EPS15 homology domain 2 [Arabidopsis thaliana]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| EHD | cd09913 | Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ... |
199-443 | 1.47e-146 | |||||
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling. : Pssm-ID: 206740 Cd Length: 241 Bit Score: 420.91 E-value: 1.47e-146
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| DUF5600 | pfam18150 | Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ... |
435-537 | 6.82e-42 | |||||
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase 2 (EHD2) present in Mus musculus. The domain is helical in nature and has extensive contacts with the G-domain. : Pssm-ID: 465667 Cd Length: 107 Bit Score: 145.84 E-value: 6.82e-42
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| EH | cd00052 | Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
20-86 | 7.01e-24 | |||||
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs. : Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 94.98 E-value: 7.01e-24
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| EHD_N | pfam16880 | N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ... |
163-195 | 3.49e-14 | |||||
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins. : Pssm-ID: 465295 [Multi-domain] Cd Length: 33 Bit Score: 66.27 E-value: 3.49e-14
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| Name | Accession | Description | Interval | E-value | |||||
| EHD | cd09913 | Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ... |
199-443 | 1.47e-146 | |||||
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling. Pssm-ID: 206740 Cd Length: 241 Bit Score: 420.91 E-value: 1.47e-146
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| DUF5600 | pfam18150 | Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ... |
435-537 | 6.82e-42 | |||||
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase 2 (EHD2) present in Mus musculus. The domain is helical in nature and has extensive contacts with the G-domain. Pssm-ID: 465667 Cd Length: 107 Bit Score: 145.84 E-value: 6.82e-42
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| EH | cd00052 | Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
20-86 | 7.01e-24 | |||||
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs. Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 94.98 E-value: 7.01e-24
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| EH | smart00027 | Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
15-94 | 2.35e-17 | |||||
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences. Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 77.32 E-value: 2.35e-17
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| Dynamin_N | pfam00350 | Dynamin family; |
200-360 | 4.09e-15 | |||||
Dynamin family; Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 73.03 E-value: 4.09e-15
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| EHD_N | pfam16880 | N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ... |
163-195 | 3.49e-14 | |||||
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins. Pssm-ID: 465295 [Multi-domain] Cd Length: 33 Bit Score: 66.27 E-value: 3.49e-14
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| FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
21-79 | 6.61e-06 | |||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 45.94 E-value: 6.61e-06
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| Era | COG1159 | GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
287-369 | 4.99e-05 | |||||
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 45.36 E-value: 4.99e-05
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| EF-hand_7 | pfam13499 | EF-hand domain pair; |
24-79 | 5.04e-05 | |||||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 41.47 E-value: 5.04e-05
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| era | PRK00089 | GTPase Era; Reviewed |
287-369 | 5.88e-05 | |||||
GTPase Era; Reviewed Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 45.04 E-value: 5.88e-05
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| Name | Accession | Description | Interval | E-value | |||||
| EHD | cd09913 | Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ... |
199-443 | 1.47e-146 | |||||
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling. Pssm-ID: 206740 Cd Length: 241 Bit Score: 420.91 E-value: 1.47e-146
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| DUF5600 | pfam18150 | Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ... |
435-537 | 6.82e-42 | |||||
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase 2 (EHD2) present in Mus musculus. The domain is helical in nature and has extensive contacts with the G-domain. Pssm-ID: 465667 Cd Length: 107 Bit Score: 145.84 E-value: 6.82e-42
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| EH | cd00052 | Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
20-86 | 7.01e-24 | |||||
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs. Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 94.98 E-value: 7.01e-24
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| EH | smart00027 | Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
15-94 | 2.35e-17 | |||||
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences. Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 77.32 E-value: 2.35e-17
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| Dynamin_N | pfam00350 | Dynamin family; |
200-360 | 4.09e-15 | |||||
Dynamin family; Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 73.03 E-value: 4.09e-15
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| EHD_N | pfam16880 | N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ... |
163-195 | 3.49e-14 | |||||
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins. Pssm-ID: 465295 [Multi-domain] Cd Length: 33 Bit Score: 66.27 E-value: 3.49e-14
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| Ras_like_GTPase | cd00882 | Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
202-379 | 2.62e-11 | |||||
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions. Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 62.09 E-value: 2.62e-11
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| MMR_HSR1 | pfam01926 | 50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
200-359 | 1.90e-07 | |||||
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide. Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 49.54 E-value: 1.90e-07
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| Era_like | cd00880 | E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
280-367 | 2.99e-06 | |||||
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 47.24 E-value: 2.99e-06
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| DLP_2 | cd09912 | Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
200-368 | 4.29e-06 | |||||
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner. Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 47.16 E-value: 4.29e-06
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| FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
21-79 | 6.61e-06 | |||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 45.94 E-value: 6.61e-06
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| Era | COG1159 | GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
287-369 | 4.99e-05 | |||||
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 45.36 E-value: 4.99e-05
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| EF-hand_7 | pfam13499 | EF-hand domain pair; |
24-79 | 5.04e-05 | |||||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 41.47 E-value: 5.04e-05
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| YfjP | cd11383 | YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
285-363 | 5.26e-05 | |||||
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 43.48 E-value: 5.26e-05
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| era | PRK00089 | GTPase Era; Reviewed |
287-369 | 5.88e-05 | |||||
GTPase Era; Reviewed Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 45.04 E-value: 5.88e-05
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| EF-hand_4 | pfam12763 | Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
15-107 | 1.22e-04 | |||||
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species. Pssm-ID: 289529 Cd Length: 104 Bit Score: 41.20 E-value: 1.22e-04
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| Era | cd04163 | E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
287-367 | 2.02e-04 | |||||
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA. Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 42.06 E-value: 2.02e-04
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| EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
24-79 | 4.02e-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: 35.99 E-value: 4.02e-03
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| EFh_PI-PLCeta2 | cd16221 | EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also ... |
21-82 | 4.22e-03 | |||||
EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2, or phosphoinositide phospholipase C-like 4, or phospholipase C-like protein 4 (PLC-L4), or phospholipase C-eta-2 (PLC-eta2), 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 pituitary gland, pineal gland, retina, and lung, as well as in neuroendocrine cells. PI-PLC-eta2 has been implicated in the regulation of neuronal differentiation/maturation. It is required for retinoic acid-stimulated neurite growth. It may also in part function downstream of G-protein-coupled receptors and play an important role in the formation and maintenance of the neuronal network in the postnatal brain. Moreover, PI-PLC-eta2 acts as a Ca2+ sensor that shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Its activation can be triggered either by intracellular calcium mobilization or by G beta-gamma signaling. PI-PLC-eta2 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: 320051 [Multi-domain] Cd Length: 141 Bit Score: 37.99 E-value: 4.22e-03
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| EFh_PI-PLC | cd15898 | EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
20-79 | 6.39e-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. Pssm-ID: 320029 [Multi-domain] Cd Length: 137 Bit Score: 37.26 E-value: 6.39e-03
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