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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585638553  99 AQLRCYFCKTVHKEEPCTELQSCGPSQPSCEMVITQSETESRSLATYSGWCADTCQPIIRTFVGTRLTVSCCNTALCNRP 178
Cdd:cd23575    1 HSLKCYTCVSAHSNSDCLTETNCSSSDTYCKTLVASASGGSGSLTTITKWCASSCTPSTRTVEGTKVTVSCCQTDLCNVS 80

                 ...
gi 585638553 179 PWQ 181
Cdd:cd23575   81 GAQ 83

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585638553  99 AQLRCYFCKTVHKEEPCTELQSCGPSQPSCEMVITQSETESRSLATYSGWCADTCQPIIRTFVGTRLTVSCCNTALCNRP 178
Cdd:cd23575    1 HSLKCYTCVSAHSNSDCLTETNCSSSDTYCKTLVASASGGSGSLTTITKWCASSCTPSTRTVEGTKVTVSCCQTDLCNVS 80

                 ...
gi 585638553 179 PWQ 181
Cdd:cd23575   81 GAQ 83

u-PAR/Ly-6 domain; This extracellular disulphide bond rich domain is related to pfam00087.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585638553  103 CYFCKTVHkEEPCTELQSCGPSQPSCEMVITQSETESRSLATYSGWCA-DTCQPIIRTFV---GTRLTVSCCNTALCN 176
Cdd:pfam00021   1 CYSCLGVS-NEDCLSEVTCPLSDGQCVTTTLELPEGNLRGTVVSKGCArSSCPRLLSDFInggIISVSESCCQSDLCN 77

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585638553  99 AQLRCYFCKTVHKEEPCTELQSCGPSQPSCEMVITQSETESRSLATYSGWCADTCQPIIRTFVGTRLTVSCCNTALCNRP 178
Cdd:cd23575    1 HSLKCYTCVSAHSNSDCLTETNCSSSDTYCKTLVASASGGSGSLTTITKWCASSCTPSTRTVEGTKVTVSCCQTDLCNVS 80

                 ...
gi 585638553 179 PWQ 181
Cdd:cd23575   81 GAQ 83

Ly-6 antigen / uPA receptor -like domain; Three-fold repeated domain in urokinase-type plasminogen activator receptor; occurs singly in other GPI-linked cell-surface glycoproteins (Ly-6 family, CD59, thymocyte B cell antigen, Sgp-2). Topology of these domains is similar to that of snake venom neurotoxins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585638553   101 LRCYFCKTVhKEEPCTELQSCGPSQPSCEMVITQSETESRSLATYSG-WCADTCQ--PIIRTFVG-TRLTVSCCNTALCN 176
Cdd:smart00134   1 LQCYSCTGN-PDSSCSSEEECRSPDDVCLTVVAEVISDSRGSVVYKGcATSPICPgsHGYEINLTiAFLKVSCCQTDLCN 79

                   ...
gi 585638553   177 RPP 179
Cdd:smart00134  80 AAG 82

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585638553 101 LRCYFCKTVHKEEPCT---ELQSCGPSQPSCeMVITQSETESRSLATYSgwCADTCQP-----IIRTFVGTRLTVSCCNT 172
Cdd:cd00117    1 LKCYQCNSSNDPNCCNsspTLVTCSSPETFC-RKIVGKVGGGETLVIRG--CATECECgctecCSGTGTSGTTCTSCCDT 77

                 ....
gi 585638553 173 ALCN 176
Cdd:cd00117   78 DLCN 81

extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 1 (LYPD1) and similar proteins; LYPD1 (also called putative HeLa tumor suppressor (PHTS)) may act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro LYPD1 increases receptor desensitization and decreases affinity for ACh of alpha-4:beta-2-containing nAChRs. It may play a role in the intracellular trafficking of alpha-4:beta-2 and alpha-7-containing nAChRs and may inhibit their expression at the cell surface. It may be involved in the control of anxiety. LYPD1 also functions as a novel putative tumor suppressor involved in the transformation reversion of HeLaHF cells independently of the p53 pathway. LYPD1 contains an extracellular domain (ECD) that 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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585638553 100 QLRCYFCKTVHKEEPCTE---LQSCGPSQPSCEMVITQSETES--RSLATYSGWCADTcQPIIRTF----VGTRLTVSCC 170
Cdd:cd23559    1 QIQCYQCETFQLNDDCSSpefIVNCTSVQDMCQKEVMNHSAGImyRKSCAQSAACLIA-SAGYQSFctpgKVGSVCISCC 79

                 ....*.
gi 585638553 171 NTALCN 176
Cdd:cd23559   80 NTPLCN 85

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).

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585638553 101 LRCYFCKTVHKEEPCTELQSCGPSQPSCEmviTQSETESRSLATYSGWCADTCQPIIRTF-VGTRlTVSCCNTALCNR 177
Cdd:cd23573    3 LQCYTCKAQLSNSNCQTETPCRENAKACK---TDVIRAVGLLKVISKECSSSCTEDYQDYfVGKR-NITCCSTDLCNV 76

extracellular domain (ECD) found in lymphocyte antigen 6E (Ly-6E) and similar proteins; Ly-6E (also called retinoic acid-induced gene E protein (RIG-E), or stem cell antigen 2 (SCA-2), or thymic shared antigen 1 (TSA-1)) is a GPI-anchored cell surface protein that regulates T-lymphocytes proliferation, differentiation, and activation. It restricts the entry of human coronaviruses, including SARS-CoV, MERS-CoV and SARS-CoV-2, by interfering with spike protein-mediated membrane fusion. It plays an essential role in placenta formation by acting as the main receptor for syncytin-A (SynA). It may also act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. Ly-6E 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).

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585638553 101 LRCYFCKTVHKEEPCTELQSCGPSQPSCEMVITQSETESRSLATYSGWCADTCqPIIRTFVG-TRLTVSCCNTALCN 176
Cdd:cd23543    3 LYCYTCENQSSNWNCLKPTKCSDNDKYCVTTVASGGTGSSSGVRITKKCSPKC-PETNVNIGiASVSTSCCQSSLCN 78