Tyrosine-protein kinase Abl; Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis; critical for embryonic epithelial morphogenesis regulating cell shape changes and cell migration. Plays a critical role in transducing embryonic midline repulsive cues; may regulate cytoskeletal dynamics underlying a growth cone's response to midline cues. The ability of pCC/MP2 axons to correctly interpret midline repulsive cues and stay on the ipsilateral side is dependent on the strength of both Slit/robo and Abl-dependent signaling pathways.

Heat shock protein 83; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Together with Hop and piwi, mediates canalization, also known as develop [...]

Tyrosine-protein kinase Abl; Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis; critical for embryonic epithelial morphogenesis regulating cell shape changes and cell migration. Plays a critical role in transducing embryonic midline repulsive cues; may regulate cytoskeletal dynamics underlying a growth cone's response to midline cues. The ability of pCC/MP2 axons to correctly interpret midline repulsive cues and stay on the ipsilateral side is dependent on the strength of both Slit/robo and Abl-dependent signaling pathways.

Phospholipase; Phosphatidylinositol binding; phospholipase D activity.

Tyrosine-protein kinase Abl; Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis; critical for embryonic epithelial morphogenesis regulating cell shape changes and cell migration. Plays a critical role in transducing embryonic midline repulsive cues; may regulate cytoskeletal dynamics underlying a growth cone's response to midline cues. The ability of pCC/MP2 axons to correctly interpret midline repulsive cues and stay on the ipsilateral side is dependent on the strength of both Slit/robo and Abl-dependent signaling pathways.

Failed axon connections; Together with Abl, involved in embryonic axonal development.

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Eukaryotic translation initiation factor 5A; mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis; Belongs to the eIF-5A family.

Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Eukaryotic translation initiation factor 5A; mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis; Belongs to the eIF-5A family.

Phosrestin-2; Regulates photoreceptor cell deactivation. Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade.

Phosrestin-1; Arrestin 2 (Arr2) encodes a protein involved in rhodopsin inactivation that contributes to photoreceptor maintenance and smell and sound perception.

Phosrestin-2; Regulates photoreceptor cell deactivation. Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade.

Dopamine/Ecdysteroid receptor (DopEcR) encodes a GPCR that shows ligand-biased activation. It can be activated by dopamine to increase cyclic AMP levels and by the insect steroid ecdysone to activate the MAPKinase pathway. It is widely expressed in the nervous system and can modulate a wide variety of complex behaviors including male courtship, locomotion, the response to stressful social interactions and the regulation of appetite.

Phosrestin-2; Regulates photoreceptor cell deactivation. Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade.

G protein alpha q subunit; Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Could be the transducin analog, an amplifier and one of the transducers of a visual impulse that performs the coupling between opsin and cGMP-phosphodiesterase. Could mediate a subset of olfactory and gustatory responses.

Phosrestin-2; Regulates photoreceptor cell deactivation. Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade.

Guanine nucleotide-binding protein subunit beta-2; G protein beta-subunit 76C (Gbeta76C) encodes a protein that forms a Gbeta-gamma complex that is anchored to the plasma membrane via lipid modification of the gamma-subunit. The Gbeta-gamma complex plays an essential role in phototransduction by presenting the Gqalpha-subunit to rhodopsin GPCRs for efficient activation, and preventing spontaneous GDP-GTP exchange on the Gqalpha-subunit.

Phosrestin-2; Regulates photoreceptor cell deactivation. Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade.

Chaoptin; Required for photoreceptor cell morphogenesis. Mediates homophilic cellular adhesion; Belongs to the chaoptin family.

Phosrestin-2; Regulates photoreceptor cell deactivation. Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade.

Protein kinase C, eye isozyme; This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. This isozyme is a negative regulator of the visual transduction cascade and has been shown to be required for photoreceptor cell inactivation and light adaptation. Negative regulation is dependent on interaction with scaffolding protein inaD. Acts in a hh-signaling pathway which regulates the Duox- dependent gut immune response to bacterial uracil; required for the activation of Cad99C and consequently Cad99C-dependent endosome formation, which is essential for the [...]

Phosrestin-2; Regulates photoreceptor cell deactivation. Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade.

Opsin Rh1; Neither inactivation nor afterpotential E (ninaE) encodes a protein that plays a major role in light detection and vision. It is the rhodopsin expressed in the largest class of photoreceptors in the adult retina. The stimulation by light of the product of ninaE induces G-protein signaling activation, the opening of the channels encoded by trp and trpl and photoreceptor cell membrane depolarization.

Phosrestin-2; Regulates photoreceptor cell deactivation. Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade.

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (By similarity). Essential component of the phototransduction pathway. Essential downstream component of a hh-signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required for the activation of Cad99C and consequently Cad99C-dependent endosome formation, which is essential for the Duox-dependent product [...]

Phosrestin-2; Regulates photoreceptor cell deactivation. Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade.

Transient-receptor-potential-like protein; A light-sensitive calcium channel that is required for inositide-mediated Ca(2+) entry in the retina during phospholipase C (PLC)-mediated phototransduction. Required for vision in the dark and in dim light. Binds calmodulin. Trp and trpl act together in the light response, although it is unclear whether as heteromultimers or distinct units. Also forms a functional cation channel with Trpgamma. Activated by fatty acids, metabolic stress, inositols and GTP-binding proteins.