beta-trefoil domain found in the family of interleukin-36 (IL-36) and similar proteins; The IL-36 family includes three members, IL-36 alpha (also called FIL1 epsilon, or interleukin-1 epsilon, or IL-1 epsilon, or interleukin-1 family member 6, or IL-1F6), IL-36 beta (also called FIL1 eta, or interleukin-1 eta, or IL-1 eta, or interleukin-1 family member 8, or IL-1F8, or interleukin-1 homolog 2, or IL-1H2), and IL-36 gamma (also called IL-1-related protein 2, or IL-1RP2, or interleukin-1 epsilon, or IL-1 epsilon, or interleukin-1 family member 9, or IL-1F9, or interleukin-1 homolog 1, or IL-1H1). They act as cytokines that bind to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. They are parts of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; like the IL-1 system with which they share the co-receptor IL1RAP. They may be involved in skin inflammatory response by acting on keratinocytes, dendritic cells, and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. Members in this family contain a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388113  14 AVYQS-----ITVAVITCKYPEALEQGRGDPIYLGIQNPEMCLYCEKVGEQPTLQLKEQKIMDLYGQPEPVKPFLFYRAK 88
Cdd:cd23300   24 AVPRSdnvtpVTLALIPCRDTEFLEKDKGNPIYLGIKGPELCLFCEEIGGQPTLQLKEKNIMDLYNEPEAVKPFLFYHNQ 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 514388113  89 TGRTSTLESVAFPDWFIASS-KRDQPIILTSELGKSYNTAFELNI 132
Cdd:cd23300  104 TGSTSTFESAAYPGWFIASSsEGGQPIILTKERGKTYNTNFYLDS 148

beta-trefoil domain found in the family of interleukin-36 (IL-36) and similar proteins; The IL-36 family includes three members, IL-36 alpha (also called FIL1 epsilon, or interleukin-1 epsilon, or IL-1 epsilon, or interleukin-1 family member 6, or IL-1F6), IL-36 beta (also called FIL1 eta, or interleukin-1 eta, or IL-1 eta, or interleukin-1 family member 8, or IL-1F8, or interleukin-1 homolog 2, or IL-1H2), and IL-36 gamma (also called IL-1-related protein 2, or IL-1RP2, or interleukin-1 epsilon, or IL-1 epsilon, or interleukin-1 family member 9, or IL-1F9, or interleukin-1 homolog 1, or IL-1H1). They act as cytokines that bind to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. They are parts of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; like the IL-1 system with which they share the co-receptor IL1RAP. They may be involved in skin inflammatory response by acting on keratinocytes, dendritic cells, and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. Members in this family contain a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388113  14 AVYQS-----ITVAVITCKYPEALEQGRGDPIYLGIQNPEMCLYCEKVGEQPTLQLKEQKIMDLYGQPEPVKPFLFYRAK 88
Cdd:cd23300   24 AVPRSdnvtpVTLALIPCRDTEFLEKDKGNPIYLGIKGPELCLFCEEIGGQPTLQLKEKNIMDLYNEPEAVKPFLFYHNQ 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 514388113  89 TGRTSTLESVAFPDWFIASS-KRDQPIILTSELGKSYNTAFELNI 132
Cdd:cd23300  104 TGSTSTFESAAYPGWFIASSsEGGQPIILTKERGKTYNTNFYLDS 148

Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and beta are also known as hematopoietin and catabolin.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388113    39 PIYLGIQNPEMCLYCEKVGEQPTLQLKEQKIMDlYGQPEPVKPFLFYRAKTGRTSTLESVAFPDWFIASSK-RDQPIILT 117
Cdd:smart00125  55 PVTLGISGTNLYLSCVKKGDEPTLQLEMVDPPK-YPKKEMEKRFVFEKHEIGNKVEFESAAHPNWFISTSQeEDKPVFLG 133

                           90
                   ....*....|.
gi 514388113   118 SELGKSYNTAF 128
Cdd:smart00125 134 NGPPSQDITDF 144

beta-trefoil domain found in the family of interleukin-36 (IL-36) and similar proteins; The IL-36 family includes three members, IL-36 alpha (also called FIL1 epsilon, or interleukin-1 epsilon, or IL-1 epsilon, or interleukin-1 family member 6, or IL-1F6), IL-36 beta (also called FIL1 eta, or interleukin-1 eta, or IL-1 eta, or interleukin-1 family member 8, or IL-1F8, or interleukin-1 homolog 2, or IL-1H2), and IL-36 gamma (also called IL-1-related protein 2, or IL-1RP2, or interleukin-1 epsilon, or IL-1 epsilon, or interleukin-1 family member 9, or IL-1F9, or interleukin-1 homolog 1, or IL-1H1). They act as cytokines that bind to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. They are parts of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; like the IL-1 system with which they share the co-receptor IL1RAP. They may be involved in skin inflammatory response by acting on keratinocytes, dendritic cells, and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. Members in this family contain a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388113  14 AVYQS-----ITVAVITCKYPEALEQGRGDPIYLGIQNPEMCLYCEKVGEQPTLQLKEQKIMDLYGQPEPVKPFLFYRAK 88
Cdd:cd23300   24 AVPRSdnvtpVTLALIPCRDTEFLEKDKGNPIYLGIKGPELCLFCEEIGGQPTLQLKEKNIMDLYNEPEAVKPFLFYHNQ 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 514388113  89 TGRTSTLESVAFPDWFIASS-KRDQPIILTSELGKSYNTAFELNI 132
Cdd:cd23300  104 TGSTSTFESAAYPGWFIASSsEGGQPIILTKERGKTYNTNFYLDS 148

beta-trefoil domain found in interleukin-37 (IL-37) and similar proteins; IL-37, also called FIL1 zeta, or IL-1X, or interleukin-1 family member 7, or IL-1F7, or interleukin-1 homolog 4, or IL-1H, or IL-1H4, or interleukin-1 zeta, or IL-1 zeta, or interleukin-1-related protein, or IL-1RP1, or interleukin-23, or IL-23, acts as a suppressor of innate inflammatory and immune responses involved in curbing excessive inflammation. This function requires SMAD3. It suppresses, or reduces, proinflammatory cytokine production, including IL1A and IL6, as well as CCL12, CSF1, CSF2, CXCL13, IL1B, IL23A, and IL1RN, but spares anti-inflammatory cytokines and inhibits dendritic cell activation. IL-37 contains a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388113  33 EQGRGDPIYLGIQNPEMCLYCEKVGEQ--PTLQLKEQKIMDLYGQPEP-VKPFLFYRAKTGRTSTLESVAFPDWFI-ASS 108
Cdd:cd23301   48 SEEKGNPIFLAVSKGELCLCCEKVKGQkhPSLQLKKKKINELNSQKEKeLLPFTFYKEKVGSYFTLESAANPGYFIcTSN 127

                         90       100
                 ....*....|....*....|.
gi 514388113 109 KRDQPIILTSELGKSYNTAFE 129
Cdd:cd23301  128 TPGQPVGVTDKLGKEKNIEFS 148

beta-trefoil domain found in interleukin-1 beta (IL-1 beta) and similar proteins; IL-1 beta, also called catabolin, is a potent inflammatory cytokine that activates the inflammatory process. It was initially discovered as the major endogenous pyrogen. It induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. IL-1 beta promotes Th17 differentiation of T-cells and synergizes with IL12/interleukin-12 to induce IFN-gamma synthesis from T-helper 1 (Th1) cells. It plays a role in angiogenesis by inducing vascular endothelial growth factor (VEGF) production synergistically with tumor necrosis factor (TNF) and IL-6. IL-1 beta contains a C-terminal beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388113  35 GRGDPIYLGIQNPEMCLYCEKVGEQPTLQLKEQKIMDlYGQPEPVKPFLFYRAKT-GRTSTLESVAFPDWFIASSKRD-Q 112
Cdd:cd23296   53 GGKIPVALGIKGKNLYLSCVKKGDKPTLQLEEVDPKN-DSKSKDLKRFLFYKIESiGSTTTFESAAFPGWYISTSQAEnQ 131

                         90
                 ....*....|....*...
gi 514388113 113 PIILTSELGKSYNTAFEL 130
Cdd:cd23296  132 PVFLGNQKGQQRITDFTL 149

Interleukin-1 / 18; This family includes interleukin-1 and interleukin-18.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388113   17 QSITVAVITCKYP-EALEQGRGDPIYLGIQNPEMCLYCEKVGEqPTLQLKEQKIMDLYGQPEPVKPFLFYRAKTGRTSTL 95
Cdd:pfam00340   4 QNLNLEVKFDMSFyKGDSDDSKIPVTLGIKGKKLYLSCVNKDE-PVLQLEEVNIPKLIKNKESDKRFFFIRSESKNYVEF 82

                          90       100
                  ....*....|....*....|...
gi 514388113   96 ESVAFPDWFIASSK-RDQPIILT 117
Cdd:pfam00340  83 ESAAYPGWFIATKQeEDLPVFLV 105

beta-trefoil domain found in interleukin-38 (IL-38) and similar proteins; IL-38, also called interleukin-1 family member 10, or IL-1F10, or family of interleukin 1-theta, or FIL1 theta, or interleukin-1 HY2, or IL-1HY2, or interleukin-1 theta, or IL-1 theta, acts as cytokine with immunomodulatory activity. Alone, it does not induce cytokine production, but reduces IL22 and IL17A production by T-cells in response to heat-killed Candida albicans. It also reduces IL36G-induced production of IL8 by peripheral blood mononuclear cells. It increases IL6 production by dendritic cells stimulated by bacterial lipopolysaccharides (LPS). IL-38 contains a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514388113  39 PIYLGIQNPEMCLYCEKVGEQPTLQLKEQKIMDLYGQPEPVKPFLFYRAKTGRTSTLESVAFPDWFI-ASSKRDQPIILT 117
Cdd:cd23302   54 PIFLGIQGGSRCLACVETEEGPSLQLEDVNIEELYKGGEEATRFTFFQSSSGSAFRLEAAAWPGWFLcGPAEPQQPVQLT 133

                         90
                 ....*....|.
gi 514388113 118 SELGKSYNTAF 128
Cdd:cd23302  134 KESEPSARTKF 144