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FLASH GENE
Symbol GPIHBP1 contributors: mct/npt - updated : 31-01-2016
HGNC name glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1
HGNC id 24945
Location 8q24.3      Physical location : 144.295.067 - 144.299.043
Synonym name
  • GPI anchored high density lipoprotein binding protein 1
  • high density lipoprotein-binding protein
    • Synonym symbol(s) GPI-HBP1, LOC338328, HBP1, HYPL1D
    DNA
    TYPE functioning gene
    STRUCTURE 3.97 kb     4 Exon(s)
    motif repetitive sequence
    MAPPING cloned Y linked N status provisional
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    4 - 2296 19.7 184 - Gin (2007)
    - - 625 - 125 - -
    EXPRESSION
    Type restricted
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularheart   highly Homo sapiens
    Endocrinepancreas   highly Mus musculus
    cells
    SystemCellPubmedSpeciesStageRna symbol
    Cardiovascularendothelial cell Homo sapiens
    Endocrineislet cell (alpha,beta...) Mus musculus
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • a N-terminal acidic domain in which most of the AAs are aspartate or glutamate (21 of 26 amino acids in the human protein, required but not sufficient for LPL binding
  • two main structural motifs, an N-terminal acidic domain enriched in aspartates and glutamates and a lymphocyte antigen 6 (Ly6) motif containing 10 cysteines, important for the ability of GPIHBP1 to bind and transport LPL
  • a three-fingered Ly6/uPAR (LU) domain
  • LU domain is followed by a C-terminal GPI membrane anchor attachment sequence
    • HOMOLOGY
    Homologene
    FAMILY
  • large family of "lymphocyte antigen 6" (Ly6) proteins
    • CATEGORY regulatory
    SUBCELLULAR LOCALIZATION     plasma membrane
    text exclusively in the lumen of the microvascular endothelial cells of heart, adipose tissue, and muscle, precisely where the lipolytic processing of chylomicrons occurs
    basic FUNCTION
  • endothelial cell protein that serves as a platform for lipoprotein lipase-mediated processing of triglyceride-rich lipoproteins within the capillaries of heart, adipose tissue, and skeletal muscle
  • plays a key role in the lipolysis of triglyceride-rich lipoproteins (chylomicrons)
  • endothelial cell protein that transports lipoprotein lipase (LPL) from the subendothelial spaces to the capillary lumen
  • glycosylphosphatidylinositol-anchored protein of capillary endothelial cells, that shuttles lipoprotein lipase (LPL) from subendothelial spaces to the capillary lumen
  • collects LPL from the interstitial space and transfers it across ECs onto the luminal binding sites of these cells, where the enzyme is functional
    • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • LPL bound avidly to GPIHBP1
  • binding of LPL to GPIHBP1 requires only the C-terminal portion of LPL and does not depend on full-length LPL homodimers
  • is transported and attached to the capillary endothelium by the protein GPIHBP1
  • GPIHBP1-bound LPL is the main determinant of Triglyceride-rich lipoproteins (TRLs) margination
  • ANGPTL4 was capable of binding and inactivating LPL complexed to GPIHBP1 on the surface of endothelial cells
  • GPIHBP1's LU domain binds to LPL's C-terminal domain, largely by hydrophobic interactions
  • GPIHBP1 is LPL's essential partner: it binds LPL and transports it to the capillary lumen; it is essential for lipoprotein margination along capillaries, allowing lipolysis to proceed
    • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional        
    absence of GPIHBP1 abolishes the entry of LPL (lipoprotein lipase) into capillaries, causing severe chylomicronemia and an accumulation of catalytically active LPL in the interstitial spaces
    Susceptibility to hyperlipidemia with chylomicronemia
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS