Conserved Protein Domain Family
7tmB2_Latrophilin_Adhesion_I

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cd15252: 7tmB2_Latrophilin_Adhesion_I 
Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors
Group I adhesion GPCRs consist of latrophilins (also called lectomedins or latrotoxin receptors) and ETL (EGF-TM7-latrophilin-related protein. These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.
Statistics
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PSSM-Id: 320380
View PSSM: cd15252
Aligned: 3 rows
Threshold Bit Score: 413.826
Threshold Setting Gi: 212276505
Created: 11-Nov-2013
Updated: 26-Jul-2017
Structure
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Aligned Rows:
  next features
Feature 1:putative polypeptide ligand binding pocket [polypeptide binding site]
Evidence:
  • Comment:based on mutagenesis of human glucagon receptor (GCGR), and modeling studies of GCGR and other related class B GPCRs
  • Comment:Residues in the globular N-terminal extracellular domain and the extracellular loops of the 7TM domain may also be involved in ligand binding.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                #   #                                         #  ##  #      #      #     
gi 47116772   861 DLLLDVITWVGILLSLVCLLICIFTFCFFRGLqsDRNTIHKNLCISLFVAELLFLIGINRTdqpiaCAVFAALLHFFFLA 940
gi 270016377  551 QIALKIITLVGCIISIVCLILAIITFQLFRGLksDRTTIHCNLCICLLIAELIFLIGVDQTenkivCGVIAGFLQYFFLC 630
gi 212276505  424 YNILTRITQLGIIISLICLAICIFTFWFFSEIqsTRTTIHKNLCCSLFLAELVFLVGINTNtnklfCSIIAGLLHYFFLA 503
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                           ## # #        
gi 47116772   941 AFTWMFLEGVQLYIMLVevfesehSRRKYFYLVGYGMPALIVAVSAAVDyrsygtdkvCWLrlDTYFIWSFIGPATLIIM 1020
gi 270016377  631 AFIWMFFEGFQLYVMLIevfeaekSRVKWYYFFAYGLPLVIVLVSAAIYpqgygteqhCWLktNNYFIYSFVGPVTLVLV 710
gi 212276505  504 AFAWMCIEGIHLYLIVVgviynkgFLHKNFYIFGYLSPAVVVGFSAALGyryygttkvCWLstENNFIWSFIGPACLIIL 583
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                            #  #           #   #         
gi 47116772  1021 LNVIFLGIALYKMFHHTAilkpe----sgcldNIKSWVIGAIALLCLLGLTWAFGLMYINestVIMAYLFTIFNSLQGMF 1096
gi 270016377  711 LNLIFLAMAVVMMCRHASasvsiknkehsrlaSTRAWLKGAIVLVFLLGLTWTFGFLFINqesVVMAYLFALLNSLQGFF 790
gi 212276505  584 VNLLAFGVIIYKVFRHTAglkpe----vscfeNIRSCARGALALLFLLGTTWIFGVLHVVhasVVTAYLFTVSNAFQGMF 659
                         250       260
                  ....*....|....*....|.
Feature 1                              
gi 47116772  1097 IFIFHCVLQKKVRKEYGKCLR 1117
gi 270016377  791 IFSFHCVQNEKVRKEYRKFIR 811
gi 212276505  660 IFLFLCVLSRKIQEEYYRLFK 680

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