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Field | Value |
---|---|
Namespace | Molecular function |
Short description | Clathrin adaptor activity |
Full defintion | The binding activity of a molecule that brings together clathrin and one or more other molecules, permitting them to function in a coordinated way. |
Subterm of |
The relationship of GO:0035615 with other GO terms.
Relationship type | GO terms |
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Is a | |
Regulates | n.a. |
Part of | n.a. |
Positively regulates | n.a. |
Negatively regulates | n.a. |
A force layout showing the ancestor tree for GO:0035615, and its immediate children. If you wish to explore the tree dynamically, please use the GO Explorer.
This table contains additional metadata associated with the GO entry's definition field.
Field | Value |
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GOC | BHF |
PMID | Functional dissection of an AP-2 beta2 appendage-binding sequence within the autosomal recessive hypercholesterolemia protein. J Biol Chem. 2005 May 13; 280 (19): 19270–80.PMID: 15728179 The autosomal recessive hypercholesterolemia (ARH) protein plays a critical role in regulating plasma low density lipoprotein (LDL) levels. Inherited defects in ARH lead to a hypercholesterolemia that closely phenocopies that caused by a defective LDL receptor. The elevated serum LDL-cholesterol levels typical of ARH patients and the pronounced accumulation of the LDL receptor at the cell surface of hepatocytes in ARH-null mice argue that ARH operates by promoting the internalization of the LDL receptor within clathrin-coated vesicles. ARH contains an amino-terminal phosphotyrosine-binding domain that associates physically with the LDL receptor internalization sequence and with phosphoinositides. The carboxyl-terminal half of ARH contains a clathrin-binding sequence and a separate AP-2 adaptor binding region providing a plausible mechanism for how ARH can act as an endocytic adaptor or CLASP (clathrin-associated sorting protein) to couple LDL receptors with the clathrin machinery. Because the interaction with AP-2 is highly selective for the independently folded appendage domain of the beta2 subunit, we have characterized the ARH beta2 appendage-binding sequence in detail. Unlike the known alpha appendage-binding motifs, ARH requires an extensive sequence tract to bind the beta appendage with comparably high affinity. A minimal 16-residue sequence functions autonomously and depends upon ARH residues Asp253, Phe259, Leu262, and Arg266. We suggested that biased beta subunit engagement by ARH and the only other beta2 appendage selective adaptor, beta-arrestin, promotes efficient incorporation of this mechanistically distinct subset of CLASPs into clathrin-coated buds. |
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
Transcript | Name | Description | GO terms | GO count |
---|---|---|---|---|
– | AP-2 complex subunit alpha; TAIR: AT5G22770.1 alpha-adaptin; Swiss-Prot: sp|Q8LPL6|AP2A1_ARATH AP-2 complex subunit alpha-1; TrEMBL-Plants: tr|A0A151RV94|A0A151RV94_CAJCA AP-2 complex subunit alpha; Found in the gene: LotjaGi3g1v0172200 | 4 | ||
– | AP-2 complex subunit alpha; TAIR: AT5G22770.1 alpha-adaptin; Swiss-Prot: sp|Q8LPL6|AP2A1_ARATH AP-2 complex subunit alpha-1; TrEMBL-Plants: tr|A0A151RV94|A0A151RV94_CAJCA AP-2 complex subunit alpha; Found in the gene: LotjaGi3g1v0172200 | 4 | ||
– | AP-2 complex subunit alpha; TAIR: AT5G22770.1 alpha-adaptin; Swiss-Prot: sp|Q8LPL6|AP2A1_ARATH AP-2 complex subunit alpha-1; TrEMBL-Plants: tr|A0A151RV94|A0A151RV94_CAJCA AP-2 complex subunit alpha; Found in the gene: LotjaGi3g1v0172200 | 4 |
A list of co-occurring GO terms within the L. japonicus gene space:
GO term | Namespace | Name | Observations | Saturation (%) |
---|---|---|---|---|
Biological process | Clathrin-dependent endocytosis | 1 | 33.33 |