Annotation |
Description | jgi|Araly1|486064|fgenesh2_kg.5__2056__AT3G56240.1 |
Sequence |
CGAATCTTTG CTTTTCCGTT ACTATAAATA CTTAAGAAGA CACCATTTCT TCTCATTCAA CAAACAGACA TCTCATTCCC TTATTCAGAT CATCGGTCTC AAAGCTTAGT CGTTTCCTTT CTTCTTATAT ATTATAGCCA TGGCTCAGAC CGTTGTCCTC AAAGTTGGTA TGTCATGCCA AGGCTGCGTT GGTGCCGTCA ATAGAGTCCT AGGCAAAATG GAAGGGGTTG AGTCATTTGA CATTGATATC AAGGAGCAAA AGGTGACAGT GAAAGGTAAT GTTGAGCCTG AAGCAGTTTT CCAAACAGTT TCAAAGACTG GAAAGAAGAC TTCTTACTGG CCAGTGGATG CTGAGACTGA GCCAAAAGCC GAGGCTGAGC CTAAGGCCGA GGCCGTGACT GAGACTAAAA CCGAGGCTGA GACTAAGACT GAGGCTAAGG TTGATGCAAA AGCGGATGTT GAACCAAAAG CCGCAGAAGC CGAGACTAAG CCATCACAAG TTTAAGTATA CTAAAGATGA GAAGGAAGGC TAATCTACCT TTACAATGCT TCTTTATCTT TTGCTTGTGT GTGTTGTTGT AAGCAATGCT TTCTCTAAAC ATCTAATATT TTCATGTATA CCTTTTTCAA CCTTTGATAA GAAGATGTTG GACCCATGTT GGTCCGACTT TCTTTTATAA TAAATTT |
Length | 687 |
Protein Sequence | |
Protein Residue | |
Map Location | scaffold_5: 16869773.. 16870967 |
Download Sequence |
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A.thaliana |
AGI-code | AT3G56240.1 |
Description | copper chaperone |
TAIR curator summary | CCH protein belongs to a family of eukaryotic proteins that participate in intracellular copper homeostasis by delivering this metal to the secretory pathway; mainly located along the vascular bundles of senescing leaves and petioles as well as in stem sieve elements; hypothesized to have a role in copper mobilization from decaying organs towards reproductive structures, as a result of metalloprotein breakdown. The plant-specific C-terminal domain of the CCH protein forms amyloid-like fibrils in vitro. |
Alias | [CCH][copper chaperone] |
Gene coexpression |
MR |
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RNA-seq |
Seasonal expression (July 2011 to June 2013) |
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The four seasons |
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Growth Chamber expression |
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