| Tissue Specificity | Detected in aqueous humor. Detected in the eye (at protein level). Widely expressed. Highly expressed in various types of muscle, ciliary body, papillary sphincter, skeletal muscle, heart, and bone marrow-derived mesenchymal stem cells. Expressed predominantly in the retina. In normal eyes, found in the inner uveal meshwork region and the anterior portion of the meshwork. In contrast, in many glaucomatous eyes, it is found in more regions of the meshwork and seems to be expressed at higher levels than in normal eyes, regardless of the type or clinical severity of glaucoma. The myocilin 35 kDa fragment is detected in aqueous humor and to a lesser extent in iris and ciliary body. |
| Post Translational Modifications | Different isoforms may arise by post-translational modifications. Glycosylated. Palmitoylated. Undergoes a calcium-dependent proteolytic cleavage at Arg-226 by CAPN2 in the endoplasmic reticulum. The result is the production of two fragments, one of 35 kDa containing the C-terminal olfactomedin-like domain, and another of 20 kDa containing the N-terminal leucine zipper-like domain. |
| Function | Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork. |
| Peptide Name | MyocilinMyocilin 55 Kda SubunitTrabecular Meshwork-Induced Glucocorticoid Response Protein Cleaved Into - Myocilin - N-Terminal FragmentMyocilin 20 Kda N-Terminal Fragment - Myocilin - C-Terminal FragmentMyocilin 35 Kda N-Terminal Fragment |
| Cellular Localisation | SecretedGolgi ApparatusCytoplasmic VesicleExtracellular SpaceExtracellular MatrixExtracellular ExosomeMitochondrionMitochondrion Intermembrane SpaceMitochondrion Inner MembraneMitochondrion Outer MembraneRough Endoplasmic ReticulumCell ProjectionCiliumLocated Preferentially In The Ciliary Rootlet And Basal Body Of The Connecting Cilium Of Photoreceptor CellsAnd In The Rough Endoplasmic ReticulumIt Is Only Imported To Mitochondria In The Trabecular MeshworkLocalizes To The Golgi Apparatus In Schlemm's Canal Endothelial CellsAppears In The Extracellular Space Of Trabecular Meshwork Cells By An Unconventional MechanismLikely Associated With Exosome-Like VesiclesLocalizes In Trabecular Meshwork Extracellular MatrixMyocilinC-Terminal Fragment: SecretedN-Terminal Fragment: Endoplasmic ReticulumRemains Retained In The Endoplasmic Reticulum |
| Alternative Peptide Names | Myocilin proteinMyocilin 55 Kda Subunit proteinTrabecular Meshwork-Induced Glucocorticoid Response Protein Cleaved Into - Myocilin - N-Terminal Fragment proteinMyocilin 20 Kda N-Terminal Fragment - Myocilin - C-Terminal Fragment proteinMyocilin 35 Kda N-Terminal Fragment proteinMYOC proteinGLC1A proteinTIGR protein |
Information sourced from Uniprot.org
