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 194474096  68 PLQCYFCQVLHSGESCNETQSCSSSKPFCITVISHGKTDTGVLTTYSMWCTDTCQPIVKTVDSTQMTQTCCQSTLCNIPP 147
Cdd:cd23575    2 SLKCYTCVSAHSNSDCLTETNCSSSDTYCKTLVASASGGSGSLTTITKWCASSCTPSTRTVEGTKVTVSCCQTDLCNVSG 81

                 ..
gi 194474096 148 WQ 149
Cdd:cd23575   82 AQ 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 194474096  68 PLQCYFCQVLHSGESCNETQSCSSSKPFCITVISHGKTDTGVLTTYSMWCTDTCQPIVKTVDSTQMTQTCCQSTLCNIPP 147
Cdd:cd23575    2 SLKCYTCVSAHSNSDCLTETNCSSSDTYCKTLVASASGGSGSLTTITKWCASSCTPSTRTVEGTKVTVSCCQTDLCNVSG 81

                 ..
gi 194474096 148 WQ 149
Cdd:cd23575   82 AQ 83

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194474096   71 CYFCQVLHSgESCNETQSCSSSKPFCITVISHGKTDTGVLTTYSMWC-TDTCQPIVK---TVDSTQMTQTCCQSTLCN 144
Cdd:pfam00021   1 CYSCLGVSN-EDCLSEVTCPLSDGQCVTTTLELPEGNLRGTVVSKGCaRSSCPRLLSdfiNGGIISVSESCCQSDLCN 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 194474096  68 PLQCYFCQVLHSGESCNETQSCSSSKPFCITVISHGKTDTGVLTTYSMWCTDTCQPIVKTVDSTQMTQTCCQSTLCNIPP 147
Cdd:cd23575    2 SLKCYTCVSAHSNSDCLTETNCSSSDTYCKTLVASASGGSGSLTTITKWCASSCTPSTRTVEGTKVTVSCCQTDLCNVSG 81

                 ..
gi 194474096 148 WQ 149
Cdd:cd23575   82 AQ 83

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 194474096  68 PLQCYFCQVLHSGESCNETQSCSSSKPFCITVISHGKTDTGVLTTYSMWCTDTCQPIVKTVDSTQMTQTCCQSTLCN 144
Cdd:cd23543    2 SLYCYTCENQSSNWNCLKPTKCSDNDKYCVTTVASGGTGSSSGVRITKKCSPKCPETNVNIGIASVSTSCCQSSLCN 78

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 194474096  69 LQCYFCQVLHSGESCN---ETQSCSSSKPFCITVISHGKTDTGVLT---TYSMWCTDTCQPIVKTVDSTQMTqTCCQSTL 142
Cdd:cd00117    1 LKCYQCNSSNDPNCCNsspTLVTCSSPETFCRKIVGKVGGGETLVIrgcATECECGCTECCSGTGTSGTTCT-SCCDTDL 79

                 ..
gi 194474096 143 CN 144
Cdd:cd00117   80 CN 81

extracellular domain (ECD) found in CD59 glycoprotein and similar proteins; CD59 (also called 1F5 antigen, or 20 kDa homologous restriction factor, or HRF-20, or MAC-inhibitory protein (MAC-IP), or MEM43 antigen, or membrane attack complex inhibition factor (MACIF), or membrane inhibitor of reactive lysis (MIRL), or protectin) is an LY-6-like protein expressed in human lymphoid cells and inhibits the action of the complement membrane attack complex (MAC) on homologous cells. It acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. CD59 is also involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase. CD59 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 194474096  69 LQCYFCqVLHSGeSCNETQSCSSSKPFCITVIShgktdtGVLTTYSMWCTDTC--QPIVKTVDSTQMTQTCCQSTLCN 144
Cdd:cd23554    1 LKCYNC-PNPTS-NCNTNVTCSSNLDACLIVKA------GNRIYRQCWKYSDCnfDFISERFGESNFKYRCCQKDLCN 70

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194474096   71 CYFCQVLHSgESCNETQSCSSSKPFCITVISHGKTDTGVLTTYSMWC-TDTCQPIVK---TVDSTQMTQTCCQSTLCN 144
Cdd:pfam00021   1 CYSCLGVSN-EDCLSEVTCPLSDGQCVTTTLELPEGNLRGTVVSKGCaRSSCPRLLSdfiNGGIISVSESCCQSDLCN 77

extracellular domain (ECD) found in mouse Ly-6A like lymphocyte antigens and similar proteins; The family includes mouse Ly-6 lymphocyte antigens, such as Ly-6A/Ly-6E, Ly-6B, Ly-6C1/6C2, Ly-6F, and Ly-6I/Ly-6M. Ly-6A/Ly-6E (also called stem cell antigen 1/SCA-1, or T-cell-activating protein/TAP) and Ly-6C are involved in T-cell activation. Members in this family contain 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 194474096  69 LQCYFCQVLHSGESCNETqSCSSSKPFCITVISHGKTDTGVLTTYSMWCTDTCQP---IVKTVDSTQ--MTQTCCQSTLC 143
Cdd:cd23541    3 LRCYQCLGVPLETSCPSV-TCSYPDGVCVSQEVETIVGSQRVKLKNKFCLPFCPKnlyFLEEILGTTvnVKTSCCKEDLC 81

                 .
gi 194474096 144 N 144
Cdd:cd23541   82 N 82