short coiled-coil protein isoform 2 [Rattus norvegicus]
Protein Classification
short coiled-coil protein( domain architecture ID 10562948)
short coiled-coil protein is a positive regulator of amino acid starvation-induced autophagy
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| DUF2205 | pfam10224 | Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil ... |
13-73 | 3.03e-22 | ||
Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil region which is found in short coiled-coil protein (SCOC) in human and UNC-69 in Caenorhabditis elegans. In human, SCOC is required for autophagosome formation during amino acid starvation. It forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. In C. elegans, this small, evolutionarily conserved coiled-coil domain-containing protein, UNC-69, acts as a binding partner of UNC-76. Together they participate in a common genetic pathway necessary for axon extension and cooperate to regulate the size and position of synaptic vesicles in axons. Moreover, both proteins colocalize as puncta in neuronal processes and mutations in UNC-69 preferentially disrupt membrane traffic within axons. : Pssm-ID: 431150 Cd Length: 71 Bit Score: 81.21 E-value: 3.03e-22
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| Name | Accession | Description | Interval | E-value | ||
| DUF2205 | pfam10224 | Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil ... |
13-73 | 3.03e-22 | ||
Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil region which is found in short coiled-coil protein (SCOC) in human and UNC-69 in Caenorhabditis elegans. In human, SCOC is required for autophagosome formation during amino acid starvation. It forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. In C. elegans, this small, evolutionarily conserved coiled-coil domain-containing protein, UNC-69, acts as a binding partner of UNC-76. Together they participate in a common genetic pathway necessary for axon extension and cooperate to regulate the size and position of synaptic vesicles in axons. Moreover, both proteins colocalize as puncta in neuronal processes and mutations in UNC-69 preferentially disrupt membrane traffic within axons. Pssm-ID: 431150 Cd Length: 71 Bit Score: 81.21 E-value: 3.03e-22
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| Name | Accession | Description | Interval | E-value | ||
| DUF2205 | pfam10224 | Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil ... |
13-73 | 3.03e-22 | ||
Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil region which is found in short coiled-coil protein (SCOC) in human and UNC-69 in Caenorhabditis elegans. In human, SCOC is required for autophagosome formation during amino acid starvation. It forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. In C. elegans, this small, evolutionarily conserved coiled-coil domain-containing protein, UNC-69, acts as a binding partner of UNC-76. Together they participate in a common genetic pathway necessary for axon extension and cooperate to regulate the size and position of synaptic vesicles in axons. Moreover, both proteins colocalize as puncta in neuronal processes and mutations in UNC-69 preferentially disrupt membrane traffic within axons. Pssm-ID: 431150 Cd Length: 71 Bit Score: 81.21 E-value: 3.03e-22
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