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Conserved domains on  [gi|240255491|ref|NP_001155315|]
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interleukin-18 receptor 1 isoform b precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 131-205 1.25e-08

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.


The actual alignment was detected with superfamily member cd05757:

Pssm-ID: 472250  Cd Length: 92  Bit Score: 51.94  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491 131 VEVNKSLHITC------KNPNYEELIQdtWlYKNCKEISKTPR--------ILKDAEFGDEGYYSCVFSVHHNGTRYNIT 196
Cdd:cd05757    7 LPITKGGKITCpdlddyKNENVLPPIQ--W-YKDCKPLQGDKRfipkgsklLIQNVTEEDAGNYTCKFTYTHNGKQYNVT 83


                 ....*....
gi 240255491 197 KTVNITVIE 205
Cdd:cd05757   84 RTISLTVTE 92
Ig_6 super family cl39786
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
 3-98 2.54e-05

Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 receptor alpha (IL-18Ra). IL-18Ra ectodomain folds into three immunoglobulin (Ig)-like domains, similar to IL-1 receptors. Each domain comprises a two-layer sandwich of six to nine beta-strands and contains at least one intra-domain disulfide bond.


The actual alignment was detected with superfamily member pfam18452:

Pssm-ID: 465773  Cd Length: 128  Bit Score: 43.56  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491    3 HEELILtLCILIVKSASKSCiHRSQIHVVEGEPfylKPCGISAPVHRnetatMRWFKGSASHEYRELNNRSSPRVTFHDH 82
Cdd:pfam18452   4 EEEFVL-FCDLPEPQKTHFY-HRSQLSPTQGPH---LPCSGSKDLSD-----VQWYWQPKNGDPLEAITESSPHIIQEGN 73

                          90
                  ....*....|....*.
gi 240255491   83 TLEFWPVEMEDEGTYI 98
Cdd:pfam18452  74 ALWFLPVGVNDSGSYI 89
PHA02785 super family cl31505
IL-beta-binding protein; Provisional
 157-257 2.11e-04

IL-beta-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02785:

Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 42.70  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491 157 KNCKEISKTPRIL--KDAEFGDEGYYSCVFSVHHNGTRYNITKTVNITViegRSKVTPAILG-PkcEKVGVELGKDVELN 233
Cdd:PHA02785 167 RNKRLKQRTPGIItiEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEV---RDRIIPPTMQlP--EGVVTSIGSNLTIA 241

                         90       100       110
                 ....*....|....*....|....*....|.
gi 240255491 234 CSASLN----KDDLFYWS---IRKEDSSDPN 257
Cdd:PHA02785 242 CRVSLRppttDADVFWISngmYYEEDDEDGD 272
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 212-312 1.53e-03

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.


The actual alignment was detected with superfamily member cd20932:

Pssm-ID: 472250  Cd Length: 104  Bit Score: 37.64  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491 212 PAILGPKCEKVGVELGKDVELNCSASLNKDDLFYW----SIRKEDssDPNVQEDRKETTTWISEGKLHASKILRFQKITE 287
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWkwngSEIDED--DPVLGEDYYSVENPANKRKSTLITVLNISEIES 78

                         90       100
                 ....*....|....*....|....*
gi 240255491 288 NYLNVLYNCTVANEEAIDTKSFVLV 312
Cdd:cd20932   79 RFYKHPFTCFAKNTHGLDAAYVQLI 103
 
Name Accession Description Interval E-value
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 131-205 1.25e-08

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.


Pssm-ID: 409415  Cd Length: 92  Bit Score: 51.94  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491 131 VEVNKSLHITC------KNPNYEELIQdtWlYKNCKEISKTPR--------ILKDAEFGDEGYYSCVFSVHHNGTRYNIT 196
Cdd:cd05757    7 LPITKGGKITCpdlddyKNENVLPPIQ--W-YKDCKPLQGDKRfipkgsklLIQNVTEEDAGNYTCKFTYTHNGKQYNVT 83


                 ....*....
gi 240255491 197 KTVNITVIE 205
Cdd:cd05757   84 RTISLTVTE 92
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
 3-98 2.54e-05

Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 receptor alpha (IL-18Ra). IL-18Ra ectodomain folds into three immunoglobulin (Ig)-like domains, similar to IL-1 receptors. Each domain comprises a two-layer sandwich of six to nine beta-strands and contains at least one intra-domain disulfide bond.


Pssm-ID: 465773  Cd Length: 128  Bit Score: 43.56  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491    3 HEELILtLCILIVKSASKSCiHRSQIHVVEGEPfylKPCGISAPVHRnetatMRWFKGSASHEYRELNNRSSPRVTFHDH 82
Cdd:pfam18452   4 EEEFVL-FCDLPEPQKTHFY-HRSQLSPTQGPH---LPCSGSKDLSD-----VQWYWQPKNGDPLEAITESSPHIIQEGN 73

                          90
                  ....*....|....*.
gi 240255491   83 TLEFWPVEMEDEGTYI 98
Cdd:pfam18452  74 ALWFLPVGVNDSGSYI 89
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 157-257 2.11e-04

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 42.70  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491 157 KNCKEISKTPRIL--KDAEFGDEGYYSCVFSVHHNGTRYNITKTVNITViegRSKVTPAILG-PkcEKVGVELGKDVELN 233
Cdd:PHA02785 167 RNKRLKQRTPGIItiEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEV---RDRIIPPTMQlP--EGVVTSIGSNLTIA 241

                         90       100       110
                 ....*....|....*....|....*....|.
gi 240255491 234 CSASLN----KDDLFYWS---IRKEDSSDPN 257
Cdd:PHA02785 242 CRVSLRppttDADVFWISngmYYEEDDEDGD 272
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 26-112 1.32e-03

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 37.48  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491    26 SQIHVVEGEPFYLkPCgisaPVHRNETATMRWFKGSasHEYRELNNRSSPRVTFHDHTLEFWPVEMEDEGTYI----SQV 101
Cdd:smart00410   2 PSVTVKEGESVTL-SC----EASGSPPPEVTWYKQG--GKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTcaatNSS 74

                           90
                   ....*....|.
gi 240255491   102 GNDRRNWTLNV 112
Cdd:smart00410  75 GSASSGTTLTV 85
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 212-312 1.53e-03

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.


Pssm-ID: 409526  Cd Length: 104  Bit Score: 37.64  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491 212 PAILGPKCEKVGVELGKDVELNCSASLNKDDLFYW----SIRKEDssDPNVQEDRKETTTWISEGKLHASKILRFQKITE 287
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWkwngSEIDED--DPVLGEDYYSVENPANKRKSTLITVLNISEIES 78

                         90       100
                 ....*....|....*....|....*
gi 240255491 288 NYLNVLYNCTVANEEAIDTKSFVLV 312
Cdd:cd20932   79 RFYKHPFTCFAKNTHGLDAAYVQLI 103
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 27-103 9.28e-03

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. 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.


Pssm-ID: 409584  Cd Length: 108  Bit Score: 35.67  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491  27 QIHVVEGEPFYLKPCGISAPVHRNETA------TMRWFKGSASHEYRELNNRSSP--RVTFHDHTLEFWPVEMEDEGTYI 98
Cdd:cd20992   10 QIQVFEGEPARIKCPLFEHFLKYNYSTahsaglTLIWYWTRQDRDLEEPINFRLPdnRISKEKDVLWFRPTLLNDTGNYT 89


                 ....*
gi 240255491  99 SQVGN 103
Cdd:cd20992   90 CMLRN 94
 
Name Accession Description Interval E-value
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 131-205 1.25e-08

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.


Pssm-ID: 409415  Cd Length: 92  Bit Score: 51.94  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491 131 VEVNKSLHITC------KNPNYEELIQdtWlYKNCKEISKTPR--------ILKDAEFGDEGYYSCVFSVHHNGTRYNIT 196
Cdd:cd05757    7 LPITKGGKITCpdlddyKNENVLPPIQ--W-YKDCKPLQGDKRfipkgsklLIQNVTEEDAGNYTCKFTYTHNGKQYNVT 83


                 ....*....
gi 240255491 197 KTVNITVIE 205
Cdd:cd05757   84 RTISLTVTE 92
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
 3-98 2.54e-05

Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 receptor alpha (IL-18Ra). IL-18Ra ectodomain folds into three immunoglobulin (Ig)-like domains, similar to IL-1 receptors. Each domain comprises a two-layer sandwich of six to nine beta-strands and contains at least one intra-domain disulfide bond.


Pssm-ID: 465773  Cd Length: 128  Bit Score: 43.56  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491    3 HEELILtLCILIVKSASKSCiHRSQIHVVEGEPfylKPCGISAPVHRnetatMRWFKGSASHEYRELNNRSSPRVTFHDH 82
Cdd:pfam18452   4 EEEFVL-FCDLPEPQKTHFY-HRSQLSPTQGPH---LPCSGSKDLSD-----VQWYWQPKNGDPLEAITESSPHIIQEGN 73

                          90
                  ....*....|....*.
gi 240255491   83 TLEFWPVEMEDEGTYI 98
Cdd:pfam18452  74 ALWFLPVGVNDSGSYI 89
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 142-205 3.14e-05

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). 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.


Pssm-ID: 409586  Cd Length: 94  Bit Score: 42.45  E-value: 3.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240255491 142 KNPNyEELIQDTWlYKNCKEISKTPR---------ILKDAEFGDEGYYSCVFSVHHNGTRYNITKTVNITVIE 205
Cdd:cd20994   24 KDEN-NNLPKVQW-YKDCKPLLLDDKrfaglesdlLIFNVTVQDQGNYTCHTSYTYMGKQYNISRTISLIVLE 94
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 157-257 2.11e-04

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 42.70  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491 157 KNCKEISKTPRIL--KDAEFGDEGYYSCVFSVHHNGTRYNITKTVNITViegRSKVTPAILG-PkcEKVGVELGKDVELN 233
Cdd:PHA02785 167 RNKRLKQRTPGIItiEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEV---RDRIIPPTMQlP--EGVVTSIGSNLTIA 241

                         90       100       110
                 ....*....|....*....|....*....|.
gi 240255491 234 CSASLN----KDDLFYWS---IRKEDSSDPN 257
Cdd:PHA02785 242 CRVSLRppttDADVFWISngmYYEEDDEDGD 272
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 26-112 1.32e-03

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 37.48  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491    26 SQIHVVEGEPFYLkPCgisaPVHRNETATMRWFKGSasHEYRELNNRSSPRVTFHDHTLEFWPVEMEDEGTYI----SQV 101
Cdd:smart00410   2 PSVTVKEGESVTL-SC----EASGSPPPEVTWYKQG--GKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTcaatNSS 74

                           90
                   ....*....|.
gi 240255491   102 GNDRRNWTLNV 112
Cdd:smart00410  75 GSASSGTTLTV 85
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 212-312 1.53e-03

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.


Pssm-ID: 409526  Cd Length: 104  Bit Score: 37.64  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491 212 PAILGPKCEKVGVELGKDVELNCSASLNKDDLFYW----SIRKEDssDPNVQEDRKETTTWISEGKLHASKILRFQKITE 287
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWkwngSEIDED--DPVLGEDYYSVENPANKRKSTLITVLNISEIES 78

                         90       100
                 ....*....|....*....|....*
gi 240255491 288 NYLNVLYNCTVANEEAIDTKSFVLV 312
Cdd:cd20932   79 RFYKHPFTCFAKNTHGLDAAYVQLI 103
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 169-205 3.95e-03

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). 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 the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and 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.


Pssm-ID: 409478  Cd Length: 95  Bit Score: 36.27  E-value: 3.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 240255491 169 LKDAEFGDEGYYSCVFSVHHNGTRYNITKTVNITVIE 205
Cdd:cd05897   59 IHDVSLNDSGYYTCKLTFTHEGKKYNITRSIELRIVK 95
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 27-103 9.28e-03

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. 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.


Pssm-ID: 409584  Cd Length: 108  Bit Score: 35.67  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255491  27 QIHVVEGEPFYLKPCGISAPVHRNETA------TMRWFKGSASHEYRELNNRSSP--RVTFHDHTLEFWPVEMEDEGTYI 98
Cdd:cd20992   10 QIQVFEGEPARIKCPLFEHFLKYNYSTahsaglTLIWYWTRQDRDLEEPINFRLPdnRISKEKDVLWFRPTLLNDTGNYT 89


                 ....*
gi 240255491  99 SQVGN 103
Cdd:cd20992   90 CMLRN 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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