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 564367946 226 PVIMSPRNETMEADPGSTIQLICNVTGQFTDLVYWKWNGSEIEWDDPILAEDYQFLEHPSAKRKYTLITTLNVSEVKSQF 305
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                         90       100
                 ....*....|....*....|....
gi 564367946 306 YRYPFICFVKNTHILETAHVRLVY 329
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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946  24 EYPNEVISFSSVNEIDIRSCPLTPNEmHGGTIIWYKNDSKTPISADKDSRIHQQNEHLWFVPAKMEDSGYYYCIMRNSTY 103
Cdd:cd20991    2 EREEQIILVSSANEIDVRSCPLNPNE-SKGTITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTY 80

                         90
                 ....*....|.
gi 564367946 104 CLKTKITMSVL 114
Cdd:cd20991   81 CLKIKITAKFV 91

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 564367946 226 PVIMSPRNETMEADPGSTIQLICNVTGQFTDLVYWKWNGSEIEWDDPILAEDYQFLEHPSAKRKYTLITTLNVSEVKSQF 305
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                         90       100
                 ....*....|....*....|....
gi 564367946 306 YRYPFICFVKNTHILETAHVRLVY 329
Cdd:cd20932   81 YKHPFTCFAKNTHGLDAAYVQLIY 104

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). 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. IL-1 receptor antagonist (IL-1RA), a naturally occurring cytokine, is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946  24 EYPNEVISFSSVNEIDIRSCPLTPNEmHGGTIIWYKNDSKTPISADKDSRIHQQNEHLWFVPAKMEDSGYYYCIMRNSTY 103
Cdd:cd20991    2 EREEQIILVSSANEIDVRSCPLNPNE-SKGTITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTY 80

                         90
                 ....*....|.
gi 564367946 104 CLKTKITMSVL 114
Cdd:cd20991   81 CLKIKITAKFV 91

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 564367946  388 YVLYPKTYGEGSFaylDTFVFKLLPEVleGQFGYKLFICGRDDYVGEDTIEVTNENVKRSRRLIIILVRDMGSFS-CLgq 466
Cdd:pfam01582   1 YDVFLSFRGSDTR---EWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGwCL-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946  467 sSEEQIAIYDALiREGIKIILLELEKIQDYE-----KMPESIQFIKQKH---GAICWSGDFKERP-------QSAKTRFW 531
Cdd:pfam01582  74 -DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEVAniwhsksVSDESKFW 151

                  ....*..
gi 564367946  532 KNLRYQM 538
Cdd:pfam01582 152 KKIAYDI 158

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946  130 QRLHVAGDGSLVCPYLdffkdeNNELPKVQWYKNCKPLPlDDGNFFgfknklmVMNVAEEHRGNYTCRTSYTYQGKQYPV 209
Cdd:pfam13895   9 TVVTEGEPVTLTCSAP------GNPPPSYTWYKDGSAIS-SSPNFF-------TLSVSAEDSGTYTCVARNGRGGKVSNP 74

                  ....*
gi 564367946  210 TRVIT 214
Cdd:pfam13895  75 VELTV 79

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

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564367946    42 SCPLTPNEMHggTIIWYKNDSKTPISADKDSRIHQQNEH-LWFVPAKMEDSGYYYCIMRNSTYCLKTKITMSV 113
Cdd:smart00410  15 SCEASGSPPP--EVTWYKQGGKLLAESGRFSVSRSGSTStLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 564367946   54 TIIWYKNDSKTPISADKDSRIHQQNEHLWFVPAKMEDSGYYYCIMRN 100
Cdd:pfam13927  32 TITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564367946  225 RPVIMSPRNETmEADPGSTIQLICNVTGQFTDLVYWKWNGSEI 267
Cdd:pfam13927   1 KPVITVSPSSV-TVREGETVTLTCEATGSPPPTITWYKNGEPI 42

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 564367946 226 PVIMSPRNETMEADPGSTIQLICNVTGQFTDLVYWKWNGSEIEWDDPILAEDYQFLEHPSAKRKYTLITTLNVSEVKSQF 305
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                         90       100
                 ....*....|....*....|....
gi 564367946 306 YRYPFICFVKNTHILETAHVRLVY 329
Cdd:cd20932   81 YKHPFTCFAKNTHGLDAAYVQLIY 104

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). 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. IL-1 receptor antagonist (IL-1RA), a naturally occurring cytokine, is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946  24 EYPNEVISFSSVNEIDIRSCPLTPNEmHGGTIIWYKNDSKTPISADKDSRIHQQNEHLWFVPAKMEDSGYYYCIMRNSTY 103
Cdd:cd20991    2 EREEQIILVSSANEIDVRSCPLNPNE-SKGTITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTY 80

                         90
                 ....*....|.
gi 564367946 104 CLKTKITMSVL 114
Cdd:cd20991   81 CLKIKITAKFV 91

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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946 127 SFIQRLHVAGDGSLVCPYLDFFKDENNeLPKVQWYKNCKPLPlDDGNFFGFKNKLMVMNVAEEHRGNYTCRTSYTYQGKQ 206
Cdd:cd05757    2 RYKQKLPITKGGKITCPDLDDYKNENV-LPPIQWYKDCKPLQ-GDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQ 79

                         90
                 ....*....|.
gi 564367946 207 YPVTRVITFIT 217
Cdd:cd05757   80 YNVTRTISLTV 90

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 564367946  388 YVLYPKTYGEGSFaylDTFVFKLLPEVleGQFGYKLFICGRDDYVGEDTIEVTNENVKRSRRLIIILVRDMGSFS-CLgq 466
Cdd:pfam01582   1 YDVFLSFRGSDTR---EWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGwCL-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946  467 sSEEQIAIYDALiREGIKIILLELEKIQDYE-----KMPESIQFIKQKH---GAICWSGDFKERP-------QSAKTRFW 531
Cdd:pfam01582  74 -DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEVAniwhsksVSDESKFW 151

                  ....*..
gi 564367946  532 KNLRYQM 538
Cdd:pfam01582 152 KKIAYDI 158

IL-beta-binding protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946  16 SLETDKCTEYPNEVISFSSV-NEIDIRSCPLTpNEMHGG----TIIWYKNdsktpiSADKDSRIHQQN-EHLWFVPAKME 89
Cdd:PHA02785  20 TFNAPECIDKGQYFASFMELeNEPVILPCPQI-NTLSSGynilDILWEKR------GADNDRIIPIDNgSNMLILNPTQS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946  90 DSGYYYCIMRNSTYC--LKTKITM-SVLENDPGLCyntqaSFIQRLHVAGDGSLVCPYLDFFKDENNELpKVQWYKNCKp 166
Cdd:PHA02785  93 DSGIYICITKNETYCdmMSLNLTIvSVSESNIDLI-----SYPQIVNERSTGEMVCPNINAFIASNVNA-DIIWSGHRR- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946 167 lplddgnffgFKNK---------LMVMNVAEEHRGNYTCRTSYTYQGKQYPVTRVITFitiddSKRDR---PVIMSPrnE 234
Cdd:PHA02785 166 ----------LRNKrlkqrtpgiITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKL-----EVRDRiipPTMQLP--E 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 564367946 235 TMEADPGSTIQLICNVTGQ--FTDL-VYWKWNGSEIEWDD 271
Cdd:PHA02785 229 GVVTSIGSNLTIACRVSLRppTTDAdVFWISNGMYYEEDD 268

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564367946  130 QRLHVAGDGSLVCPYLdffkdeNNELPKVQWYKNCKPLPlDDGNFFgfknklmVMNVAEEHRGNYTCRTSYTYQGKQYPV 209
Cdd:pfam13895   9 TVVTEGEPVTLTCSAP------GNPPPSYTWYKDGSAIS-SSPNFF-------TLSVSAEDSGTYTCVARNGRGGKVSNP 74

                  ....*
gi 564367946  210 TRVIT 214
Cdd:pfam13895  75 VELTV 79

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
                 ....*....|....*....|....*....|....*....|....*...
gi 564367946  54 TIIWYKNDSKTPISADKDSRIHQQNEHLWFVPAKMEDSGYYYCIMRNS 101
Cdd:cd00096   14 TITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNS 61

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        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564367946 139 SLVCPYldffkdENNELPKVQWYKNCKPLPLDDGNFFGFKN---KLMVMNVAEEHRGNYTCRTSYTYQGKQ 206
Cdd:cd00096    2 TLTCSA------SGNPPPTITWYKNGKPLPPSSRDSRRSELgngTLTISNVTLEDSGTYTCVASNSAGGSA 66

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

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564367946    42 SCPLTPNEMHggTIIWYKNDSKTPISADKDSRIHQQNEH-LWFVPAKMEDSGYYYCIMRNSTYCLKTKITMSV 113
Cdd:smart00410  15 SCEASGSPPP--EVTWYKQGGKLLAESGRFSVSRSGSTStLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 564367946 156 PKVQWYKNCKPLPLDDGNFFGFKNKLMVMNVAEEHRGNYTC 196
Cdd:cd05731   25 PDIRWIKLGGELPKGRTKFENFNKTLKIENVSEADSGEYQC 65

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. 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, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564367946  43 CPLTPNEMHggTIIWYKNDSKTPisadKDSRIHQQNEHLWFVPA-KMEDSGYYYCIMRN 100
Cdd:cd20957   23 CSVTGNPIH--TVLWMKDGKPLG----HSSRVQILSEDVLVIPSvKREDKGMYQCFVRN 75

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 564367946  156 PKVQWYKN---CKPLPLDDGNFFGFKNKLMVMNVAEEHRGNYTCRTS 199
Cdd:pfam13927  31 PTITWYKNgepISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. 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, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564367946 130 QRLHVAGDGSLVCPYldffkdENNELPKVQWYKNCKPLPLDDGNFFGFKNKLMVMNVAEEHRGNYTC 196
Cdd:cd20957   11 QTVDFGRTAVFNCSV------TGNPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSVKREDKGMYQC 71

Immunoglobulin I-set domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564367946   54 TIIWYKNDSktPISADKDSRIHQQNEH--LWFVPAKMEDSGYYYCIMRNSTYCLKTKITMSV 113
Cdd:pfam07679  31 EVSWFKDGQ--PLRSSDRFKVTYEGGTytLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90