engulfment and cell motility protein 1 [Gallus gallus]
Protein Classification
engulfment and cell motility protein( domain architecture ID 10570670)
engulfment and cell motility protein acts in association with DOCK1 and CRK, and is involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| ELMO_ARM | pfam11841 | ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ... |
115-280 | 4.03e-82 | ||||
ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ELMO (Elongation and Cell motility) proteins and corresponds to the armadillo repeats domain (ARR). It may play an important role in defining the functions of the ELMO family members and may be functionally linked to the ELMO domain in these proteins, being involved in protein-protein interactions. : Pssm-ID: 463369 Cd Length: 154 Bit Score: 257.50 E-value: 4.03e-82
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| PH_ELMO1_CED-12 | cd13359 | Engulfment and cell motility protein 1 pleckstrin homology (PH) domain; DOCK2 (Dedicator of ... |
546-675 | 2.28e-77 | ||||
Engulfment and cell motility protein 1 pleckstrin homology (PH) domain; DOCK2 (Dedicator of cytokinesis 2), a hematopoietic cell-specific, atypical GEF, controls lymphocyte migration through Rac activation. A DOCK2-ELMO1 complex s necessary for DOCK2-mediated Rac signaling. DOCK2 contains a SH3 domain at its N-terminus, followed by a lipid binding DHR1 domain, and a Rac-binding DHR2 domain at its C-terminus. ELMO1, a mammalian homolog of C. elegans CED-12, contains the N-terminal RhoG-binding region, the ELMO domain, the PH domain, and the C-terminal sequence with three PxxP motifs. The C-terminal region of ELMO1, including the Pro-rich sequence, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle along with the PH domain of ELMO1. Autoinhibition of ELMO1 and DOCK2 is accomplished by the interactions of the EID and EAD domains and SH3 and DHR2 domains, respectively. The interaction of DOCK2 and ELMO1 mutually relieve their autoinhibition and results in the activation of Rac1. The PH domain of ELMO1 does not bind phosphoinositides due to the absence of key binding residues. It more closely resembles the FERM domain rather than other PH domains. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. : Pssm-ID: 270166 [Multi-domain] Cd Length: 126 Bit Score: 244.14 E-value: 2.28e-77
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| ELMO_CED12 | pfam04727 | ELMO/CED-12 family; This family represents a conserved domain which is found in a number of ... |
303-481 | 3.48e-54 | ||||
ELMO/CED-12 family; This family represents a conserved domain which is found in a number of eukaryotic proteins including CED-12, ELMO I and ELMO II. ELMO1 is a component of signalling pathways that regulate phagocytosis and cell migration and is the mammalian orthologue of the C. elegans gene, ced-12. CED-12 is required for the engulfment of dying cells and cell migration. In mammalian cells, ELMO1 interacts with Dock180 as part of the CrkII/Dock180/Rac pathway responsible for phagocytosis and cell migration. ELMO1 is ubiquitously expressed, although its expression is highest in the spleen, an organ rich in immune cells. ELMO1 has a PH domain and a polyproline sequence motif at its C terminus which are not present in this alignment. : Pssm-ID: 461411 Cd Length: 161 Bit Score: 183.58 E-value: 3.48e-54
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| Name | Accession | Description | Interval | E-value | ||||
| ELMO_ARM | pfam11841 | ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ... |
115-280 | 4.03e-82 | ||||
ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ELMO (Elongation and Cell motility) proteins and corresponds to the armadillo repeats domain (ARR). It may play an important role in defining the functions of the ELMO family members and may be functionally linked to the ELMO domain in these proteins, being involved in protein-protein interactions. Pssm-ID: 463369 Cd Length: 154 Bit Score: 257.50 E-value: 4.03e-82
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| PH_ELMO1_CED-12 | cd13359 | Engulfment and cell motility protein 1 pleckstrin homology (PH) domain; DOCK2 (Dedicator of ... |
546-675 | 2.28e-77 | ||||
Engulfment and cell motility protein 1 pleckstrin homology (PH) domain; DOCK2 (Dedicator of cytokinesis 2), a hematopoietic cell-specific, atypical GEF, controls lymphocyte migration through Rac activation. A DOCK2-ELMO1 complex s necessary for DOCK2-mediated Rac signaling. DOCK2 contains a SH3 domain at its N-terminus, followed by a lipid binding DHR1 domain, and a Rac-binding DHR2 domain at its C-terminus. ELMO1, a mammalian homolog of C. elegans CED-12, contains the N-terminal RhoG-binding region, the ELMO domain, the PH domain, and the C-terminal sequence with three PxxP motifs. The C-terminal region of ELMO1, including the Pro-rich sequence, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle along with the PH domain of ELMO1. Autoinhibition of ELMO1 and DOCK2 is accomplished by the interactions of the EID and EAD domains and SH3 and DHR2 domains, respectively. The interaction of DOCK2 and ELMO1 mutually relieve their autoinhibition and results in the activation of Rac1. The PH domain of ELMO1 does not bind phosphoinositides due to the absence of key binding residues. It more closely resembles the FERM domain rather than other PH domains. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270166 [Multi-domain] Cd Length: 126 Bit Score: 244.14 E-value: 2.28e-77
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| PH_12 | pfam16457 | Pleckstrin homology domain; |
548-674 | 2.63e-54 | ||||
Pleckstrin homology domain; Pssm-ID: 465123 [Multi-domain] Cd Length: 128 Bit Score: 182.46 E-value: 2.63e-54
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| ELMO_CED12 | pfam04727 | ELMO/CED-12 family; This family represents a conserved domain which is found in a number of ... |
303-481 | 3.48e-54 | ||||
ELMO/CED-12 family; This family represents a conserved domain which is found in a number of eukaryotic proteins including CED-12, ELMO I and ELMO II. ELMO1 is a component of signalling pathways that regulate phagocytosis and cell migration and is the mammalian orthologue of the C. elegans gene, ced-12. CED-12 is required for the engulfment of dying cells and cell migration. In mammalian cells, ELMO1 interacts with Dock180 as part of the CrkII/Dock180/Rac pathway responsible for phagocytosis and cell migration. ELMO1 is ubiquitously expressed, although its expression is highest in the spleen, an organ rich in immune cells. ELMO1 has a PH domain and a polyproline sequence motif at its C terminus which are not present in this alignment. Pssm-ID: 461411 Cd Length: 161 Bit Score: 183.58 E-value: 3.48e-54
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| Name | Accession | Description | Interval | E-value | ||||
| ELMO_ARM | pfam11841 | ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ... |
115-280 | 4.03e-82 | ||||
ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ELMO (Elongation and Cell motility) proteins and corresponds to the armadillo repeats domain (ARR). It may play an important role in defining the functions of the ELMO family members and may be functionally linked to the ELMO domain in these proteins, being involved in protein-protein interactions. Pssm-ID: 463369 Cd Length: 154 Bit Score: 257.50 E-value: 4.03e-82
|
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| PH_ELMO1_CED-12 | cd13359 | Engulfment and cell motility protein 1 pleckstrin homology (PH) domain; DOCK2 (Dedicator of ... |
546-675 | 2.28e-77 | ||||
Engulfment and cell motility protein 1 pleckstrin homology (PH) domain; DOCK2 (Dedicator of cytokinesis 2), a hematopoietic cell-specific, atypical GEF, controls lymphocyte migration through Rac activation. A DOCK2-ELMO1 complex s necessary for DOCK2-mediated Rac signaling. DOCK2 contains a SH3 domain at its N-terminus, followed by a lipid binding DHR1 domain, and a Rac-binding DHR2 domain at its C-terminus. ELMO1, a mammalian homolog of C. elegans CED-12, contains the N-terminal RhoG-binding region, the ELMO domain, the PH domain, and the C-terminal sequence with three PxxP motifs. The C-terminal region of ELMO1, including the Pro-rich sequence, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle along with the PH domain of ELMO1. Autoinhibition of ELMO1 and DOCK2 is accomplished by the interactions of the EID and EAD domains and SH3 and DHR2 domains, respectively. The interaction of DOCK2 and ELMO1 mutually relieve their autoinhibition and results in the activation of Rac1. The PH domain of ELMO1 does not bind phosphoinositides due to the absence of key binding residues. It more closely resembles the FERM domain rather than other PH domains. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270166 [Multi-domain] Cd Length: 126 Bit Score: 244.14 E-value: 2.28e-77
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| PH_12 | pfam16457 | Pleckstrin homology domain; |
548-674 | 2.63e-54 | ||||
Pleckstrin homology domain; Pssm-ID: 465123 [Multi-domain] Cd Length: 128 Bit Score: 182.46 E-value: 2.63e-54
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| ELMO_CED12 | pfam04727 | ELMO/CED-12 family; This family represents a conserved domain which is found in a number of ... |
303-481 | 3.48e-54 | ||||
ELMO/CED-12 family; This family represents a conserved domain which is found in a number of eukaryotic proteins including CED-12, ELMO I and ELMO II. ELMO1 is a component of signalling pathways that regulate phagocytosis and cell migration and is the mammalian orthologue of the C. elegans gene, ced-12. CED-12 is required for the engulfment of dying cells and cell migration. In mammalian cells, ELMO1 interacts with Dock180 as part of the CrkII/Dock180/Rac pathway responsible for phagocytosis and cell migration. ELMO1 is ubiquitously expressed, although its expression is highest in the spleen, an organ rich in immune cells. ELMO1 has a PH domain and a polyproline sequence motif at its C terminus which are not present in this alignment. Pssm-ID: 461411 Cd Length: 161 Bit Score: 183.58 E-value: 3.48e-54
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| PH_PLC_ELMO1 | cd01248 | Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The ... |
556-673 | 4.97e-26 | ||||
Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The C-terminal region of ELMO1, the PH domain and Pro-rich sequences, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle allowing for DOCK mediated Rac1 activation. ELMO1, a mammalian homolog of C. elegans CED-12, contains an N-terminal RhoG-binding region, a ELMO domain, a PH domain, and a C-terminal sequence with three PxxP motifs. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). All PLCs, except for PLCzeta, have a PH domain which is for most part N-terminally located, though lipid binding specificity is not conserved between them. In addition PLC gamma contains a split PH domain within its catalytic domain that is separated by 2 SH2 domains and a single SH3 domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 269952 Cd Length: 108 Bit Score: 102.79 E-value: 4.97e-26
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