calsequestrin-1 precursor [Mus musculus]
Protein Classification
PDI_b'_Calsequestrin_C domain-containing protein( domain architecture ID 12014829)
PDI_b'_Calsequestrin_C domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| Calsequestrin | pfam01216 | Calsequestrin; |
37-386 | 0e+00 | ||||||
Calsequestrin; : Pssm-ID: 395972 [Multi-domain] Cd Length: 350 Bit Score: 656.32 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| Calsequestrin | pfam01216 | Calsequestrin; |
37-386 | 0e+00 | ||||||
Calsequestrin; Pssm-ID: 395972 [Multi-domain] Cd Length: 350 Bit Score: 656.32 E-value: 0e+00
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| PDI_b'_Calsequestrin_C | cd03074 | Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold ... |
262-381 | 1.26e-67 | ||||||
Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store. The C-terminal TRX-fold domain (or domain III) mediates back-to-back dimer interaction and also contriubutes to the front-to-front dimer interface, both of which are important features in the formation of calsequestrin polymers. Pssm-ID: 239372 Cd Length: 120 Bit Score: 210.03 E-value: 1.26e-67
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| ER_PDI_fam | TIGR01130 | protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ... |
93-385 | 3.60e-13 | ||||||
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs). Pssm-ID: 273457 [Multi-domain] Cd Length: 462 Bit Score: 70.86 E-value: 3.60e-13
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| PTZ00102 | PTZ00102 | disulphide isomerase; Provisional |
95-256 | 2.35e-11 | ||||||
disulphide isomerase; Provisional Pssm-ID: 240266 [Multi-domain] Cd Length: 477 Bit Score: 65.16 E-value: 2.35e-11
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| Name | Accession | Description | Interval | E-value | ||||||
| Calsequestrin | pfam01216 | Calsequestrin; |
37-386 | 0e+00 | ||||||
Calsequestrin; Pssm-ID: 395972 [Multi-domain] Cd Length: 350 Bit Score: 656.32 E-value: 0e+00
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| PDI_b'_Calsequestrin_C | cd03074 | Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold ... |
262-381 | 1.26e-67 | ||||||
Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store. The C-terminal TRX-fold domain (or domain III) mediates back-to-back dimer interaction and also contriubutes to the front-to-front dimer interface, both of which are important features in the formation of calsequestrin polymers. Pssm-ID: 239372 Cd Length: 120 Bit Score: 210.03 E-value: 1.26e-67
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| PDI_b_Calsequestrin_N | cd03065 | PDIb family, Calsequestrin subfamily, N-terminal TRX-fold domain; Calsequestrin is the major ... |
39-158 | 2.19e-62 | ||||||
PDIb family, Calsequestrin subfamily, N-terminal TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store. The N-terminal TRX-fold domain (or domain I) mediates front-to-front dimer interaction, an important feature in the formation of calsequestrin polymers. Pssm-ID: 239363 Cd Length: 120 Bit Score: 196.50 E-value: 2.19e-62
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| PDI_b_Calsequestrin_middle | cd03066 | PDIb family, Calsequestrin subfamily, Middle TRX-fold domain; Calsequestrin is the major ... |
160-261 | 8.40e-57 | ||||||
PDIb family, Calsequestrin subfamily, Middle TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store. Pssm-ID: 239364 [Multi-domain] Cd Length: 102 Bit Score: 181.47 E-value: 8.40e-57
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| PDI_b_family | cd02981 | Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ... |
161-259 | 6.96e-18 | ||||||
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition. Pssm-ID: 239279 Cd Length: 97 Bit Score: 78.15 E-value: 6.96e-18
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| Thioredoxin_6 | pfam13848 | Thioredoxin-like domain; |
186-379 | 6.48e-17 | ||||||
Thioredoxin-like domain; Pssm-ID: 463999 [Multi-domain] Cd Length: 184 Bit Score: 78.17 E-value: 6.48e-17
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| PDI_b'_family | cd02982 | Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ... |
272-381 | 1.51e-14 | ||||||
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity. Pssm-ID: 239280 [Multi-domain] Cd Length: 103 Bit Score: 69.22 E-value: 1.51e-14
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| ER_PDI_fam | TIGR01130 | protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ... |
93-385 | 3.60e-13 | ||||||
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs). Pssm-ID: 273457 [Multi-domain] Cd Length: 462 Bit Score: 70.86 E-value: 3.60e-13
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| PTZ00102 | PTZ00102 | disulphide isomerase; Provisional |
95-256 | 2.35e-11 | ||||||
disulphide isomerase; Provisional Pssm-ID: 240266 [Multi-domain] Cd Length: 477 Bit Score: 65.16 E-value: 2.35e-11
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| PDI_b_family | cd02981 | Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ... |
49-155 | 5.28e-08 | ||||||
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition. Pssm-ID: 239279 Cd Length: 97 Bit Score: 50.41 E-value: 5.28e-08
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| PDI_b_ERp72 | cd03068 | PDIb family, ERp72 subfamily, first redox inactive TRX-like domain b; ERp72 exhibits both ... |
160-259 | 2.40e-06 | ||||||
PDIb family, ERp72 subfamily, first redox inactive TRX-like domain b; ERp72 exhibits both disulfide oxidase and reductase functions like PDI, by catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER and acting as isomerases to correct any non-native disulfide bonds. It also displays chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. ERp72 contains three redox-active TRX (a) domains and two redox inactive TRX-like (b) domains. Its molecular structure is a"abb'a', compared to the abb'a' structure of PDI. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. Similar to PDI, the b domain of ERp72 is likely involved in binding to substrates. Pssm-ID: 239366 Cd Length: 107 Bit Score: 45.94 E-value: 2.40e-06
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