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| GABARAPL2 | Gamma-aminobutyric acid receptor-associated protein-like 2; Ubiquitin-like modifier involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved [...] (117 aa) | |||
| VAMP3 | Vesicle-associated membrane protein 3; SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network; Belongs to the synaptobrevin family (100 aa) | |||
| PLLP | Plasmolipin; Appears to be involved in myelination. Could also participate in ion transport events as addition of plasmolipin to lipid bilayers induces the formation of ion channels, which are voltage-dependent and K(+)-selective (By similarity); Belongs to the MAL family (182 aa) | |||
| DEFB129 | Beta-defensin 129; Has antibacterial activity; Defensins, beta (183 aa) | |||
| DEFB118 | Beta-defensin 118; Has antibacterial activity; Defensins, beta (123 aa) | |||
| DEFA4 | 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; Defensins, alpha (97 aa) | |||
| DEFB1 | 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; Belongs to the beta-defensin family (68 aa) | |||
| NINJ2 | Ninjurin-2; Homophilic cell adhesion molecule that promotes axonal growth. May play a role in nerve regeneration and in the formation and function of other tissues (188 aa) | |||
| DEFB114 | Beta-defensin 114; Has a salt-sensitive antimicrobial activity against Gram-negative bacteria, including E.coli, Gram-positive, including S.aureus, and fungi, including C.albicans. Binds to and neutralizes bacterial lipopolysaccharides (LPS), abolishing TNF production by macrophages challenged with LPS. Rescues the LPS- induced reduction of sperm motility in vitro and may protect from LPS-induced lethality; Defensins, beta (69 aa) | |||
| DEFB112 | Beta-defensin 112; Has antibacterial activity; Defensins, beta (113 aa) | |||
| TMEM86B | Lysoplasmalogenase; Enzyme catalyzing the degradation of lysoplasmalogen. Lysoplasmalogens are formed by the hydrolysis of the abundant membrane glycerophospholipids plasmalogens. May control the respective levels of plasmalogens and lysoplasmalogens in cells and modulate cell membrane properties; Belongs to the TMEM86 family (226 aa) | |||
| DEFB124 | Beta-defensin 124; Has antibacterial activity; Defensins, beta (71 aa) | |||
| DEFA3 | Neutrophil defensin 3; 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; Defensins, alpha (94 aa) | |||
| DEFA5 | 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; Defensins, alpha (94 aa) | |||
| DEFB108B | Beta-defensin 108B; Has antibacterial activity; Defensins, beta (73 aa) | |||
| DEFB128 | Beta-defensin 128; Has antibacterial activity; Defensins, beta (93 aa) | |||
| DEFB131 | Beta-defensin 131A; Has antibacterial activity (Probable). Upon stimulation with lipoteichoic acid, promotes cytokines and chemokines production and secretion; Belongs to the beta-defensin family (70 aa) | |||
| DEFB110 | Beta-defensin 110; Has antibacterial activity; Defensins, beta (67 aa) | |||
| DEFB123 | Beta-defensin 123; Has antibacterial activity; Belongs to the beta-defensin family (67 aa) | |||
| DEFB119 | Defensin beta 119 (88 aa) | |||
| DEFB135 | Beta-defensin 135; Has antibacterial activity; Defensins, beta (77 aa) | |||
| DEFB136 | Beta-defensin 136; Has antibacterial activity; Defensins, beta (78 aa) | |||
| DEFB132 | Beta-defensin 132; Has antibacterial activity; Defensins, beta (95 aa) | |||
| TMEM128 | Transmembrane protein 128 (165 aa) | |||
| GUCA1A | Guanylyl cyclase-activating protein 1; Stimulates retinal guanylyl cyclase when free calcium ions concentration is low and inhibits guanylyl cyclase when free calcium ions concentration is elevated. This Ca(2+)-sensitive regulation of retinal guanylyl cyclase is a key event in recovery of the dark state of rod photoreceptors following light exposure; EF-hand domain containing (201 aa) | |||
| TMUB2 | Transmembrane and ubiquitin like domain containing 2 (321 aa) | |||
