Conserved Protein Domain Family
7tmB2_GPR111_115

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cd15994: 7tmB2_GPR111_115 
orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of seven-transmembrane G protein-coupled receptors
GPR111 and GPR115 are highly homologous orphan receptors that belong to group VI adhesion-GPCRs along with GPR110, GPR113, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B 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. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS. Both GPR111 and GPR5 are present only in land-living animals and are predominantly expressed in the developing skin.
Statistics
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PSSM-Id: 320660
View PSSM: cd15994
Aligned: 3 rows
Threshold Bit Score: 418.858
Threshold Setting Gi: 449269779
Created: 26-Jun-2014
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 134288847 375 SLILTYITYVGLGISICSLILCLSIEVLVWSqvtkteitylrHVCIVNIAATLLMADVWFIVASFLSgpithhkgCVAAT 454
gi 449269779 328 NAVLDYITRIGLGLSIFSLALCLTIEAVVWQhvtkteitymrHFCLVNIATSLLIADVLFILAAIVHntalnyplCVAAT 407
gi 296439339 398 DKVLDYITCIGLSVSILSLVLCLIIEATVWSrvvvteisymrHVCIVNIAVSLLTANVWFIIGSHFNikaqdynmCVAVT 477
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1           #                                                                            
gi 134288847 455 FFVHFFYLSVFFWMLAKALLILYGIMivfhtlpksVLVASLFSVGYGCPLAIAAITVAATepgkgylrpeiCWLnwdMTK 534
gi 449269779 408 FFLHFFYLALFFWMFTLGLLILYGLLlvffkitrpVFIATAFSIGYGCPLVISVLTVAITepkngylrsgaCWLnwyETK 487
gi 296439339 478 FFSHFFYLSLFFWMLFKALLIIYGILvifrrmmksRMMVIGFAIGYGCPLIIAVTTVAITepekgymrpeaCWLnwdNTK 557
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        ## # #                                                       #  #            #  
gi 134288847 535 ALLAFVIPALAIVVVNLITVTLVIVKTQRAAIgnsmf-qevraIVRISKNIAILTPLLGLTWGFGVATVIddrsLAFHII 613
gi 449269779 488 ALLAFIVPALSIIVVNVVVVGVVVAKTGRSSVgescksqdlsnMIRISKNVALLTPLLGLTWGFGLATIVdsrsLPFHIT 567
gi 296439339 558 ALLAFAIPAFVIVAVNLIVVLVVAVNTQRPSIgssks-qdvviIMRISKNVAILTPLLGLTWGFGIATLIegtsLTFHII 636
                        250       260
                 ....*....|....*....|....*...
Feature 1         #                          
gi 134288847 614 FSLLNAFQGFFILVFGTILDpKIREALK 641
gi 449269779 568 FALLNAFQGFFILLFGTLLDrKVLILDY 595
gi 296439339 637 FALLNAFQGFFILLFGTIMDhKIRDALR 664

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