CASQ2_CHICK
ID CASQ2_CHICK Reviewed; 406 AA.
AC P19204;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Calsequestrin-2;
DE AltName: Full=Laminin-binding protein;
DE Flags: Precursor;
GN Name=CASQ2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn;
RX PubMed=3417769; DOI=10.1083/jcb.107.2.699;
RA Clegg D.O., Helder J.C., Hann B.C., Hall D.E., Reichardt L.F.;
RT "Amino acid sequence and distribution of mRNA encoding a major skeletal
RT muscle laminin binding protein: an extracellular matrix-associated protein
RT with an unusual COOH-terminal polyaspartate domain.";
RL J. Cell Biol. 107:699-705(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-406, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2390076; DOI=10.1016/0006-291x(90)90504-g;
RA Yazaki P.J., Salvatori S., Dahms A.S.;
RT "Amino acid sequence of chicken calsequestrin deduced from cDNA: comparison
RT of calsequestrin and aspartactin.";
RL Biochem. Biophys. Res. Commun. 170:1089-1095(1990).
RN [3]
RP ERRATUM OF PUBMED:2390076.
RX PubMed=2260982; DOI=10.1016/s0006-291x(05)80101-9;
RA Yazaki P.J., Salvatori S., Dahms A.S.;
RL Biochem. Biophys. Res. Commun. 173:763-763(1990).
RN [4]
RP PROTEIN SEQUENCE OF 20-39.
RC STRAIN=White leghorn; TISSUE=Skeletal muscle;
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 [5]
RP PROTEIN SEQUENCE OF 20-39, AND SUBCELLULAR LOCATION.
RC STRAIN=New Hampshire;
RX PubMed=2302244; DOI=10.1016/0006-291x(90)90895-t;
RA Yazaki P.J., Salvatori S., Sabbadini R.A., Dahms A.S.;
RT "Calsequestrin, an intracellular calcium-binding protein of skeletal muscle
RT sarcoplasmic reticulum, is homologous to aspartactin, a putative laminin-
RT binding protein of the extracellular matrix.";
RL Biochem. Biophys. Res. Commun. 166:898-903(1990).
RN [6]
RP CAUTION, AND LACK OF LAMININ BINDING.
RX PubMed=1825466; DOI=10.1016/0006-291x(91)91550-v;
RA Choi E.S., Sullivan P.D., Clegg D.O.;
RT "Evidence against a laminin receptor role for calsequestrin.";
RL Biochem. Biophys. Res. Commun. 174:1208-1216(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 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:O09161}.
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen
CC {ECO:0000269|PubMed:2302244}. Note=This isoform of calsequestrin occurs
CC in the sarcoplasmic reticulum's terminal cisternae luminal spaces of
CC cardiac and slow skeletal muscle cells. {ECO:0000269|PubMed:2302244}.
CC -!- TISSUE SPECIFICITY: Skeletal and heart muscle.
CC {ECO:0000269|PubMed:3417769}.
CC -!- SIMILARITY: Belongs to the calsequestrin family. {ECO:0000305}.
CC -!- CAUTION: Was initially identified as a laminin-binding protein
CC (PubMed:3417768), but later studies indicate that this is highly
CC unlikely (PubMed:1825466 and PubMed:2302244). {ECO:0000305}.
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DR EMBL; Y00789; CAA68743.1; -; mRNA.
DR EMBL; M58048; AAA48674.1; -; mRNA.
DR PIR; A31050; A31050.
DR RefSeq; NP_989857.1; NM_204526.1.
DR AlphaFoldDB; P19204; -.
DR SMR; P19204; -.
DR STRING; 9031.ENSGALP00000036165; -.
DR PaxDb; P19204; -.
DR GeneID; 395198; -.
DR KEGG; gga:395198; -.
DR CTD; 845; -.
DR VEuPathDB; HostDB:geneid_395198; -.
DR eggNOG; ENOG502QU4Q; Eukaryota.
DR InParanoid; P19204; -.
DR OrthoDB; 1091027at2759; -.
DR PhylomeDB; P19204; -.
DR PRO; PR:P19204; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0014802; C:terminal cisterna; IDA:AgBase.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Glycoprotein; Muscle protein;
KW Reference proteome; Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2302244,
FT ECO:0000269|PubMed:3417768"
FT CHAIN 20..406
FT /note="Calsequestrin-2"
FT /id="PRO_0000004215"
FT REGION 365..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..406
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="V -> I (in Ref. 2; AAA48674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 47151 MW; 928CF5A785A2DC7C CRC64;
MKATCWILAG FCLLFCCKAE EGLNFPTYDG KDRVIDLNEK NYKHALKKYD MLCLLFHEPV
SSDRVSQKQF QMTEMVLELA AQVLEPRSIG FGMVDSKKDA KLAKKLGLVE EGSLYVFKEE
RLIEFDGELA TDVLVEFLLD LLEDPVEVIN SKLELQAFDQ IDDEIKLIGY FKGEDSEHYK
AFEEAAEHFQ PYVKFFATFD KGVAKKLGLK MNEVDFYEPF MDEPVHIPDK PYTEEELVEF
VKEHKRATLR KLRPEDMFET WEDDMEGIHI VAFAEEDDPD GFEFLEILKQ VARDNTDNPD
LSIVWIDPDD FPLLITYWEK TFKIDLFRPQ IGIVNVTDAD SVWMEIRDDD DLPTAEELED
WIEDVLSGKI NTEDDDDDDD DDDDDDDDDD DDDDDDDDDD DDDDDD
