GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R.

Neutrophil defensin 1; Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.

GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R.

Neutrophil defensin 2; Defensin 2 and defensin 3 have antibiotic, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.

GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R.

Neutrophil defensin 4; Has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi. Protects blood cells against infection with HIV-1 (in vitro). Inhibits corticotropin (ACTH)-stimulated corticosterone production.

GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R.

Defensin-5; Has antimicrobial activity against Gram-negative and Gram- positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing.

GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R.

Defensin-6; Has very low antimicrobial activity against Gram-negative and Gram-positive bacteria. May protect cells against infection with HIV-1.

GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R.

Beta-defensin 1; Has bactericidal activity. May act as a ligand for C-C chemokine receptor CCR6. Positively regulates the sperm motility and bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and triggers Ca2+ mobilization in the sperm which is important for its motility.

GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1; Has ADP-ribosyltransferase activity toward GLP1R.

Beta-defensin 4A; Exhibits antimicrobial activity against Gram-negative bacteria and Gram-positive bacteria. May act as a ligand for C-C chemokine receptor CCR6. Can bind to both human and mouse CCR6 and induce chemotactic activity of CCR6-expressing cells. Belongs to the beta-defensin family. LAP/TAP subfamily.

Copper transport protein ATOX1; Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense; Belongs to the ATX1 family.

Copper-transporting ATPase 1; May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.

Copper transport protein ATOX1; Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense; Belongs to the ATX1 family.

PDZ domain-containing protein 11; Mediates docking of ADAM10 to zonula adherens by interacting with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10- binding protein TSPAN33.

Copper-transporting ATPase 1; May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.

Copper transport protein ATOX1; Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense; Belongs to the ATX1 family.

Copper-transporting ATPase 1; May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.

Clusterin alpha chain; [Isoform 1]: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and sub [...]

Copper-transporting ATPase 1; May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.

PDZ domain-containing protein 11; Mediates docking of ADAM10 to zonula adherens by interacting with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10- binding protein TSPAN33.

Copper-transporting ATPase 1; May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.

Natural resistance-associated macrophage protein 1; Divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Macrophage-specific membrane transport function. Controls natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis [...]

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

BPI fold-containing family A member 1; Lipid-binding protein which shows high specificity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC). Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway surface liquid ho [...]

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

BPI fold-containing family A member 2; Has strong antibacterial activity against P. aeruginosa. Belongs to the BPI/LBP/Plunc superfamily. Plunc family.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

BPI fold-containing family B member 1; May play a role in innate immunity in mouth, nose and lungs. Binds bacterial lipopolysaccharide (LPS) and modulates the cellular responses to LPS; Belongs to the BPI/LBP/Plunc superfamily. Plunc family.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Cathepsin G; Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, antibacterial activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe-CH2Cl and phenylmethylsulfonyl fluoride.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Neutrophil defensin 1; Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.

Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Neutrophil defensin 2; Defensin 2 and defensin 3 have antibiotic, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.