HRG

Histidine-rich glycoprotein

526 amino acids

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Inhibits rosette formation. Acts as an adapter protein and implicated in regulating many processes such as immune complex and pathogen clearance, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Binds T-cells and alters the cell morphology Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2 (By similarity). Tethers plasminogen to the cell surface.

58.877 kDa

single

ATLQCSWALTPTDCKTTKPLAEKALDLINKWRRDGYLFQLLRVADAHLDGAESATVYYLVLDVKETDCSVLSRKHWEDCDPDLTKRPSLDVIGQCKVIATRYSDEYQTLRLNDFNCTTSSVSSALANTKDSPVLFDFIEDTEPFRKSADKALEVYKSESEAYASFRVDRVERVTRVKGGERTNYYVDFSVRNCSRSHFHRHPAFGFCRADLSFDVEASNLENPEDVIISCEVFNFEEHGNISGFRPHLGKTPLGTDGSRDHHHPHKPHKFGCPPPQEGEDFSEGPPLQGGTPPLSPPFRPRCRHRPFGTNETHRFPHHRISVNIIHRPPPHGHHPHGPPPHGHHPHGPPPHGHPPHGPPPRHPPHGPPPHGHPPHGPPPHGHPPHGPPPHGHPPHGPPPHGHPPHGHGFHDHGPCDPPSHKEGPQDLHQHAMGPPPKHPGKRGPGKGHFPFHWRRIGSVYQLPPLQKGEVLPLPEANFPQLLLRNHTHPLKPEIQPFPQVASERCPEEFNGEFAQLSKFFPSTFPK

HRG

Histidine-rich glycoprotein

526 amino acids

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Inhibits rosette formation. Acts as an adapter protein and implicated in regulating many processes such as immune complex and pathogen clearance, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Binds T-cells and alters the cell morphology Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2 (By similarity). Tethers plasminogen to the cell surface.

58.877 kDa

single

ATLQCSWALTPTDCKTTKPLAEKALDLINKWRRDGYLFQLLRVADAHLDGAESATVYYLVLDVKETDCSVLSRKHWEDCDPDLTKRPSLDVIGQCKVIATRYSDEYQTLRLNDFNCTTSSVSSALANTKDSPVLFDFIEDTEPFRKSADKALEVYKSESEAYASFRVDRVERVTRVKGGERTNYYVDFSVRNCSRSHFHRHPAFGFCRADLSFDVEASNLENPEDVIISCEVFNFEEHGNISGFRPHLGKTPLGTDGSRDHHHPHKPHKFGCPPPQEGEDFSEGPPLQGGTPPLSPPFRPRCRHRPFGTNETHRFPHHRISVNIIHRPPPHGHHPHGPPPHGHHPHGPPPHGHPPHGPPPRHPPHGPPPHGHPPHGPPPHGHPPHGPPPHGHPPHGPPPHGHPPHGHGFHDHGPCDPPSHKEGPQDLHQHAMGPPPKHPGKRGPGKGHFPFHWRRIGSVYQLPPLQKGEVLPLPEANFPQLLLRNHTHPLKPEIQPFPQVASERCPEEFNGEFAQLSKFFPSTFPK

HRG

Histidine-rich glycoprotein

525 amino acids

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis.

59.578 kDa

MKALIAALLLITLQYSCAVSPTDCSAVEPEAEKALDLINKRRRDGYLFQLLRIADAHLDRVENTTVYYLVLDVQESDCSVLSRKYWNDCEPPDSRRPSEIVIGQCKVIATRHSHESQDLRVIDFNCTTSSVSSALANTKDSPVLIDFFEDTERYRKQANKALEKYKEENDDFASFRVDRIERVARVRGGEGTGYFVDFSVRNCPRHHFPRHPNVFGFCRADLFYDVEALDLESPKNLVINCEVFDPQEHENINGVPPHLGHPFHWGGHERSSTTKPPFKPHGSRDHHHPHKPHEHGPPPPPDERDHSHGPPLPQGPPPLLPMSCSSCQHATFGTNGAQRHSHNNNSSDLHPHKHHSHEQHPHGHHPHAHHPHEHDTHRQHPHGHHPHGHHPHGHHPHGHHPHGHHPHCHDFQDYGPCDPPPHNQGHCCHGHGPPPGHLRRRGPGKGPRPFHCRQIGSVYRLPPLRKGEVLPLPEANFPSFPLPHHKHPLKPDNQPFPQSVSESCPGKFKSGFPQVSMFFTHTFPK

Hrg

Histidine-rich glycoprotein

525 amino acids

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis (By similarity). Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2.

59.163 kDa

MKVLTTALLLVTLQCSHALSPTNCDASEPLAEKVLDLINKGRRSGYVFELLRVSDAHLDRAGTATVYYLALDVIESDCWVLSTKAQDDCLPSRWQSEIVIGQCKVIATRYSNESQDLSVNGYNCTTSSVSSALRNTKDSPVLLDFFEDSELYRKQARKALDKYKTDNGDFASFRVERAERVIRARGGERTNYYVEFSMRNCSTQHFPRSPLVFGFCRALLSYSIETSDLETPDSIDINCEVFNIEDHKDTSDMKPHWGHERPLCDKHLCKLSGSRDHHHTHKTDKLGCPPPPEGKDNSDRPRLQEGALPQLPPGYPPHSGANRTHRPSYNHSCNEHPCHGHRPHGHHPHSHHPPGHHSHGHHPHGHHPHSHHSHGHHPPGHHPHGHHPHGHHPHGHHPHGHHPHGHDFLDYGPCDPPSNSQELKGQYHRGYGPPHGHSRKRGPGKGLFPFHHQQIGYVYRLPPLNIGEVLTLPEANFPSFSLPNCNRSLQPEIQPFPQTASRSCPGKFESEFPQISKFFGYTPPK

Hrg

Histidine-rich glycoprotein

525 amino acids

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Inhibits rosette formation. Acts as an adapter protein and implicated in regulating many processes such as immune complex and pathogen clearance, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2 (By similarity).

59.049 kDa

MKVLTTALLLVTLQCSHALSPTNCDASKPLAEKVLDLINKGRRSGYTFQLLRVSDAHLDRVETATIYYLVLDVVESDCWVLSTKAQDECLPAMRTSEVVIGQCKVIATRYSNESQDLSVNGYNCTMRSVSSAYINTKDSPVLVDSFEDSEPYRKLARKALDKYKAENGDFASFRVERAERVIRMRGGERTSYFIEFSVRNCSTQHFPRHPPVFGLCRVVLTYSTEASDLETPEYTDLICEVFNTEDLKNRSDMKPHRGHEHPHCDKHLCKLSGPRDHHHTHKTHEIGCPPPPEGKDNSDRPPLQEGALPQMLPGHSGPSGTNRSHRPPHNHSCNEHPCHGQHPHGHHPHGQHPHGHHPHGQHPHGHHPHGQHPHGHHPHGQHPHGHHPHGHHPHGDHPHGHHPHGHDFLDYGPCDPPSNSQELKGQYHRGHGPPHGHSRKRGPGKGLFPFHQRQIGYVYRLPPLNVGEVLTPPEANFPIFSLPNCNRPPQPEIRPFPQTASKSCPGKFEGKFPQVSNFFEHTPPK

HRG

Histidine-rich glycoprotein

525 amino acids

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis.

59.578 kDa

MKALIAALLLITLQYSCAVSPTDCSAVEPEAEKALDLINKRRRDGYLFQLLRIADAHLDRVENTTVYYLVLDVQESDCSVLSRKYWNDCEPPDSRRPSEIVIGQCKVIATRHSHESQDLRVIDFNCTTSSVSSALANTKDSPVLIDFFEDTERYRKQANKALEKYKEENDDFASFRVDRIERVARVRGGEGTGYFVDFSVRNCPRHHFPRHPNVFGFCRADLFYDVEALDLESPKNLVINCEVFDPQEHENINGVPPHLGHPFHWGGHERSSTTKPPFKPHGSRDHHHPHKPHEHGPPPPPDERDHSHGPPLPQGPPPLLPMSCSSCQHATFGTNGAQRHSHNNNSSDLHPHKHHSHEQHPHGHHPHAHHPHEHDTHRQHPHGHHPHGHHPHGHHPHGHHPHGHHPHCHDFQDYGPCDPPPHNQGHCCHGHGPPPGHLRRRGPGKGPRPFHCRQIGSVYRLPPLRKGEVLPLPEANFPSFPLPHHKHPLKPDNQPFPQSVSESCPGKFKSGFPQVSMFFTHTFPK

Hrg

Histidine-rich glycoprotein

525 amino acids

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis (By similarity). Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2.

59.163 kDa

MKVLTTALLLVTLQCSHALSPTNCDASEPLAEKVLDLINKGRRSGYVFELLRVSDAHLDRAGTATVYYLALDVIESDCWVLSTKAQDDCLPSRWQSEIVIGQCKVIATRYSNESQDLSVNGYNCTTSSVSSALRNTKDSPVLLDFFEDSELYRKQARKALDKYKTDNGDFASFRVERAERVIRARGGERTNYYVEFSMRNCSTQHFPRSPLVFGFCRALLSYSIETSDLETPDSIDINCEVFNIEDHKDTSDMKPHWGHERPLCDKHLCKLSGSRDHHHTHKTDKLGCPPPPEGKDNSDRPRLQEGALPQLPPGYPPHSGANRTHRPSYNHSCNEHPCHGHRPHGHHPHSHHPPGHHSHGHHPHGHHPHSHHSHGHHPPGHHPHGHHPHGHHPHGHHPHGHHPHGHDFLDYGPCDPPSNSQELKGQYHRGYGPPHGHSRKRGPGKGLFPFHHQQIGYVYRLPPLNIGEVLTLPEANFPSFSLPNCNRSLQPEIQPFPQTASRSCPGKFESEFPQISKFFGYTPPK

Hrg

Histidine-rich glycoprotein

525 amino acids

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Inhibits rosette formation. Acts as an adapter protein and implicated in regulating many processes such as immune complex and pathogen clearance, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2 (By similarity).

59.049 kDa

MKVLTTALLLVTLQCSHALSPTNCDASKPLAEKVLDLINKGRRSGYTFQLLRVSDAHLDRVETATIYYLVLDVVESDCWVLSTKAQDECLPAMRTSEVVIGQCKVIATRYSNESQDLSVNGYNCTMRSVSSAYINTKDSPVLVDSFEDSEPYRKLARKALDKYKAENGDFASFRVERAERVIRMRGGERTSYFIEFSVRNCSTQHFPRHPPVFGLCRVVLTYSTEASDLETPEYTDLICEVFNTEDLKNRSDMKPHRGHEHPHCDKHLCKLSGPRDHHHTHKTHEIGCPPPPEGKDNSDRPPLQEGALPQMLPGHSGPSGTNRSHRPPHNHSCNEHPCHGQHPHGHHPHGQHPHGHHPHGQHPHGHHPHGQHPHGHHPHGQHPHGHHPHGHHPHGDHPHGHHPHGHDFLDYGPCDPPSNSQELKGQYHRGHGPPHGHSRKRGPGKGLFPFHQRQIGYVYRLPPLNVGEVLTPPEANFPIFSLPNCNRPPQPEIRPFPQTASKSCPGKFEGKFPQVSNFFEHTPPK

HRG

Histidine-rich glycoprotein

396 amino acids

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Inhibits rosette formation. Acts as an adapter protein and implicated in regulating many processes such as immune complex and pathogen clearance, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2 (By similarity).

44.471 kDa

multiple

AVNPTGCDAVEPVAVRALDLINKGRDGYLFQLLRVADAHLDKVESIAVYYLVESDCPVLSRKHWDDCELNVTVIGQCKLAGPEDLSVNDFNCTTSSVSSALTNMRARGGEGTSYFLDFSVRNCSSHHFPRHHIFGFCRADLFYDVEASDLETPKDIVTNCEVFHRRFSAVQHHLGRPFHSGEHEHSPAGRPPFKPSGSKDHGHPHESYNFRCPPPLEHKNHSDSPPFQARAPLPFPPPGLRCPHPPFGTKGNHRPPHDHSSDEHHPHGHHPHGHHPHGHHPHGHHPPDNDFYDHGPCDPPPHRPPPRHSKERGPGKGHFRFHWRPTGYIHRLPSLKKGEVLPLPEANFPSFSLPNHNNPLQPEIQAFPQSASESCPGTFNIKFLHISKFFAYTLPK

HRG

Histidine-rich glycoprotein

396 amino acids

Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Inhibits rosette formation. Acts as an adapter protein and implicated in regulating many processes such as immune complex and pathogen clearance, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2 (By similarity).

44.471 kDa

multiple

AVNPTGCDAVEPVAVRALDLINKGRDGYLFQLLRVADAHLDKVESIAVYYLVESDCPVLSRKHWDDCELNVTVIGQCKLAGPEDLSVNDFNCTTSSVSSALTNMRARGGEGTSYFLDFSVRNCSSHHFPRHHIFGFCRADLFYDVEASDLETPKDIVTNCEVFHRRFSAVQHHLGRPFHSGEHEHSPAGRPPFKPSGSKDHGHPHESYNFRCPPPLEHKNHSDSPPFQARAPLPFPPPGLRCPHPPFGTKGNHRPPHDHSSDEHHPHGHHPHGHHPHGHHPHGHHPPDNDFYDHGPCDPPPHRPPPRHSKERGPGKGHFRFHWRPTGYIHRLPSLKKGEVLPLPEANFPSFSLPNHNNPLQPEIQAFPQSASESCPGTFNIKFLHISKFFAYTLPK