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Conserved domains on  [gi|568914340|ref|XP_006498415|]
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ly6/PLAUR domain-containing protein 6B isoform X1 [Mus musculus]

Protein Classification

TFP_LU_ECD_LYPD6B domain-containing protein( domain architecture ID 11246579)

TFP_LU_ECD_LYPD6B domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UPAR_LY6_2 pfam16975
Ly6/PLAUR domain-containing protein 6, Lypd6; UPAR_LY6_2 is a family of higher eukaryotic ...
58-163 6.20e-57

Ly6/PLAUR domain-containing protein 6, Lypd6; UPAR_LY6_2 is a family of higher eukaryotic proteins expressed in neurons. It modulates nicotinic acetylcholine receptors by selectively increasing Ca2+-influx through this ion channel. The family carries an LU protein domain - about 80 amino acids long characterized by a conserved pattern of 10 cysteine residues. The family is a positive feedback regulator of Wnt/beta-catenin signalling, eg for patterning of the mesoderm and neuroectoderm in zebrafish gastrulation, where Lypd6 is GPI-anchored to the plasma-membrane and interacts with the Wnt receptor Frizzled8 and the co-receptor Lrp6.


:

Pssm-ID: 435685  Cd Length: 106  Bit Score: 174.84  E-value: 6.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340   58 PTPFPNSFKCFTCENAGDNYNCNRWAEDKWCPQDTQYCLTVHHFTSHGRSTSITKKCASKNECHFVGCRHSRDSEHTECR 137
Cdd:pfam16975   1 TTPYPSGFKCFTCEAADDNYCCNRWAPDWCCPRTTYYCTTHHFMSHGGSSVSVTKRCATEEECLVGGCHHRDDGGHEVCS 80
                          90       100
                  ....*....|....*....|....*.
gi 568914340  138 SCCEGMICNVELPTNHTNAVFAVMHA 163
Cdd:pfam16975  81 SCCEGNICNVVLPNNTTAAVFATTSP 106
 
Name Accession Description Interval E-value
UPAR_LY6_2 pfam16975
Ly6/PLAUR domain-containing protein 6, Lypd6; UPAR_LY6_2 is a family of higher eukaryotic ...
58-163 6.20e-57

Ly6/PLAUR domain-containing protein 6, Lypd6; UPAR_LY6_2 is a family of higher eukaryotic proteins expressed in neurons. It modulates nicotinic acetylcholine receptors by selectively increasing Ca2+-influx through this ion channel. The family carries an LU protein domain - about 80 amino acids long characterized by a conserved pattern of 10 cysteine residues. The family is a positive feedback regulator of Wnt/beta-catenin signalling, eg for patterning of the mesoderm and neuroectoderm in zebrafish gastrulation, where Lypd6 is GPI-anchored to the plasma-membrane and interacts with the Wnt receptor Frizzled8 and the co-receptor Lrp6.


Pssm-ID: 435685  Cd Length: 106  Bit Score: 174.84  E-value: 6.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340   58 PTPFPNSFKCFTCENAGDNYNCNRWAEDKWCPQDTQYCLTVHHFTSHGRSTSITKKCASKNECHFVGCRHSRDSEHTECR 137
Cdd:pfam16975   1 TTPYPSGFKCFTCEAADDNYCCNRWAPDWCCPRTTYYCTTHHFMSHGGSSVSVTKRCATEEECLVGGCHHRDDGGHEVCS 80
                          90       100
                  ....*....|....*....|....*.
gi 568914340  138 SCCEGMICNVELPTNHTNAVFAVMHA 163
Cdd:pfam16975  81 SCCEGNICNVVLPNNTTAAVFATTSP 106
TFP_LU_ECD_LYPD6B cd23626
extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 6B (LYPD6B) and ...
65-152 7.73e-55

extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 6B (LYPD6B) and similar proteins; LYPD6B (also called LYPD7) may act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro it acts on nAChRs in a subtype- and stoichiometry-dependent manner. LYPD6B modulates specifically alpha-3(3):beta-4(2) nAChRs by enhancing the sensitivity to ACh, decreasing ACh-induced maximal current response and increasing the rate of desensitization to ACh; has no effect on alpha-7 homomeric nAChRs; modulates alpha-3(2):alpha-5:beta-4(2) nAChRs in the context of CHRNA5/alpha-5 variant Asn-398, but not its wild-type sequence. LYPD6B also activates AP1 (PMA)-mediated transcriptional activation. LYPD6B 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).


Pssm-ID: 467146  Cd Length: 88  Bit Score: 168.90  E-value: 7.73e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340  65 FKCFTCENAGDNYNCNRWAEDKWCPQDTQYCLTVHHFTSHGRSTSITKKCASKNECHFVGCRHSRDSEHTECRSCCEGMI 144
Cdd:cd23626    1 FKCFTCENAPDNYNCNRWAEDKWCPQNTQYCLTIHHFTSHGKSKSVTKKCASREECHFVGCHHHRDSGHTECVSCCEGMI 80

                 ....*...
gi 568914340 145 CNVELPTN 152
Cdd:cd23626   81 CNVEVPTN 88
LU smart00134
Ly-6 antigen / uPA receptor -like domain; Three-fold repeated domain in urokinase-type ...
67-151 6.59e-05

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.


Pssm-ID: 214530  Cd Length: 85  Bit Score: 39.83  E-value: 6.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340    67 CFTCENAGDNyNCNRWAEdkwCPQDTQYCLTVH-HFTSHGRSTSITKKCASKNECHFVGCRHSRDSEHTECRSCCEGMIC 145
Cdd:smart00134   3 CYSCTGNPDS-SCSSEEE---CRSPDDVCLTVVaEVISDSRGSVVYKGCATSPICPGSHGYEINLTIAFLKVSCCQTDLC 78

                   ....*.
gi 568914340   146 NVELPT 151
Cdd:smart00134  79 NAAGPG 84
 
Name Accession Description Interval E-value
UPAR_LY6_2 pfam16975
Ly6/PLAUR domain-containing protein 6, Lypd6; UPAR_LY6_2 is a family of higher eukaryotic ...
58-163 6.20e-57

Ly6/PLAUR domain-containing protein 6, Lypd6; UPAR_LY6_2 is a family of higher eukaryotic proteins expressed in neurons. It modulates nicotinic acetylcholine receptors by selectively increasing Ca2+-influx through this ion channel. The family carries an LU protein domain - about 80 amino acids long characterized by a conserved pattern of 10 cysteine residues. The family is a positive feedback regulator of Wnt/beta-catenin signalling, eg for patterning of the mesoderm and neuroectoderm in zebrafish gastrulation, where Lypd6 is GPI-anchored to the plasma-membrane and interacts with the Wnt receptor Frizzled8 and the co-receptor Lrp6.


Pssm-ID: 435685  Cd Length: 106  Bit Score: 174.84  E-value: 6.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340   58 PTPFPNSFKCFTCENAGDNYNCNRWAEDKWCPQDTQYCLTVHHFTSHGRSTSITKKCASKNECHFVGCRHSRDSEHTECR 137
Cdd:pfam16975   1 TTPYPSGFKCFTCEAADDNYCCNRWAPDWCCPRTTYYCTTHHFMSHGGSSVSVTKRCATEEECLVGGCHHRDDGGHEVCS 80
                          90       100
                  ....*....|....*....|....*.
gi 568914340  138 SCCEGMICNVELPTNHTNAVFAVMHA 163
Cdd:pfam16975  81 SCCEGNICNVVLPNNTTAAVFATTSP 106
TFP_LU_ECD_LYPD6B cd23626
extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 6B (LYPD6B) and ...
65-152 7.73e-55

extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 6B (LYPD6B) and similar proteins; LYPD6B (also called LYPD7) may act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro it acts on nAChRs in a subtype- and stoichiometry-dependent manner. LYPD6B modulates specifically alpha-3(3):beta-4(2) nAChRs by enhancing the sensitivity to ACh, decreasing ACh-induced maximal current response and increasing the rate of desensitization to ACh; has no effect on alpha-7 homomeric nAChRs; modulates alpha-3(2):alpha-5:beta-4(2) nAChRs in the context of CHRNA5/alpha-5 variant Asn-398, but not its wild-type sequence. LYPD6B also activates AP1 (PMA)-mediated transcriptional activation. LYPD6B 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).


Pssm-ID: 467146  Cd Length: 88  Bit Score: 168.90  E-value: 7.73e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340  65 FKCFTCENAGDNYNCNRWAEDKWCPQDTQYCLTVHHFTSHGRSTSITKKCASKNECHFVGCRHSRDSEHTECRSCCEGMI 144
Cdd:cd23626    1 FKCFTCENAPDNYNCNRWAEDKWCPQNTQYCLTIHHFTSHGKSKSVTKKCASREECHFVGCHHHRDSGHTECVSCCEGMI 80

                 ....*...
gi 568914340 145 CNVELPTN 152
Cdd:cd23626   81 CNVEVPTN 88
TFP_LU_ECD_LYPD6_like cd23567
extracellular domain (ECD) found in the Ly6/PLAUR domain-containing protein 6 (LYPD6)-like ...
65-150 1.83e-39

extracellular domain (ECD) found in the Ly6/PLAUR domain-containing protein 6 (LYPD6)-like family; The LYPD6-like family includes LYPD6 and LYPD6B. LYPD6 acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain. It inhibits nicotine-induced Ca(2+) influx through nAChRs. It functions as a positive regulator of Wnt/beta-catenin signaling. LYPD6B (also called LYPD7) may act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro it acts on nAChRs in a subtype- and stoichiometry-dependent manner. LYPD6B modulates specifically alpha-3(3):beta-4(2) nAChRs by enhancing the sensitivity to ACh, decreasing ACh-induced maximal current response and increasing the rate of desensitization to ACh; has no effect on alpha-7 homomeric nAChRs; modulates alpha-3(2):alpha-5:beta-4(2) nAChRs in the context of CHRNA5/alpha-5 variant Asn-398, but not its wild-type sequence. LYPD6B also activates AP1 (PMA)-mediated transcriptional activation. Members in this family contain 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).


Pssm-ID: 467097  Cd Length: 88  Bit Score: 129.78  E-value: 1.83e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340  65 FKCFTCENAGDNYNCNRWAEDKWCPQDTQYCLTVHHFTSHGRSTSITKKCASKNECH--FVGCRHSRDSEHTECRSCCEG 142
Cdd:cd23567    1 ITCFTCENKTDNYECNRWAIDRPCPQGTSYCYTVHVMDSRGRSVSVTKKCATPSECTpnTVGCRDSTDTGHTVCISCCDG 80

                 ....*...
gi 568914340 143 MICNVELP 150
Cdd:cd23567   81 SYCNVEVP 88
TFP_LU_ECD_LYPD6 cd23625
extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 6 (LYPD6) and similar ...
65-152 5.45e-33

extracellular domain (ECD) found in Ly6/PLAUR domain-containing protein 6 (LYPD6) and similar proteins; LYPD6 acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain. It inhibits nicotine-induced Ca(2+) influx through nAChRs. It functions as a positive regulator of Wnt/beta-catenin signaling. LYPD6 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).


Pssm-ID: 467145  Cd Length: 89  Bit Score: 113.34  E-value: 5.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340  65 FKCFTCENAGDNYNCNRWAEDKWCPQDTQYCLTVHHFTSHGRSTSITKKCASKNECHFVGCRHSRDSEHTECRSCCEGMI 144
Cdd:cd23625    2 FKCFTCEKAADNYECNRWAPDIYCPRETRYCYTQHTMEVTGNSISVTKRCVPLEKCLSTGCRDSEHEGHKVCTSCCEGNI 81

                 ....*...
gi 568914340 145 CNVELPTN 152
Cdd:cd23625   82 CNLPLPRN 89
TFP cd00117
three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU ...
66-146 4.69e-07

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.


Pssm-ID: 467060  Cd Length: 81  Bit Score: 45.94  E-value: 4.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340  66 KCFTCENAGDNYNCNRWAEDKWCPQDTQYCLTVHHFTSHGrSTSITKKCASKNECHFVGCRHSRDSEHTECRSCCEGMIC 145
Cdd:cd00117    2 KCYQCNSSNDPNCCNSSPTLVTCSSPETFCRKIVGKVGGG-ETLVIRGCATECECGCTECCSGTGTSGTTCTSCCDTDLC 80

                 .
gi 568914340 146 N 146
Cdd:cd00117   81 N 81
LU smart00134
Ly-6 antigen / uPA receptor -like domain; Three-fold repeated domain in urokinase-type ...
67-151 6.59e-05

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.


Pssm-ID: 214530  Cd Length: 85  Bit Score: 39.83  E-value: 6.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340    67 CFTCENAGDNyNCNRWAEdkwCPQDTQYCLTVH-HFTSHGRSTSITKKCASKNECHFVGCRHSRDSEHTECRSCCEGMIC 145
Cdd:smart00134   3 CYSCTGNPDS-SCSSEEE---CRSPDDVCLTVVaEVISDSRGSVVYKGCATSPICPGSHGYEINLTIAFLKVSCCQTDLC 78

                   ....*.
gi 568914340   146 NVELPT 151
Cdd:smart00134  79 NAAGPG 84
TFP_LU_ECD_GPIHBP1 cd23575
extracellular domain (ECD) found in glycosylphosphatidylinositol-anchored high density ...
64-147 7.25e-04

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: 36.93  E-value: 7.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340  64 SFKCFTCENAGDNYNCNRWAEdkwCPQDTQYCLTV--HHFTSHGRSTSITKKCASknECHFVgcrhSRDSEHTECR-SCC 140
Cdd:cd23575    2 SLKCYTCVSAHSNSDCLTETN---CSSSDTYCKTLvaSASGGSGSLTTITKWCAS--SCTPS----TRTVEGTKVTvSCC 72

                 ....*..
gi 568914340 141 EGMICNV 147
Cdd:cd23575   73 QTDLCNV 79
TFP_LU_ECD_CinHb4_like cd23539
extracellular domain (ECD) found in Ciona intestinalis globin CinHb4 and similar proteins; ...
65-146 9.86e-04

extracellular domain (ECD) found in Ciona intestinalis globin CinHb4 and similar proteins; Four distinct globin genes have been identified in the Ciona genome. CinHb4 is encoded by the fourth globin gene. It shows an unusual extension at its N-terminus, which reveals a conserved region with similarity to the extracellular domain (ECD) of the TGF-beta receptor type I/II protein family involved in signal transduction. The functional relevance of these matches is currently unknown. The ECD 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: 467069  Cd Length: 91  Bit Score: 37.01  E-value: 9.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914340  65 FKCFTCENAGDNYNCNRWAEDKWCPQDTQYCLTVHHFTSHGRsTSITKKCASKNECH------FVGCRHSR----DSEHT 134
Cdd:cd23539    1 LSCWTCDNASSNEECLANGTLVTCQSNEESCQTEVRRRGGGV-YLISKGCKQRQACEnnkkqnFKAAWNPTqcnpESPNS 79
                         90
                 ....*....|..
gi 568914340 135 ECRSCCEGMICN 146
Cdd:cd23539   80 VCRCCCSTDLCN 91
 
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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