Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R) and similar proteins. Members of this family are characterized by extracellular immunoglobulin-like domains and intracellular Toll/Interleukin-1R (TIR) domain. Three naturally occurring ligands for the IL-1 receptor (IL1R) are known: the agonists IL-1alpha and IL-1beta and the IL-1-receptor antagonist IL1RA. IL-1Rs are involved in immune host defense and hematopoiesis. After binding to interleukin-1, IL1R associates with the coreceptor IL1RAP (interleukin 1 receptor accessory protein, also known as IL-1R3) to form the high affinity interleukin-1 receptor complex, which induces multiple cellular responses including NF-kappa-B activation, IL-2 secretion, and IL-2 promoter activation. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. IL1R binds ligands with comparable affinity to its antagonist IL1RA, and binding of IL1RA to IL1R, prevents association of the latter with IL1RAP to form a signaling complex.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079  43 PVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRF 122
Cdd:cd20932     1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                          90       100
                  ....*....|....*....|....
gi 1005261079 123 YKHPFTCFAKNTHGIDAAYIQLIY 146
Cdd:cd20932    81 YKHPFTCFAKNTHGLDAAYVQLIY 104

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
                  ....*....|....*....|....*....|....*.
gi 1005261079   1 MNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLE 36
Cdd:cd20994    59 FNVTVQDQGNYTCHTSYTYMGKQYNISRTISLIVLE 94

Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R) and similar proteins. Members of this family are characterized by extracellular immunoglobulin-like domains and intracellular Toll/Interleukin-1R (TIR) domain. Three naturally occurring ligands for the IL-1 receptor (IL1R) are known: the agonists IL-1alpha and IL-1beta and the IL-1-receptor antagonist IL1RA. IL-1Rs are involved in immune host defense and hematopoiesis. After binding to interleukin-1, IL1R associates with the coreceptor IL1RAP (interleukin 1 receptor accessory protein, also known as IL-1R3) to form the high affinity interleukin-1 receptor complex, which induces multiple cellular responses including NF-kappa-B activation, IL-2 secretion, and IL-2 promoter activation. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. IL1R binds ligands with comparable affinity to its antagonist IL1RA, and binding of IL1RA to IL1R, prevents association of the latter with IL1RAP to form a signaling complex.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079  43 PVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRF 122
Cdd:cd20932     1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                          90       100
                  ....*....|....*....|....
gi 1005261079 123 YKHPFTCFAKNTHGIDAAYIQLIY 146
Cdd:cd20932    81 YKHPFTCFAKNTHGLDAAYVQLIY 104

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079 205 YILYPKTVGEGSTsdcDIFVFKVLPEVleKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSW-Lgg 283
Cdd:pfam01582   1 YDVFLSFRGSDTR---EWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWcL-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079 284 sSEEQIAMYNALvQDGIKVVLLELEKIQDYE-----KMPESIKFIKQKH---GAIRWSGDFTQGP-------QSAKTRFW 348
Cdd:pfam01582  74 -DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEVAniwhsksVSDESKFW 151

                  ....*..
gi 1005261079 349 KNVRYHM 355
Cdd:pfam01582 152 KKIAYDI 158

IL-beta-binding protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079   2 NVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPtrPVIVSPanETMEVDLGSQIQLICNVTGQLSDI---AYWK 78
Cdd:PHA02785  183 DVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDRIIP--PTMQLP--EGVVTSIGSNLTIACRVSLRPPTTdadVFWI 258

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005261079  79 WNGSVIDEDDPVlGEDYYSVENP---ANKRRsTLITVLNISEIESRfYKHPFTCFAKNTHGI 137
Cdd:PHA02785  259 SNGMYYEEDDED-GDGRISVANKiytTDKRR-VITSRLNINPVKEE-DATTFTCMAFTIPSI 317

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079  42 RPVIVSPaNETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDpvlgedyySVENPANKRRSTLiTVLNISEIESR 121
Cdd:pfam13927   1 KPVITVS-PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGS--------TRSRSLSGSNSTL-TISNVTRSDAG 70

                          90
                  ....*....|..
gi 1005261079 122 FYkhpfTCFAKN 133
Cdd:pfam13927  71 TY----TCVASN 78

Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R) and similar proteins. Members of this family are characterized by extracellular immunoglobulin-like domains and intracellular Toll/Interleukin-1R (TIR) domain. Three naturally occurring ligands for the IL-1 receptor (IL1R) are known: the agonists IL-1alpha and IL-1beta and the IL-1-receptor antagonist IL1RA. IL-1Rs are involved in immune host defense and hematopoiesis. After binding to interleukin-1, IL1R associates with the coreceptor IL1RAP (interleukin 1 receptor accessory protein, also known as IL-1R3) to form the high affinity interleukin-1 receptor complex, which induces multiple cellular responses including NF-kappa-B activation, IL-2 secretion, and IL-2 promoter activation. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. IL1R binds ligands with comparable affinity to its antagonist IL1RA, and binding of IL1RA to IL1R, prevents association of the latter with IL1RAP to form a signaling complex.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079  43 PVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRF 122
Cdd:cd20932     1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                          90       100
                  ....*....|....*....|....
gi 1005261079 123 YKHPFTCFAKNTHGIDAAYIQLIY 146
Cdd:cd20932    81 YKHPFTCFAKNTHGLDAAYVQLIY 104

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079 205 YILYPKTVGEGSTsdcDIFVFKVLPEVleKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSW-Lgg 283
Cdd:pfam01582   1 YDVFLSFRGSDTR---EWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWcL-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079 284 sSEEQIAMYNALvQDGIKVVLLELEKIQDYE-----KMPESIKFIKQKH---GAIRWSGDFTQGP-------QSAKTRFW 348
Cdd:pfam01582  74 -DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEVAniwhsksVSDESKFW 151

                  ....*..
gi 1005261079 349 KNVRYHM 355
Cdd:pfam01582 152 KKIAYDI 158

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1005261079   1 MNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLE 36
Cdd:cd05757    57 QNVTEEDAGNYTCKFTYTHNGKQYNVTRTISLTVTE 92

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079   51 ETMEVDLGSQIQLICNVTGQLSDIAYWKWNGsvideDDPVLGEDYYSVENpaNKRRSTLiTVLNISEIESRFYkhpfTCF 130
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQG-----GKLLAESGRFSVSR--SGSTSTL-TISNVTPEDSGTY----TCA 69

                           90
                   ....*....|....*
gi 1005261079  131 AKNTHGIDAAYIQLI 145
Cdd:smart00410  70 ATNSSGSASSGTTLT 84

Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261079  56 DLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSvenpANKRRSTLITVLNISEIESRFYkhpFTCFAKNTH 135
Cdd:cd05773    21 DGSSDANLVCQAQGVPRVQFRWAKNGVPLDLGNPRYEETTEH----TGTVHTSILTIINVSAALDYAL---FTCTAHNSL 93

                          90
                  ....*....|
gi 1005261079 136 GIDAAYIQLI 145
Cdd:cd05773    94 GEDSLDIQLV 103