RecName: Full=Atypical chemokine receptor 1; AltName: Full=Duffy antigen/chemokine receptor; AltName: CD_antigen=CD234
7tmA_ACKR1_DARC domain-containing protein( domain architecture ID 11606633)
7tmA_ACKR1_DARC domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
7tmA_ACKR1_DARC | cd15010 | Duffy antigen receptor for chemokines, member of the class A family of seven-transmembrane G ... |
54-310 | 2.76e-131 | |||||
Duffy antigen receptor for chemokines, member of the class A family of seven-transmembrane G protein-coupled receptors; Atypical chemokine receptor 1 (ACKR1), also known as DARC (Duffy antigen receptor for chemokines) or Fy glycoprotein (GpFy), was originally identified on erythrocytes. ACKR1 is also ubiquitously expressed by endothelial cells of venules and is highly promiscuous among all chemokine receptor. It binds many proinflammatory chemokines from both the CC and CXC subfamilies, including CCL2, CCL5, CCL7, CCL11, CXCL1, CXCL2, CXCL3, and CXCL5. Erythrocyte ACKR1 is thought to act as a chemokine sink, limiting the levels of circulating chemokines, thereby controlling leukocyte activation. ACKR1-deficient erythrocytes are shown to confer resistance to the malarial parasite, Plasmodium vivax. On the other hand, ACKR1-expressing endothelial cells can internalize chemokines. ACKR1-internalized chemokines can be moved intact across the endothelium and promotes neutrophil transmigration. Unlike the classical chemokine receptors that contain a conserved DRYLAIV motif in the second intracellular loop, which is required for G-protein coupling, the ACKRs lack this conserved motif and fail to couple to G-proteins and induce classical GPCR signaling. Five receptors have been identified for the ACKR family, including CC-Chemokine Receptors like 1 and 2 (CCRL1 and CCRL2), CXCR7, DARC, and D6. Both ACKR1 (DARC) and ACKR3 (CXCR7) show low sequence homology to the classic chemokine receptors. : Pssm-ID: 410631 Cd Length: 257 Bit Score: 374.51 E-value: 2.76e-131
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Name | Accession | Description | Interval | E-value | |||||
7tmA_ACKR1_DARC | cd15010 | Duffy antigen receptor for chemokines, member of the class A family of seven-transmembrane G ... |
54-310 | 2.76e-131 | |||||
Duffy antigen receptor for chemokines, member of the class A family of seven-transmembrane G protein-coupled receptors; Atypical chemokine receptor 1 (ACKR1), also known as DARC (Duffy antigen receptor for chemokines) or Fy glycoprotein (GpFy), was originally identified on erythrocytes. ACKR1 is also ubiquitously expressed by endothelial cells of venules and is highly promiscuous among all chemokine receptor. It binds many proinflammatory chemokines from both the CC and CXC subfamilies, including CCL2, CCL5, CCL7, CCL11, CXCL1, CXCL2, CXCL3, and CXCL5. Erythrocyte ACKR1 is thought to act as a chemokine sink, limiting the levels of circulating chemokines, thereby controlling leukocyte activation. ACKR1-deficient erythrocytes are shown to confer resistance to the malarial parasite, Plasmodium vivax. On the other hand, ACKR1-expressing endothelial cells can internalize chemokines. ACKR1-internalized chemokines can be moved intact across the endothelium and promotes neutrophil transmigration. Unlike the classical chemokine receptors that contain a conserved DRYLAIV motif in the second intracellular loop, which is required for G-protein coupling, the ACKRs lack this conserved motif and fail to couple to G-proteins and induce classical GPCR signaling. Five receptors have been identified for the ACKR family, including CC-Chemokine Receptors like 1 and 2 (CCRL1 and CCRL2), CXCR7, DARC, and D6. Both ACKR1 (DARC) and ACKR3 (CXCR7) show low sequence homology to the classic chemokine receptors. Pssm-ID: 410631 Cd Length: 257 Bit Score: 374.51 E-value: 2.76e-131
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Name | Accession | Description | Interval | E-value | |||||
7tmA_ACKR1_DARC | cd15010 | Duffy antigen receptor for chemokines, member of the class A family of seven-transmembrane G ... |
54-310 | 2.76e-131 | |||||
Duffy antigen receptor for chemokines, member of the class A family of seven-transmembrane G protein-coupled receptors; Atypical chemokine receptor 1 (ACKR1), also known as DARC (Duffy antigen receptor for chemokines) or Fy glycoprotein (GpFy), was originally identified on erythrocytes. ACKR1 is also ubiquitously expressed by endothelial cells of venules and is highly promiscuous among all chemokine receptor. It binds many proinflammatory chemokines from both the CC and CXC subfamilies, including CCL2, CCL5, CCL7, CCL11, CXCL1, CXCL2, CXCL3, and CXCL5. Erythrocyte ACKR1 is thought to act as a chemokine sink, limiting the levels of circulating chemokines, thereby controlling leukocyte activation. ACKR1-deficient erythrocytes are shown to confer resistance to the malarial parasite, Plasmodium vivax. On the other hand, ACKR1-expressing endothelial cells can internalize chemokines. ACKR1-internalized chemokines can be moved intact across the endothelium and promotes neutrophil transmigration. Unlike the classical chemokine receptors that contain a conserved DRYLAIV motif in the second intracellular loop, which is required for G-protein coupling, the ACKRs lack this conserved motif and fail to couple to G-proteins and induce classical GPCR signaling. Five receptors have been identified for the ACKR family, including CC-Chemokine Receptors like 1 and 2 (CCRL1 and CCRL2), CXCR7, DARC, and D6. Both ACKR1 (DARC) and ACKR3 (CXCR7) show low sequence homology to the classic chemokine receptors. Pssm-ID: 410631 Cd Length: 257 Bit Score: 374.51 E-value: 2.76e-131
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7tm_GPCRs | cd14964 | seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ... |
55-298 | 1.49e-10 | |||||
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections. Pssm-ID: 410628 [Multi-domain] Cd Length: 267 Bit Score: 60.90 E-value: 1.49e-10
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7tmA_Chemokine_R | cd14984 | classical and atypical chemokine receptors, member of the class A family of ... |
57-301 | 2.26e-10 | |||||
classical and atypical chemokine receptors, member of the class A family of seven-transmembrane G protein-coupled receptors; Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines. In addition to these classical chemokine receptors, there exists a subfamily of atypical chemokine receptors (ACKRs) that are unable to couple to G-proteins and, instead, they preferentially mediate beta-arrestin dependent processes, such as receptor internalization, after ligand binding. The classical chemokine receptors contain a conserved DRYLAIV motif in the second intracellular loop, which is required for G-protein coupling. However, the ACKRs lack this conserved motif and fail to couple to G-proteins and induce classical GPCR signaling. Five receptors have been identified for the ACKR family, including CC-chemokine receptors like 1 and 2 (CCRL1 and CCRL2), CXCR7, Duffy antigen receptor for chemokine (DARC), and D6. Both ACKR1 (DARC) and ACKR3 (CXCR7) show low sequence homology to the classic chemokine receptors. Pssm-ID: 341319 [Multi-domain] Cd Length: 278 Bit Score: 60.31 E-value: 2.26e-10
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7tmA_CXCR1_2 | cd15178 | CXC chemokine receptor types 1 and 2, member of the class A family of seven-transmembrane G ... |
162-301 | 1.10e-07 | |||||
CXC chemokine receptor types 1 and 2, member of the class A family of seven-transmembrane G protein-coupled receptors; CXCR1 and CXCR2 are closely related chemotactic receptors for a group of CXC chemokines distinguished by the presence of the amino acid motif ELR immediately adjacent to their CXC motif. Expression of CXCR1 and CXCR2 is strictly controlled in neutrophils by external stimuli such as lipopolysaccharide (LPS), tumor necrosis factor (TNF)-alpha, Toll-like receptor agonists, and nitric oxide. CXCL8 (formerly known as interleukin-8) binds with high-affinity and activates both receptors. CXCR1 also binds CXCL7 (neutrophil-activating protein-2), whereas CXCR2 non-selectively binds to all seven ELR-positive chemokines (CXCL1-7). Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines. Pssm-ID: 341333 [Multi-domain] Cd Length: 279 Bit Score: 52.28 E-value: 1.10e-07
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7tmA_ACKR2_D6 | cd15188 | atypical chemokine receptor 2, member of the class A family of seven-transmembrane G ... |
163-301 | 1.61e-06 | |||||
atypical chemokine receptor 2, member of the class A family of seven-transmembrane G protein-coupled receptors; ACKR2 (also known as D6) binds non-selectively to all inflammatory CC-chemokines, but not to homeostatic CC-chemokines involved in controlling the migration of cells. Unlike the classical chemokine receptors that contain a conserved DRYLAIV motif in the second intracellular loop, which is required for G-protein coupling, the ACKRs lack this conserved motif and fail to couple to G-proteins and induce classical GPCR signaling. Five receptors have been identified for the ACKR family, including CC-chemokine receptors like 1 and 2 (CCRL1 and CCRL2), CXCR7, Duffy antigen receptor for chemokine (DARC), and D6. Both ACKR1 (DARC) and ACKR3 (CXCR7) show low sequence homology to the classic chemokine receptors. Pssm-ID: 320316 [Multi-domain] Cd Length: 278 Bit Score: 48.63 E-value: 1.61e-06
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7tmA_CXCR5 | cd15181 | CXC chemokine receptor type 5, member of the class A family of seven-transmembrane G ... |
58-301 | 2.85e-05 | |||||
CXC chemokine receptor type 5, member of the class A family of seven-transmembrane G protein-coupled receptors; CXCR5 is a B-cell selective receptor that binds specifically to the homeostatic chemokine CXCL13 and regulates adaptive immunity. The receptor is found on all peripheral blood and tonsillar B cells and is involved in lymphocyte migration (homing) to specific tissues and development of normal lymphoid tissue. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines. Pssm-ID: 341336 [Multi-domain] Cd Length: 281 Bit Score: 45.12 E-value: 2.85e-05
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7tmA_CCR8 | cd15187 | CC chemokine receptor type 8, member of the class A family of seven-transmembrane G ... |
239-301 | 3.07e-03 | |||||
CC chemokine receptor type 8, member of the class A family of seven-transmembrane G protein-coupled receptors; CCR8, the receptor for the CC chemokines CCL1 and CC16, is highly expressed on allergen-specific T-helper type 2 cells, and is implicated in the pathogenesis of human asthma. CCL1- and CCR8-expressing CD4+ effector T lymphocytes are shown to have a critical role in lung mucosal inflammatory responses. CCR8 is also a functional receptor for CCL16, a liver-expressed CC chemokine that involved in attracting lymphocytes, dendritic cells, and monocytes. Chemokines are principal regulators for leukocyte trafficking, recruitment, and activation. Chemokine family membership is defined on the basis of sequence homology and on the presence of variations on a conserved cysteine motif, which allows the family to further divide into four subfamilies (CC, CXC, XC, and CX3C). Chemokines interact with seven-transmembrane receptors which are typically coupled to G protein for signaling. Currently, there are ten known receptors for CC chemokines, seven for CXC chemokines, and single receptors for the XC and CX3C chemokines. Pssm-ID: 320315 [Multi-domain] Cd Length: 276 Bit Score: 38.63 E-value: 3.07e-03
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