EF-hand calcium-binding domain-containing protein 11 [Mus musculus]
EF-hand domain-containing protein( domain architecture ID 11473824)
EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction
List of domain hits
Name | Accession | Description | Interval | E-value | |||
FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
20-156 | 8.98e-14 | |||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; : Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 64.43 E-value: 8.98e-14
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Name | Accession | Description | Interval | E-value | |||
FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
20-156 | 8.98e-14 | |||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 64.43 E-value: 8.98e-14
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PTZ00183 | PTZ00183 | centrin; Provisional |
3-156 | 2.52e-09 | |||
centrin; Provisional Pssm-ID: 185503 [Multi-domain] Cd Length: 158 Bit Score: 53.15 E-value: 2.52e-09
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EF-hand_7 | pfam13499 | EF-hand domain pair; |
93-156 | 4.17e-09 | |||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 50.33 E-value: 4.17e-09
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EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
95-152 | 3.87e-07 | |||
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 44.85 E-value: 3.87e-07
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Name | Accession | Description | Interval | E-value | |||
FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
20-156 | 8.98e-14 | |||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 64.43 E-value: 8.98e-14
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PTZ00183 | PTZ00183 | centrin; Provisional |
3-156 | 2.52e-09 | |||
centrin; Provisional Pssm-ID: 185503 [Multi-domain] Cd Length: 158 Bit Score: 53.15 E-value: 2.52e-09
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EF-hand_7 | pfam13499 | EF-hand domain pair; |
93-156 | 4.17e-09 | |||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 50.33 E-value: 4.17e-09
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PTZ00184 | PTZ00184 | calmodulin; Provisional |
52-157 | 2.69e-08 | |||
calmodulin; Provisional Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 50.15 E-value: 2.69e-08
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EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
95-152 | 3.87e-07 | |||
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 44.85 E-value: 3.87e-07
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EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
25-84 | 4.34e-05 | |||
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 39.45 E-value: 4.34e-05
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EF-hand_7 | pfam13499 | EF-hand domain pair; |
26-84 | 4.73e-05 | |||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 39.54 E-value: 4.73e-05
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EF-hand_8 | pfam13833 | EF-hand domain pair; |
108-152 | 2.23e-04 | |||
EF-hand domain pair; Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 37.29 E-value: 2.23e-04
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EFh_PI-PLCeta | cd16205 | EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ... |
96-152 | 2.26e-04 | |||
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes represent a class of neuron-specific metazoan PI-PLCs that are most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. They are phosphatidylinositol 4,5-bisphosphate-hydrolyzing enzymes that are more sensitive to Ca2+ than other PI-PLC isozymes. They function as calcium sensors activated by small increases in intracellular calcium concentrations. They are also activated through G-protein-coupled receptor (GPCR) stimulation, and further mediate GPCR signalling pathways. PI-PLC-eta isozymes contain an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. There are two PI-PLC-eta isozymes (1-2). Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family. Pssm-ID: 320035 [Multi-domain] Cd Length: 141 Bit Score: 39.29 E-value: 2.26e-04
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EFh_PI-PLC | cd15898 | EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
96-153 | 8.75e-04 | |||
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear. Pssm-ID: 320029 [Multi-domain] Cd Length: 137 Bit Score: 37.65 E-value: 8.75e-04
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FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
91-156 | 9.27e-04 | |||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 37.46 E-value: 9.27e-04
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EFh_PI-PLCeta1 | cd16220 | EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ... |
96-152 | 9.59e-04 | |||
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1, or phospholipase C-eta-1 (PLC-eta-1), or phospholipase C-like protein 3 (PLC-L3), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the zona incerta and in the spinal cord. PI-PLC-eta1 may perform a fundamental role in the brain. It may also act in synergy with other PLC subtypes. For instance, it is activated via intracellular Ca2+ mobilization and then plays a role in the amplification of GPCR (G-protein-coupled receptor)-mediated PLC-beta signals. In addition, its activity can be stimulated by ionomycin. PI-PLC-eta1 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. Pssm-ID: 320050 [Multi-domain] Cd Length: 141 Bit Score: 37.31 E-value: 9.59e-04
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EF-hand_1 | pfam00036 | EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
132-158 | 6.38e-03 | |||
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes. Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 32.76 E-value: 6.38e-03
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EFh_PEF_ALG-2_like | cd16185 | EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ... |
21-152 | 7.86e-03 | |||
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD). Pssm-ID: 320060 [Multi-domain] Cd Length: 163 Bit Score: 34.88 E-value: 7.86e-03
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EFh_HEF | cd15902 | EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ... |
24-145 | 9.00e-03 | |||
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding. Pssm-ID: 320075 [Multi-domain] Cd Length: 254 Bit Score: 35.41 E-value: 9.00e-03
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Blast search parameters | ||||
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