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Conserved domains on  [gi|684179339|ref|NP_001288701|]
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glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 isoform 2 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TFP super family cl45932
three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU ...
 63-125 1.32e-19

three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU (also known as Ly-6 antigen/uPA receptor)-like extracellular domain (ECD) occurs singly in GPI-linked cell-surface glycoproteins (Ly-6 family, CD59, thymocyte B cell antigen, Sgp-2) or as three-fold repeated domain in urokinase-type plasminogen activator receptor. It is a structural domain involved in protein-protein interactions, tolerating an unusual degree of variation and binding with high specificity to a broad spectrum of targets. The snake toxin domain is present in short and long neurotoxins, cytotoxins, and short toxins, and in other miscellaneous venom peptides. The toxin acts by binding to the nicotinic acetylcholine receptors in the postsynaptic membrane of skeletal muscles and preventing the binding of acetylcholine, thereby blocking the excitation of muscles. Both the LU-like ECD and the snake toxin domain belong to three-fingered protein (TFP) fold, which is characterized by containing 70 to 100 amino acids including eight to ten cysteine residues spaced at conserved distances.


The actual alignment was detected with superfamily member cd23575:

Pssm-ID: 480272  Cd Length: 83  Bit Score: 76.60  E-value: 1.32e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 684179339  63 LRCYTCKSLPRDERCNLTQNCSHGQT-CTTLIAHGNTESGLLTTHSTWCTDSCQPITKTVEGTQ 125
Cdd:cd23575    3 LKCYTCVSAHSNSDCLTETNCSSSDTyCKTLVASASGGSGSLTTITKWCASSCTPSTRTVEGTK 66
 
Name Accession Description Interval E-value
TFP_LU_ECD_GPIHBP1 cd23575
extracellular domain (ECD) found in glycosylphosphatidylinositol-anchored high density ...
 63-125 1.32e-19

extracellular domain (ECD) found in glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPI-HBP1) and similar proteins; GPI-HBP1 (also called GPI-anchored HDL-binding protein 1, or high density lipoprotein-binding protein 1) is an endothelial cell transporter for lipoprotein lipase. It mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries and anchors LPL on the surface of endothelial cells in the lumen of blood capillaries. GPI-HBP1 protects LPL against loss of activity, and against ANGPTL4-mediated unfolding. Thereby, it plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis. GPI-HBP1 binds chylomicrons and phospholipid particles that contain APOA5. It also binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL. GPI-HBP1 contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467105  Cd Length: 83  Bit Score: 76.60  E-value: 1.32e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 684179339  63 LRCYTCKSLPRDERCNLTQNCSHGQT-CTTLIAHGNTESGLLTTHSTWCTDSCQPITKTVEGTQ 125
Cdd:cd23575    3 LKCYTCVSAHSNSDCLTETNCSSSDTyCKTLVASASGGSGSLTTITKWCASSCTPSTRTVEGTK 66
 
Name Accession Description Interval E-value
TFP_LU_ECD_GPIHBP1 cd23575
extracellular domain (ECD) found in glycosylphosphatidylinositol-anchored high density ...
 63-125 1.32e-19

extracellular domain (ECD) found in glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPI-HBP1) and similar proteins; GPI-HBP1 (also called GPI-anchored HDL-binding protein 1, or high density lipoprotein-binding protein 1) is an endothelial cell transporter for lipoprotein lipase. It mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries and anchors LPL on the surface of endothelial cells in the lumen of blood capillaries. GPI-HBP1 protects LPL against loss of activity, and against ANGPTL4-mediated unfolding. Thereby, it plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis. GPI-HBP1 binds chylomicrons and phospholipid particles that contain APOA5. It also binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL. GPI-HBP1 contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467105  Cd Length: 83  Bit Score: 76.60  E-value: 1.32e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 684179339  63 LRCYTCKSLPRDERCNLTQNCSHGQT-CTTLIAHGNTESGLLTTHSTWCTDSCQPITKTVEGTQ 125
Cdd:cd23575    3 LKCYTCVSAHSNSDCLTETNCSSSDTyCKTLVASASGGSGSLTTITKWCASSCTPSTRTVEGTK 66
TFP_LU_ECD_PSCA cd23573
extracellular domain (ECD) found in prostate stem cell antigen (PSCA) and similar proteins; ...
 63-119 7.75e-03

extracellular domain (ECD) found in prostate stem cell antigen (PSCA) and similar proteins; PSCA may be involved in the regulation of cell proliferation. It has a cell-proliferation inhibition activity in vitro. PSCA may also act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro it inhibits nicotine-induced signaling probably implicating alpha-3:beta-2- or alpha-7-containing nAChRs. PSCA contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467103  Cd Length: 78  Bit Score: 33.19  E-value: 7.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 684179339  63 LRCYTCKSLPRDERCNLTQNCSH-GQTCTTLIAhgnTESGLLTTHSTWCTDSCQPITK 119
Cdd:cd23573    3 LQCYTCKAQLSNSNCQTETPCREnAKACKTDVI---RAVGLLKVISKECSSSCTEDYQ 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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