Summary: Transducer of regulated CREB activity, N terminus
Transducer of regulated CREB activity, N terminus Provide feedback
This family includes the N terminal region of TORC proteins. TORC (Transducer of regulated CREB activity) is a protein family of coactivators that enhances the activity of CRE-depended transcription via a phosphorylation-independent interaction with the bZIP DNA binding/dimerisation domain of CREB (cAMP Response Element-Binding) . The proteins display a highly conserved predicted N-terminal coiled-coil domain and an invariant sequence matching a protein kinase A (PKA) phosphorylation consensus sequence (RKXS) . The coiled-coil structure interacts with the bZIP domain of CREB . This interaction may occur via ionic bonds because it is disrupted under high-salt conditions . In addition to CREB-binding, the N-terminal region plays a role in the tetramer formation of TORCs  but the physiological function of the multimeric complex has not been clarified yet.
Iourgenko V, Zhang W, Mickanin C, Daly I, Jiang C, Hexham JM, Orth AP, Miraglia L, Meltzer J, Garza D, Chirn GW, McWhinnie E, Cohen D, Skelton J, Terry R, Yu Y, Bodian D, Buxton FP, Zhu J, Song C, Labow MA;, Proc Natl Acad Sci U S A. 2003;100:12147-12152.: Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells. PUBMED:14506290 EPMC:14506290
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This tab holds annotation information from the InterPro database.
InterPro entry IPR024783
This entry represents the N-terminal domain of TORC proteins. TORC (transducer of regulated CREB activity) is a protein family of coactivators that enhances the activity of CRE-dependent transcription via a phosphorylation-independent interaction with the bZIP DNA binding/dimerisation domain of CREB (cAMP Response Element-Binding) [PUBMED:14536081]. The proteins display a highly conserved predicted N-terminal coiled-coil domain and an invariant sequence matching a protein kinase A (PKA) phosphorylation consensus sequence (RKXS) [PUBMED:14506290]. The coiled-coil structure interacts with the bZIP domain of CREB [PUBMED:14536081]. This interaction may occur via ionic bonds because it is disrupted under high-salt conditions [PUBMED:17565599]. In addition to CREB-binding, the N-terminal domain plays a role in the tetramer formation of TORCs [PUBMED:14536081], but the physiological function of the multimeric complex has not been clarified yet.
|Molecular function||cAMP response element binding protein binding (GO:0008140)|
|Biological process||protein homotetramerization (GO:0051289)|
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|Author:||Zenonos ZA, Mistry J|
|Number in seed:||13|
|Number in full:||158|
|Average length of the domain:||64.30 aa|
|Average identity of full alignment:||56 %|
|Average coverage of the sequence by the domain:||11.44 %|
|HMM build commands:||
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||2|
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