Fibronectin type III domain; This domain is found in Interleukin-7 receptor subunit alpha (IL-7Ralpha), which together IL-7 form a complex crucial to several signalling cascades leading to the development and homeostasis of T and B cells. IL-7Ralpha carries a 219 residue ectodomain on the N-terminal region which is crucial for T and B-cell development. Mutations in the IL-7Ralpha ectodomain inhibits T and B cell development, resulting in patients with a form of severe combined immunodeficiency (SCID). The ectodomain folds into two fibronectin type III (FNIII) domains connected by a 310-helical linker. This entry comprises the first of the two FNIII domains, D1 while D2 domain is pfam00041. In the D1 domain of IL-7Ralpha, a disulfide bond (C22R-C37R) conserved among cytokine receptor class I (CRH I) family members bridges two beta strands.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269152    32 DADADDHSFWCHSQLEVDGSQHLLTCAFNDSDINTANLEFQICGAL-LRVKCLTLNKLQDIYFIKTSEFLLIGSSNICVK 110
Cdd:pfam18447   1 DAEPDDYSFSCFSQLEVDGSQHSLTCAFTDPDLNSTNLEFEICGALdLEVKCLNMEKLEDVYFIKTKKFLLIGNSDICVK 80

                          90
                  ....*....|....*..
gi 45269152   111 LGQKNLTCKNMAINTIV 127
Cdd:pfam18447  81 LEMKRKTCKSLKITKIV 97

Fibronectin type III domain; This domain is found in Interleukin-7 receptor subunit alpha (IL-7Ralpha), which together IL-7 form a complex crucial to several signalling cascades leading to the development and homeostasis of T and B cells. IL-7Ralpha carries a 219 residue ectodomain on the N-terminal region which is crucial for T and B-cell development. Mutations in the IL-7Ralpha ectodomain inhibits T and B cell development, resulting in patients with a form of severe combined immunodeficiency (SCID). The ectodomain folds into two fibronectin type III (FNIII) domains connected by a 310-helical linker. This entry comprises the first of the two FNIII domains, D1 while D2 domain is pfam00041. In the D1 domain of IL-7Ralpha, a disulfide bond (C22R-C37R) conserved among cytokine receptor class I (CRH I) family members bridges two beta strands.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269152    32 DADADDHSFWCHSQLEVDGSQHLLTCAFNDSDINTANLEFQICGAL-LRVKCLTLNKLQDIYFIKTSEFLLIGSSNICVK 110
Cdd:pfam18447   1 DAEPDDYSFSCFSQLEVDGSQHSLTCAFTDPDLNSTNLEFEICGALdLEVKCLNMEKLEDVYFIKTKKFLLIGNSDICVK 80

                          90
                  ....*....|....*..
gi 45269152   111 LGQKNLTCKNMAINTIV 127
Cdd:pfam18447  81 LEMKRKTCKSLKITKIV 97

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269152 130 EAPSDLKVVYRkEANDFLVTFNAPHLKKKYLKKVKhdVAYRPArGESNWTHVSL-FHTRTTIPQRKLRPKAMYEIKVRSi 208
Cdd:cd00063   2 SPPTNLRVTDV-TSTSVTLSWTPPEDDGGPITGYV--VEYREK-GSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRA- 76

                        90       100
                ....*....|....*....|.
gi 45269152 209 phndYFKGFWSEWSPSSTFET 229
Cdd:cd00063  77 ----VNGGGESPPSESVTVTT 93

Fibronectin type III domain; This domain is found in Interleukin-7 receptor subunit alpha (IL-7Ralpha), which together IL-7 form a complex crucial to several signalling cascades leading to the development and homeostasis of T and B cells. IL-7Ralpha carries a 219 residue ectodomain on the N-terminal region which is crucial for T and B-cell development. Mutations in the IL-7Ralpha ectodomain inhibits T and B cell development, resulting in patients with a form of severe combined immunodeficiency (SCID). The ectodomain folds into two fibronectin type III (FNIII) domains connected by a 310-helical linker. This entry comprises the first of the two FNIII domains, D1 while D2 domain is pfam00041. In the D1 domain of IL-7Ralpha, a disulfide bond (C22R-C37R) conserved among cytokine receptor class I (CRH I) family members bridges two beta strands.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269152    32 DADADDHSFWCHSQLEVDGSQHLLTCAFNDSDINTANLEFQICGAL-LRVKCLTLNKLQDIYFIKTSEFLLIGSSNICVK 110
Cdd:pfam18447   1 DAEPDDYSFSCFSQLEVDGSQHSLTCAFTDPDLNSTNLEFEICGALdLEVKCLNMEKLEDVYFIKTKKFLLIGNSDICVK 80

                          90
                  ....*....|....*..
gi 45269152   111 LGQKNLTCKNMAINTIV 127
Cdd:pfam18447  81 LEMKRKTCKSLKITKIV 97

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269152 130 EAPSDLKVVYRkEANDFLVTFNAPHLKKKYLKKVKhdVAYRPArGESNWTHVSL-FHTRTTIPQRKLRPKAMYEIKVRSi 208
Cdd:cd00063   2 SPPTNLRVTDV-TSTSVTLSWTPPEDDGGPITGYV--VEYREK-GSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRA- 76

                        90       100
                ....*....|....*....|.
gi 45269152 209 phndYFKGFWSEWSPSSTFET 229
Cdd:cd00063  77 ----VNGGGESPPSESVTVTT 93