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 1622872257 286 PDPPQGLRVESVPgfPRRLRASWTYPASWPRQphfLLKFRLQYRPAQHPAWSTVRPGVEPAgLEEMITDAVAGLPHAVRV 365
Cdd:cd00063     1 PSPPTNLRVTDVT--STSVTLSWTPPEDDGGP---ITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRV 74

                          90
                  ....*....|....*..
gi 1622872257 366 SARdflDAGTWSTWSPE 382
Cdd:cd00063    75 RAV---NGGGESPPSES 88

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 1622872257 286 PDPPQGLRVESVPgfPRRLRASWTYPASWPRQphfLLKFRLQYRPAQHPAWSTVRPGVEPAgLEEMITDAVAGLPHAVRV 365
Cdd:cd00063     1 PSPPTNLRVTDVT--STSVTLSWTPPEDDGGP---ITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRV 74

                          90
                  ....*....|....*..
gi 1622872257 366 SARdflDAGTWSTWSPE 382
Cdd:cd00063    75 RAV---NGGGESPPSES 88

Immunoglobulin-like domain D1 of interleukin-6 receptor alpha-chain (IL-6RA, also known as CD126); member of the C2-set of IgSF domains; The members here are composed of the immunoglobulin-like domain D1 of interleukin-6 receptor alpha-chain (IL-6RA, also known as CD126). The IL-6RA ectodomain, which is highly modular, consisting of three domains (D1, D2, and D3). Interleukin-6 (IL-6) is a multifunctional cytokine that regulates the immune response, hemopoiesis, the acute phase response and inflammation. It is generated in an infectious lesion and sends out a warning signal to the entire body. IL-6 binds first to its cognate alpha-chain receptor (IL-6R), and then the IL-6/IL-6R complex which in turn induces homodimerization of gp130. As a result, a high-affinity functional receptor complex of IL-6, IL-6R and gp130 is formed, and subsequently the complex triggers a downstream signal cascade. Aberrant production of IL-6 and its receptor (IL-6R) are implicated in the pathogenesis of multiple myeloma, autoimmune diseases and prostate cancer. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains. Unlike other Ig domain sets, the C2-set lacks the D strand.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622872257  89 PGRSVKLCCPGVTAGDPVS--W-FRDGEPRLLQGPDSGLGHELVLTQADSTDEGTYICqTLDGALGGTVTL 156
Cdd:cd20939     6 PGASVTLTCPGVEPEDNATihWvLRKPAAGSHPSRWAGMGRRLLLRSVQLSDSGNYSC-YRAGRPAGTVHL 75

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 1622872257 286 PDPPQGLRVESVPgfPRRLRASWTYPASWPRQphfLLKFRLQYRPAQHPAWSTVRPGVEPAgLEEMITDAVAGLPHAVRV 365
Cdd:cd00063     1 PSPPTNLRVTDVT--STSVTLSWTPPEDDGGP---ITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRV 74

                          90
                  ....*....|....*..
gi 1622872257 366 SARdflDAGTWSTWSPE 382
Cdd:cd00063    75 RAV---NGGGESPPSES 88

Immunoglobulin-like domain D1 of interleukin-6 receptor alpha-chain (IL-6RA, also known as CD126); member of the C2-set of IgSF domains; The members here are composed of the immunoglobulin-like domain D1 of interleukin-6 receptor alpha-chain (IL-6RA, also known as CD126). The IL-6RA ectodomain, which is highly modular, consisting of three domains (D1, D2, and D3). Interleukin-6 (IL-6) is a multifunctional cytokine that regulates the immune response, hemopoiesis, the acute phase response and inflammation. It is generated in an infectious lesion and sends out a warning signal to the entire body. IL-6 binds first to its cognate alpha-chain receptor (IL-6R), and then the IL-6/IL-6R complex which in turn induces homodimerization of gp130. As a result, a high-affinity functional receptor complex of IL-6, IL-6R and gp130 is formed, and subsequently the complex triggers a downstream signal cascade. Aberrant production of IL-6 and its receptor (IL-6R) are implicated in the pathogenesis of multiple myeloma, autoimmune diseases and prostate cancer. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains. Unlike other Ig domain sets, the C2-set lacks the D strand.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622872257  89 PGRSVKLCCPGVTAGDPVS--W-FRDGEPRLLQGPDSGLGHELVLTQADSTDEGTYICqTLDGALGGTVTL 156
Cdd:cd20939     6 PGASVTLTCPGVEPEDNATihWvLRKPAAGSHPSRWAGMGRRLLLRSVQLSDSGNYSC-YRAGRPAGTVHL 75

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622872257  93 VKLCCPgvTAGDP---VSWFRDGEPRLLQGPDS----GLGHELVLTQADSTDEGTYICQ 144
Cdd:cd00096     1 VTLTCS--ASGNPpptITWYKNGKPLPPSSRDSrrseLGNGTLTISNVTLEDSGTYTCV 57

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622872257  89 PGRSVKLCCPGVTAGDPVSWFRDGEPRLLQG----PDSGLGHELVLTQADSTDEGTYIC 143
Cdd:cd20967    11 KGHKIRLTVELADPDAEVKWYKDGQELQSSSkvifESIGAKRTLTVQQASLADAGEYQC 69