Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Beta-crystallin B1B; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Gamma-crystallin A; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Gap junction alpha-3 protein; Structural component of lens fiber gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Gap junction alpha-8 protein; Structural component of eye lens gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore ; Belongs to the connexin family. Alpha-type (group II) subfamily.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Lens fiber membrane intrinsic protein; Present in the thicker 16-17 nm junctions of mammalian lens fiber cells, where it may contribute to cell junctional organization. Acts as a receptor for calmodulin. May play an important role in both lens development and cataractogenesis; Belongs to the PMP-22/EMP/MP20 family.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Lens fiber major intrinsic protein; Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). Belongs to the MIP/aquaporin (TC 1.A.8) family.

Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).

Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Beta-crystallin B1B; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Gamma-crystallin A; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Gap junction alpha-3 protein; Structural component of lens fiber gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.

Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Gap junction alpha-8 protein; Structural component of eye lens gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore ; Belongs to the connexin family. Alpha-type (group II) subfamily.

Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Lens fiber major intrinsic protein; Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). Belongs to the MIP/aquaporin (TC 1.A.8) family.

Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens.

Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity).