terminal cisterna; IDA:RGD.
DR GO; GO:0014804; C:terminal cisterna lumen; IDA:RGD.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
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; ISS:UniProtKB.
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:0051282; P:regulation of sequestering of calcium ion; IDA:RGD.
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:0014894; P:response to denervation involved in regulation of muscle adaptation; IEP:RGD.
DR GO; GO:0009408; P:response to heat; ISO:RGD.
DR GO; GO:0014870; P:response to muscle inactivity; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISS:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP: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; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Metal-binding; Mitochondrion; Muscle protein; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255, ECO:0000269|PubMed:3417768,
FT ECO:0000269|PubMed:8042990"
FT CHAIN 35..406
FT /note="Calsequestrin-1"
FT /id="PRO_0000144072"
FT REGION 382..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 36
FT /note="D -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..54
FT /note="NA -> AD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 46449 MW; ED408245EDA12E23 CRC64;
MRATDRMGAR AVSKLRLALL FVLVLGTPRS GVQGEDGLDF PEYDGVDRVI NVNAKNYKNV
FKKYEVLALL YHEPPEDDKA SQRQFEMEEL ILELAAQVLE DKGVGFGLVD SEKDAAVAKK
LGLTEEDSVY VFKGDEVIEY DGEFSADTLV EFLLDVLEDP VELIEGEREL QAFENIEDEI
KLIGYFKSKD SEHYKAYEDA AEEFHPYIPF FATFDSKVAK KLTLKLNEID FYEAFMEEPV
TIPDKPNSEE EIVSFVEEHR RSTLRKLKPE SMYETWEDDL DGIHIVAFAE EADPDGYEFL
ETLKAVAQDN TENPDLSIIW IDPDDFPLLV PYWEKTFDID LSAPQIGVVN VTDADSIWME
MDDEEDLPSA EELEDWLEDV LEGEINTEDD DDDDDDDDDD DDDDDD
