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Conserved domains on  [gi|632952269|ref|XP_007891758|]
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parvalbumin, thymic [Callorhinchus milii]

Protein Classification

parvalbumin beta( domain architecture ID 11611181)

parvalbumin beta has some calmodulin-like activity with respect to enzyme activation and growth regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 9-109 2.41e-51

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


:

Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 156.81  E-value: 2.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632952269   9 ASDISNAIKECQALESFDFKKFFQTSGLSRKSADEIKNVFLAMDDDDSGYIELDELKFFLQRFSPIARVLTEAETEAFLK 88
Cdd:cd16255    1 AADIAAALSQCQAADSFNFKKFFATSGLSKKSADDVKKVFEIIDQDKSGFIEEEELKLFLQNFSSGARELTDAETKAFLK 80

                         90       100
                 ....*....|....*....|.
gi 632952269  89 AADTDGDERIGTQEFVTLVMS 109
Cdd:cd16255   81 AGDSDGDGKIGVEEFQALVKA 101
 
Name Accession Description Interval E-value
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 9-109 2.41e-51

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 156.81  E-value: 2.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632952269   9 ASDISNAIKECQALESFDFKKFFQTSGLSRKSADEIKNVFLAMDDDDSGYIELDELKFFLQRFSPIARVLTEAETEAFLK 88
Cdd:cd16255    1 AADIAAALSQCQAADSFNFKKFFATSGLSKKSADDVKKVFEIIDQDKSGFIEEEELKLFLQNFSSGARELTDAETKAFLK 80

                         90       100
                 ....*....|....*....|.
gi 632952269  89 AADTDGDERIGTQEFVTLVMS 109
Cdd:cd16255   81 AGDSDGDGKIGVEEFQALVKA 101
EF-hand_7 pfam13499
EF-hand domain pair;
42-108 4.95e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.09  E-value: 4.95e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 632952269   42 DEIKNVFLAMDDDDSGYIELDELKFFLQRFSpIARVLTEAETEAFLKAADTDGDERIGTQEFVTLVM 108
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLE-EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
31-109 7.82e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.09  E-value: 7.82e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 632952269  31 FQTSGLSRKSADEIKNVFLAMDDDDSGYIELDELKFFLQrfspiARVLTEAETEAFLKAADTDGDERIGTQEFVTLVMS 109
Cdd:COG5126   58 GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT-----ALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
PTZ00184 PTZ00184
calmodulin; Provisional
 40-109 1.07e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.37  E-value: 1.07e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632952269  40 SADEIKNVFLAMDDDDSGYIELDELKFFLqrfSPIARVLTEAETEAFLKAADTDGDERIGTQEFVTLVMS 109
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVM---TNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMS 148
 
Name Accession Description Interval E-value
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 9-109 2.41e-51

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 156.81  E-value: 2.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632952269   9 ASDISNAIKECQALESFDFKKFFQTSGLSRKSADEIKNVFLAMDDDDSGYIELDELKFFLQRFSPIARVLTEAETEAFLK 88
Cdd:cd16255    1 AADIAAALSQCQAADSFNFKKFFATSGLSKKSADDVKKVFEIIDQDKSGFIEEEELKLFLQNFSSGARELTDAETKAFLK 80

                         90       100
                 ....*....|....*....|.
gi 632952269  89 AADTDGDERIGTQEFVTLVMS 109
Cdd:cd16255   81 AGDSDGDGKIGVEEFQALVKA 101
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
 9-107 1.14e-34

EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319996 [Multi-domain]  Cd Length: 101  Bit Score: 114.97  E-value: 1.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632952269   9 ASDISNAIKECQALESFDFKKFFQTSGLSRKSADEIKNVFLAMDDDDSGYIELDELKFFLQRFSPIARVLTEAETEAFLK 88
Cdd:cd16253    1 ANDIDIALAACQAADSFDHKAFFKAVGLSKKSPADIKKVFNILDQDKSGFIEEEELKLFLKNFSDGARVLSDKETKNFLA 80

                         90
                 ....*....|....*....
gi 632952269  89 AADTDGDERIGTQEFVTLV 107
Cdd:cd16253   81 AGDSDGDGKIGVDEFKSMV 99
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 9-107 2.42e-34

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 114.17  E-value: 2.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632952269   9 ASDISNAIKECQALESFDFKKFFQTSGLSRKSADEIKNVFLAMDDDDSGYIELDELKFFLQRFSPIARVLTEAETEAFLK 88
Cdd:cd16251    1 AKDIEKAPSAFRAHGSFNYKKFFEHVGLKQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFSIAGRDLTDEETKALLA 80

                         90
                 ....*....|....*....
gi 632952269  89 AADTDGDERIGTQEFVTLV 107
Cdd:cd16251   81 AGDTDGDGKIGVEEFATLV 99
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 9-107 8.68e-31

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 104.91  E-value: 8.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632952269   9 ASDISNAIKECQALESFDFKKFFQTSGLSRKSADEIKNVFLAMDDDDSGYIELDELKFFLQRFSPIARVLTEAETEAFLK 88
Cdd:cd16254    1 AEDIKKAVGAFAAADSFDYKKFFEMVGLKKKSADDVKKVFHILDKDKSGFIEEDELKFVLKGFSPDGRDLSDKETKALLA 80

                         90
                 ....*....|....*....
gi 632952269  89 AADTDGDERIGTQEFVTLV 107
Cdd:cd16254   81 AGDKDGDGKIGIDEFATLV 99
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 11-107 8.32e-15

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 64.47  E-value: 8.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632952269  11 DISNAIKECQALESFDFKKFF---QTSGLSRKSADEIKNVFLAMDDDDSGYIELDELKFFLQRF--SPIARVLTEAETEA 85
Cdd:cd16252    3 DIDLLPSEMRHHGSFNYSKFFeymQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVpsSMPVAPLSDEEAEA 82

                         90       100
                 ....*....|....*....|..
gi 632952269  86 FLKAADTDGDERIGTQEFVTLV 107
Cdd:cd16252   83 MIQAADTDGDGRIDFQEFSDMV 104
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 43-108 6.39e-10

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: 50.62  E-value: 6.39e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 632952269  43 EIKNVFLAMDDDDSGYIELDELKFFLQRFSPIarvLTEAETEAFLKAADTDGDERIGTQEFVTLVM 108
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEG---LSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
42-108 4.95e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.09  E-value: 4.95e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 632952269   42 DEIKNVFLAMDDDDSGYIELDELKFFLQRFSpIARVLTEAETEAFLKAADTDGDERIGTQEFVTLVM 108
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLE-EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
31-109 7.82e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.09  E-value: 7.82e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 632952269  31 FQTSGLSRKSADEIKNVFLAMDDDDSGYIELDELKFFLQrfspiARVLTEAETEAFLKAADTDGDERIGTQEFVTLVMS 109
Cdd:COG5126   58 GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT-----ALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
PTZ00184 PTZ00184
calmodulin; Provisional
 40-109 1.07e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.37  E-value: 1.07e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632952269  40 SADEIKNVFLAMDDDDSGYIELDELKFFLqrfSPIARVLTEAETEAFLKAADTDGDERIGTQEFVTLVMS 109
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVM---TNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMS 148
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 44-109 6.95e-05

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: 39.19  E-value: 6.95e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 632952269  44 IKNVFLAMDDDDSGYIELDELKFFLQRFSPiarVLTEAETEAFLKAADTDGDERIGTQEFVTLVMS 109
Cdd:cd15898    2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNI---RVSEKELKKLFKEVDTNGDGTLTFDEFEELYKS 64
PTZ00183 PTZ00183
centrin; Provisional
 23-106 1.50e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.52  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632952269  23 ESFDFKKFFQ--TSGLS-RKSADEIKNVFLAMDDDDSGYIELDELKFFLQRfspIARVLTEAETEAFLKAADTDGDERIG 99
Cdd:PTZ00183  68 GKIDFEEFLDimTKKLGeRDPREEILKAFRLFDDDKTGKISLKNLKRVAKE---LGETITDEELQEMIDEADRNGDGEIS 144


                 ....*..
gi 632952269 100 TQEFVTL 106
Cdd:PTZ00183 145 EEEFYRI 151
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 39-107 1.19e-03

EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity.


Pssm-ID: 320076 [Multi-domain]  Cd Length: 243  Bit Score: 36.35  E-value: 1.19e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 632952269  39 KSADEIKNVFLAMDDDDSGYIELDELKFFLQRF-----SPIARVLTEAETEAFLKAADTDGDERIGTQEFVTLV 107
Cdd:cd16176   82 KSSEEFMQTWRKYDADHSGFIEADELKSFLKDLlkkanKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEMARLL 155
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
41-107 8.64e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 33.61  E-value: 8.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 632952269  41 ADEIKNVFLAMDDDDSGYIELDELkfflqrfspiaRVLTEAETEAFLKAADTDGDERIGTQEFVTLV 107
Cdd:COG5126    4 RRKLDRRFDLLDADGDGVLERDDF-----------EALFRRLWATLFSEADTDGDGRISREEFVAGM 59
 
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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