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Protein Page:
VLDLR (human)

VLDLR Binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation. Defects in VLDLR are the cause of cerebellar ataxia mental retardation and dysequilibrium syndrome type 1 (CMARQ1); also known as dysequilibrium syndrome (DES) or non- progressive cerebellar disorder with mental retardation. CMARQ1 is a congenital, non-progressive cerebellar ataxia associated with disturbed equilibrium, delayed ambulation, mental retardation and cerebellar hypoplasia. Additional features include short stature, strabismus, pes planus and, rarely, seizures. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; Receptor, misc.
Chromosomal Location of Human Ortholog: 9p24
Cellular Component: membrane; plasma membrane; receptor complex
Molecular Function: apolipoprotein binding; calcium-dependent protein binding; glycoprotein binding; low-density lipoprotein receptor activity; protein binding; very-low-density lipoprotein binding; very-low-density lipoprotein receptor activity
Biological Process: memory; negative regulation of transcription from RNA polymerase II promoter; nervous system development; receptor-mediated endocytosis; signal transduction
Disease: Cerebellar Ataxia, Mental Retardation, And Dysequilibrium Syndrome 1
Reference #:  P98155 (UniProtKB)
Alt. Names/Synonyms: CARMQ1; CHRMQ1; FLJ35024; very low density lipoprotein receptor; Very low-density lipoprotein receptor; VLDL receptor; VLDL-R; VLDLR; VLDLRCH
Gene Symbols: VLDLR
Molecular weight: 96,098 Da
Basal Isoelectric point: 4.62  Predict pI for various phosphorylation states
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Protein Structure Not Found.
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