NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|148922885|ref|NP_001092194|]
View 

N-terminal EF-hand calcium-binding protein 3 [Rattus norvegicus]

Protein Classification

antibiotic biosynthesis monooxygenase family protein( domain architecture ID 11656698)

antibiotic biosynthesis monooxygenase family protein may be involved in the biosynthesis of several antibiotics; similar to Streptomyces tetracenomycin-F1 monooxygenase and deoxynogalonate monooxygenase

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
 251-323 1.17e-09

Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.


:

Pssm-ID: 427635  Cd Length: 74  Bit Score: 54.20  E-value: 1.17e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148922885  251 LVAQRQVQVAEDALQDFHRALCCYMNFTGAQSHCLHVSAQKMLDNA-AFTLYEFWQDEASWRRHQQSPCSKAFQ 323
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRSLEDPdEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
24-74 6.58e-06

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 6.58e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148922885  24 APAAGHALFQDVFRRADKNDDGKLSFEEFQNYFADGVLSSAELRELFSGID 74
Cdd:COG5126   63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLD 113
EFh_PI-PLC super family cl28895
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 36-139 3.93e-03

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.


The actual alignment was detected with superfamily member cd16217:

Pssm-ID: 333715 [Multi-domain]  Cd Length: 139  Bit Score: 37.03  E-value: 3.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148922885  36 FRRADKNDDGKLSFEEFQNYFADGVLSSAEL--RELFSGIDEQLTDNLETEKLCDYFSthlgvyrpVLAALESLNRAvlt 113
Cdd:cd16217    6 LRKADKNKDNKMSFKELKDFLKEINIEVDDDyaEKLFKECDKSKSGFLEGEEIEEFYK--------LLTKREEIDVI--- 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148922885 114 amdttkleYEQASKVDQFVTR-----FLLRE 139
Cdd:cd16217   75 --------FGEYAKSDGTMSRnnllnFLQEE 97
 
Name Accession Description Interval E-value
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
 251-323 1.17e-09

Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.


Pssm-ID: 427635  Cd Length: 74  Bit Score: 54.20  E-value: 1.17e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148922885  251 LVAQRQVQVAEDALQDFHRALCCYMNFTGAQSHCLHVSAQKMLDNA-AFTLYEFWQDEASWRRHQQSPCSKAFQ 323
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRSLEDPdEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
24-74 6.58e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 6.58e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148922885  24 APAAGHALFQDVFRRADKNDDGKLSFEEFQNYFADGVLSSAELRELFSGID 74
Cdd:COG5126   63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLD 113
YgiN COG1359
Quinol monooxygenase YgiN [Energy production and conversion];
256-339 3.17e-05

Quinol monooxygenase YgiN [Energy production and conversion];


Pssm-ID: 440970  Cd Length: 91  Bit Score: 42.25  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148922885 256 QVQVAEDALQDFHRALCCYMNFTGAQSHCLHVS-AQKMLDNAAFTLYEFWQDEASWRRHQQSPCSKAFQRTLIDHLRAPD 334
Cdd:COG1359    6 KLTVKPGKRDEFLAALRELVEATRAEPGCLSYElYRDPDDPNRFVLYERWEDEAALEAHLASPHFKAFLAALAPLLAEPP 85


                 ....*
gi 148922885 335 TLTTV 339
Cdd:COG1359   86 EVRVY 90
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 32-74 5.11e-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: 40.61  E-value: 5.11e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 148922885  32 FQDVFRRADKNDDGKLSFEEFQNYF--ADGVLSSAELRELFSGID 74
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEMIREVD 46
EF-hand_5 pfam13202
EF hand;
32-54 7.91e-05

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 39.22  E-value: 7.91e-05
                          10        20
                  ....*....|....*....|...
gi 148922885   32 FQDVFRRADKNDDGKLSFEEFQN 54
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRR 23
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 32-52 4.28e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.97  E-value: 4.28e-04
                           10        20
                   ....*....|....*....|.
gi 148922885    32 FQDVFRRADKNDDGKLSFEEF 52
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEF 22
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 36-139 3.93e-03

EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (PLCD1), or phospholipase C-III (PLC-III), or phospholipase C-delta-1 (PLC-delta-1), is present in high abundancy in the brain, heart, lung, skeletal muscle and testis. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. PI-PLC-delta1 is required for maintenance of homeostasis in skin and metabolic tissues. Moreover, it is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta1 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta1 can be positively or negatively regulated by several binding partners, including p122/Rho GTPase activating protein (RhoGAP), Gha/Transglutaminase II, RalA, and calmodulin. It is involved in Alzheimer's disease and hypertension. Furthermore, PI-PLC-delta1 regulates cell proliferation and cell-cycle progression from G1- to S-phase by control of cyclin E-CDK2 activity and p27 levels. It can be activated by alpha1-adrenoreceptors (AR) in a calcium-dependent manner and may be important for G protein-coupled receptors (GPCR) responses in vascular smooth muscle (VSM). PI-PLC-delta1 may also be involved in noradrenaline (NA)-induced phosphatidylinositol-4,5-bisphosphate (PIP2) hydrolysis and modulate sustained contraction of mesenteric small arteries. In addition, it inhibits thermogenesis and induces lipid accumulation, and therefore contributes to the development of obesity. PI-PLC-delta1 contains 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 C-terminal C2 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. PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. In addition, PI-PLC-delta1 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, as well as a nuclear localization signal within its linker region, both of which may be responsible for translocating PI-PLC-delta1 into and out of the cell nucleus.


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 37.03  E-value: 3.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148922885  36 FRRADKNDDGKLSFEEFQNYFADGVLSSAEL--RELFSGIDEQLTDNLETEKLCDYFSthlgvyrpVLAALESLNRAvlt 113
Cdd:cd16217    6 LRKADKNKDNKMSFKELKDFLKEINIEVDDDyaEKLFKECDKSKSGFLEGEEIEEFYK--------LLTKREEIDVI--- 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148922885 114 amdttkleYEQASKVDQFVTR-----FLLRE 139
Cdd:cd16217   75 --------FGEYAKSDGTMSRnnllnFLQEE 97
 
Name Accession Description Interval E-value
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
 251-323 1.17e-09

Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.


Pssm-ID: 427635  Cd Length: 74  Bit Score: 54.20  E-value: 1.17e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148922885  251 LVAQRQVQVAEDALQDFHRALCCYMNFTGAQSHCLHVSAQKMLDNA-AFTLYEFWQDEASWRRHQQSPCSKAFQ 323
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRSLEDPdEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
24-74 6.58e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 6.58e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148922885  24 APAAGHALFQDVFRRADKNDDGKLSFEEFQNYFADGVLSSAELRELFSGID 74
Cdd:COG5126   63 FEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLD 113
YgiN COG1359
Quinol monooxygenase YgiN [Energy production and conversion];
256-339 3.17e-05

Quinol monooxygenase YgiN [Energy production and conversion];


Pssm-ID: 440970  Cd Length: 91  Bit Score: 42.25  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148922885 256 QVQVAEDALQDFHRALCCYMNFTGAQSHCLHVS-AQKMLDNAAFTLYEFWQDEASWRRHQQSPCSKAFQRTLIDHLRAPD 334
Cdd:COG1359    6 KLTVKPGKRDEFLAALRELVEATRAEPGCLSYElYRDPDDPNRFVLYERWEDEAALEAHLASPHFKAFLAALAPLLAEPP 85


                 ....*
gi 148922885 335 TLTTV 339
Cdd:COG1359   86 EVRVY 90
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 32-74 5.11e-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: 40.61  E-value: 5.11e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 148922885  32 FQDVFRRADKNDDGKLSFEEFQNYF--ADGVLSSAELRELFSGID 74
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEMIREVD 46
EF-hand_5 pfam13202
EF hand;
32-54 7.91e-05

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 39.22  E-value: 7.91e-05
                          10        20
                  ....*....|....*....|...
gi 148922885   32 FQDVFRRADKNDDGKLSFEEFQN 54
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRR 23
EF-hand_7 pfam13499
EF-hand domain pair;
33-74 1.91e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 1.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 148922885   33 QDVFRRADKNDDGKLSFEEFQNYFA----DGVLSSAELRELFSGID 74
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRkleeGEPLSDEEVEELFKEFD 50
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 32-58 2.20e-04

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: 37.77  E-value: 2.20e-04
                          10        20
                  ....*....|....*....|....*..
gi 148922885   32 FQDVFRRADKNDDGKLSFEEFQNYFAD 58
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 32-52 4.28e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.97  E-value: 4.28e-04
                           10        20
                   ....*....|....*....|.
gi 148922885    32 FQDVFRRADKNDDGKLSFEEF 52
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEF 22
EF-hand_7 pfam13499
EF-hand domain pair;
33-56 4.86e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 4.86e-04
                          10        20
                  ....*....|....*....|....
gi 148922885   33 QDVFRRADKNDDGKLSFEEFQNYF 56
Cdd:pfam13499  43 EELFKEFDLDKDGRISFEEFLELY 66
EF-hand_6 pfam13405
EF-hand domain;
32-56 5.61e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.77  E-value: 5.61e-04
                          10        20
                  ....*....|....*....|....*
gi 148922885   32 FQDVFRRADKNDDGKLSFEEFQNYF 56
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKAL 26
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
33-58 8.12e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.00  E-value: 8.12e-04
                         10        20
                 ....*....|....*....|....*.
gi 148922885  33 QDVFRRADKNDDGKLSFEEFQNYFAD 58
Cdd:COG5126  106 DELFARLDTDGDGKISFEEFVAAVRD 131
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
20-74 1.51e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 1.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148922885  20 TRHSAPAAGHALFQDVFRRADKNDDGKLSFEEFQNYFADGVLSSAE--LRELFSGID 74
Cdd:COG5126   23 ERDDFEALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEpfARAAFDLLD 79
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 30-53 1.76e-03

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: 36.37  E-value: 1.76e-03
                         10        20
                 ....*....|....*....|....
gi 148922885  30 ALFQDVFRRADKNDDGKLSFEEFQ 53
Cdd:cd00051   36 EEIDEMIREVDKDGDGKIDFEEFL 59
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 36-139 3.93e-03

EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (PLCD1), or phospholipase C-III (PLC-III), or phospholipase C-delta-1 (PLC-delta-1), is present in high abundancy in the brain, heart, lung, skeletal muscle and testis. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. PI-PLC-delta1 is required for maintenance of homeostasis in skin and metabolic tissues. Moreover, it is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta1 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta1 can be positively or negatively regulated by several binding partners, including p122/Rho GTPase activating protein (RhoGAP), Gha/Transglutaminase II, RalA, and calmodulin. It is involved in Alzheimer's disease and hypertension. Furthermore, PI-PLC-delta1 regulates cell proliferation and cell-cycle progression from G1- to S-phase by control of cyclin E-CDK2 activity and p27 levels. It can be activated by alpha1-adrenoreceptors (AR) in a calcium-dependent manner and may be important for G protein-coupled receptors (GPCR) responses in vascular smooth muscle (VSM). PI-PLC-delta1 may also be involved in noradrenaline (NA)-induced phosphatidylinositol-4,5-bisphosphate (PIP2) hydrolysis and modulate sustained contraction of mesenteric small arteries. In addition, it inhibits thermogenesis and induces lipid accumulation, and therefore contributes to the development of obesity. PI-PLC-delta1 contains 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 C-terminal C2 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. PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. In addition, PI-PLC-delta1 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, as well as a nuclear localization signal within its linker region, both of which may be responsible for translocating PI-PLC-delta1 into and out of the cell nucleus.


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 37.03  E-value: 3.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148922885  36 FRRADKNDDGKLSFEEFQNYFADGVLSSAEL--RELFSGIDEQLTDNLETEKLCDYFSthlgvyrpVLAALESLNRAvlt 113
Cdd:cd16217    6 LRKADKNKDNKMSFKELKDFLKEINIEVDDDyaEKLFKECDKSKSGFLEGEEIEEFYK--------LLTKREEIDVI--- 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148922885 114 amdttkleYEQASKVDQFVTR-----FLLRE 139
Cdd:cd16217   75 --------FGEYAKSDGTMSRnnllnFLQEE 97
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 35-78 4.55e-03

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain 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 C-terminal C2 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. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 36.82  E-value: 4.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 148922885  35 VFRRADKNDDGKLSFEEFQNYFADgVLSSAELRELF---SGIDEQLT 78
Cdd:cd16202   41 LFQEADTSGEDVLDEEEFVQFYNR-LTKRPEIEELFkkySGDDEALT 86
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH