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Conserved domains on  [gi|60687414|ref|NP_084448|]
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EF-hand calcium-binding domain-containing protein 11 [Mus musculus]

Protein Classification

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

Gene Ontology:  GO:0005509
PubMed:  2479149

Graphical summary

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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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60687414  20 RRKWVKVFKACDEDNKGYLSREDFKVAIVMLFGYKPSKIEADAvmssvnpnTSGVSLEGFLSAVKRKKEARLyRNEIRQI 99
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDG--------DGRISREEFVAGMESLFEATV-EPFARAA 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 60687414 100 FTAFDVHYRGFLTLEDFKRAFSrvAPKLPARTVLEVFREADQDSDGHVSFRDFEYAM 156
Cdd:COG5126  75 FDLLDTDGDGKISADEFRRLLT--ALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
 
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60687414  20 RRKWVKVFKACDEDNKGYLSREDFKVAIVMLFGYKPSKIEADAvmssvnpnTSGVSLEGFLSAVKRKKEARLyRNEIRQI 99
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDG--------DGRISREEFVAGMESLFEATV-EPFARAA 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 60687414 100 FTAFDVHYRGFLTLEDFKRAFSrvAPKLPARTVLEVFREADQDSDGHVSFRDFEYAM 156
Cdd:COG5126  75 FDLLDTDGDGKISADEFRRLLT--ALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60687414    3 LSEAGARPRAGEASASERRKWVKVFkacDEDNKGYLSREDFKVAIVMLfGYKPSKIEADAVMSSVNPNTSG-VSLEGFLS 81
Cdd:PTZ00183   2 RKRRSERPGLTEDQKKEIREAFDLF---DTDGSGTIDPKELKVAMRSL-GFEPKKEEIKQMIADVDKDGSGkIDFEEFLD 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60687414   82 AVKRKKEARLYRNEIRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPARTVLEVFREADQDSDGHVSFRDFEYAM 156
Cdd:PTZ00183  78 IMTKKLGERDPREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
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
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60687414    93 RNEIRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPART--VLEVFREADQDSDGHVSFRDFEYAM 156
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDeeVEELFKEFDLDKDGRISFEEFLELY 66
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
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 60687414  95 EIRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPARTVLEVFREADQDSDGHVSFRDF 152
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEF 58
 
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60687414  20 RRKWVKVFKACDEDNKGYLSREDFKVAIVMLFGYKPSKIEADAvmssvnpnTSGVSLEGFLSAVKRKKEARLyRNEIRQI 99
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDG--------DGRISREEFVAGMESLFEATV-EPFARAA 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 60687414 100 FTAFDVHYRGFLTLEDFKRAFSrvAPKLPARTVLEVFREADQDSDGHVSFRDFEYAM 156
Cdd:COG5126  75 FDLLDTDGDGKISADEFRRLLT--ALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60687414    3 LSEAGARPRAGEASASERRKWVKVFkacDEDNKGYLSREDFKVAIVMLfGYKPSKIEADAVMSSVNPNTSG-VSLEGFLS 81
Cdd:PTZ00183   2 RKRRSERPGLTEDQKKEIREAFDLF---DTDGSGTIDPKELKVAMRSL-GFEPKKEEIKQMIADVDKDGSGkIDFEEFLD 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60687414   82 AVKRKKEARLYRNEIRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPARTVLEVFREADQDSDGHVSFRDFEYAM 156
Cdd:PTZ00183  78 IMTKKLGERDPREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
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
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60687414    93 RNEIRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPART--VLEVFREADQDSDGHVSFRDFEYAM 156
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDeeVEELFKEFDLDKDGRISFEEFLELY 66
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60687414   52 GYKPSKIEADAVMSSVNPNTSG-VSLEGFLSAVKRKKEARLYRNEIRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPAR 130
Cdd:PTZ00184  41 GQNPTEAELQDMINEVDADGNGtIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDE 120

                         90       100
                 ....*....|....*....|....*..
gi 60687414  131 TVLEVFREADQDSDGHVSFRDFEYAMN 157
Cdd:PTZ00184 121 EVDEMIREADVDGDGQINYEEFVKMMM 147
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
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 60687414  95 EIRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPARTVLEVFREADQDSDGHVSFRDF 152
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEF 58
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
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60687414  25 KVFKACDEDNKGYLSREDFKvAIVMLFGYKPSKIEADAVMSSVNPNTSG-VSLEGFLSAVK 84
Cdd:cd00051   4 EAFRLFDKDGDGTISADELK-AALKSLGEGLSEEEIDEMIREVDKDGDGkIDFEEFLELMA 63
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
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60687414    26 VFKACDEDNKGYLSREDFKVAIVMLF-GYKPSKIEADAVMSSVNPNTSG-VSLEGFLSAVK 84
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEeGEPLSDEEVEELFKEFDLDKDGrISFEEFLELYS 67
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
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 60687414   108 RGFLTLEDFKRAFSRV-APKLPARTVLEVFREADQDSDGHVSFRDF 152
Cdd:pfam13833   2 KGVITREELKRALALLgLKDLSEDEVDILFREFDTDGDGYISFDEF 47
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
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 60687414  96 IRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPARTVLEVFREADQD-SDGHVSFRDF 152
Cdd:cd16205   2 LKQTFEEADKNGDGLLSIGEILQLMHKLNVNLPRRKVRQMFKEADTDdNQGTLDFEEF 59
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
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 60687414  96 IRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPARTVLEVFREADQDSDGHVSFRDFE 153
Cdd:cd15898   2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFE 59
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
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60687414  91 LYRNEIRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLpartvlevFREADQDSDGHVSFRDFEYAM 156
Cdd:COG5126   2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATL--------FSEADTDGDGRISREEFVAGM 59
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
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 60687414  96 IRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPARTVLEVFREADQDSD-GHVSFRDF 152
Cdd:cd16220   2 VKQTFEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQEADTDENqGTLTFEEF 59
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
                          10        20
                  ....*....|....*....|....*..
gi 60687414   132 VLEVFREADQDSDGHVSFRDFEYAMNH 158
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKK 28
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60687414  21 RKWvkvFKACDEDNKGYLSREDFKVAIV---MLFGYKpskiEADAVMSSVNPNTSG-VSLEGFlsavkrkkeARLYR--N 94
Cdd:cd16185   3 RQW---FRAVDRDRSGSIDVNELQKALAgggLLFSLA----TAEKLIRMFDRDGNGtIDFEEF---------AALHQflS 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 60687414  95 EIRQIFTAFDVHYRGFLTLEDFKRAFSRVAPKLPARTVLEVFREADQDSDGHVSFRDF 152
Cdd:cd16185  67 NMQNGFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60687414  24 VKVFKACDEDNKGYLSREDFKVAIVMLFGYKPSKIEADAVMSSVnpntsgvsLEGFLSAVKRKKEARLYRNEIRQIFtaf 103
Cdd:cd15902   2 MEVWMHFDADGNGYIEGKELDSFLRELLKALNGKDKTDDEVAEK--------KKEFMEKYDENEDGKIEIRELANIL--- 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 60687414 104 dvhyrgfLTLEDFKRAFSRVAPKLPARTVLEVFREADQDSDG 145
Cdd:cd15902  71 -------PTEENFLLLFRREQPLISSVEFMKIWRKYDTDGSG 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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