LMPD Database

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LMP005609

UniProt Annotations

Entry Information
Gene Namelow density lipoprotein receptor adaptor protein 1
Protein EntryARH_MOUSE
UniProt IDQ8C142
SpeciesMouse
Comments
Comment typeDescription
Disruption PhenotypeMice are extremely sensitive to cholesterol intake. LDLR are expressed at normal levels, but are sequestered at the hepatocyte surface. LDL internalization defect is caused by the inability of the LDLR to enter the endocytic cycle. {ECO:0000269|PubMed:15166224}.
DomainThe [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1. {ECO:0000250}.
FunctionAdapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface. {ECO:0000269|PubMed:12746448, ECO:0000269|PubMed:15166224}.
Sequence CautionSequence=AAH21467.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
SimilarityContains 1 PID domain. {ECO:0000255|PROSITE- ProRule:PRU00148}.
Subcellular LocationCytoplasm {ECO:0000269|PubMed:15166224}.
SubunitInteracts with LDLR. Binds to soluble clathrin trimers. Interacts with AP2B1; the interaction mediates the association with the AP-2 complex. Interacts with VLDLR. {ECO:0000269|PubMed:12746448}.