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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919669 116 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEG 195
Cdd:cd05897    1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80

                         90
                 ....*....|....*
gi 767919669 196 QQYNITRSIELRIKK 210
Cdd:cd05897   81 KKYNITRSIELRIVK 95

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 767919669  25 PCPLEVVRSNVALVRVGNGSFCLhpsacgthrtVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSIELR 104
Cdd:cd20991   20 SCPLNPNESKGTITWYKNDSKTP----------ISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKIKITAK 89

                 .
gi 767919669 105 V 105
Cdd:cd20991   90 F 90

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919669 116 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEG 195
Cdd:cd05897    1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80

                         90
                 ....*....|....*
gi 767919669 196 QQYNITRSIELRIKK 210
Cdd:cd05897   81 KKYNITRSIELRIVK 95

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; 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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767919669  56 RTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRVF 106
Cdd:cd05756   46 TPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRNSTYCSKVSISLEVV 96

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919669  221 SPLKTISASLGSRLTIPCKVFlgTGTPLTTMLWWTANDTHIESAypggRVTEGPRQEYSENnenyievpLIFDPVTREDL 300
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIESL----KVKHDNGRTTQSS--------LLISNVTKEDA 66

                          90       100
                  ....*....|....*....|.
gi 767919669  301 HmDFKCVVHNTLSFQTLRTTV 321
Cdd:pfam00047  67 G-TYTCVVNNPGGSATLSTSL 86

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919669   129 VLVCPdlsefTRDKTDVKIQWYKD--SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHegqqYNITRSIEL 206
Cdd:smart00410  13 TLSCE-----ASGSPPPEVTWYKQggKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS----GSASSGTTL 83

                   ..
gi 767919669   207 RI 208
Cdd:smart00410  84 TV 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767919669  146 KIQWYKD-SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCV 188
Cdd:pfam13927  32 TITWYKNgEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919669 116 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEG 195
Cdd:cd05897    1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80

                         90
                 ....*....|....*
gi 767919669 196 QQYNITRSIELRIKK 210
Cdd:cd05897   81 KKYNITRSIELRIVK 95

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 767919669 116 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNeKFLSVRgtTHLLVHDVALEDAGYYRCVLTFAHEG 195
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDK-RFIPKG--SKLLIQNVTEEDAGNYTCKFTYTHNG 77

                         90
                 ....*....|....
gi 767919669 196 QQYNITRSIELRIK 209
Cdd:cd05757   78 KQYNVTRTISLTVT 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). 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 767919669 118 YPQILTLSTSGVLVCPDLsEFTRDKTDV--KIQWYKDSLLLDKDNEKFLSVRGTthLLVHDVALEDAGYYRCVLTFAHEG 195
Cdd:cd20994    3 YKQKVPFTSGGRIVCPHL-DFFKDENNNlpKVQWYKDCKPLLLDDKRFAGLESD--LLIFNVTVQDQGNYTCHTSYTYMG 79

                         90
                 ....*....|....
gi 767919669 196 QQYNITRSIELRIK 209
Cdd:cd20994   80 KQYNISRTISLIVL 93

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919669  221 SPLKTISASLGSRLTIPCKVFlgTGTPLTTMLWWTANDTHIESAypggRVTEGPRQEYSENnenyievpLIFDPVTREDL 300
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIESL----KVKHDNGRTTQSS--------LLISNVTKEDA 66

                          90       100
                  ....*....|....*....|.
gi 767919669  301 HmDFKCVVHNTLSFQTLRTTV 321
Cdd:pfam00047  67 G-TYTCVVNNPGGSATLSTSL 86

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 767919669  25 PCPLEVVRSNVALVRVGNGSFCLhpsacgthrtVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSIELR 104
Cdd:cd20991   20 SCPLNPNESKGTITWYKNDSKTP----------ISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKIKITAK 89

                 .
gi 767919669 105 V 105
Cdd:cd20991   90 F 90

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919669 119 PQILTLSTSG-VLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKflsVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQ 197
Cdd:cd20993    4 PVIAYIEYGGrTITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDR---VPKGDKLVIHVMLEHYQGNYTCVVTYETKGRT 80

                         90
                 ....*....|.
gi 767919669 198 YNITRSIELRI 208
Cdd:cd20993   81 IKLTRTVNVKV 91

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919669  217 PVIISPLKTISASLGSRLTIPCKVflgTGTPLTTMLWWtandthiesaYPGGRVTEGPRQEYSENNENYIevpLIFDPVT 296
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEA---TGSPPPTITWY----------KNGEPISSGSTRSRSLSGSNST---LTISNVT 65

                          90
                  ....*....|....
gi 767919669  297 REDlHMDFKCVVHN 310
Cdd:pfam13927  66 RSD-AGTYTCVASN 78

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

                           10        20        30
                   ....*....|....*....|....*....|...
gi 767919669    73 LWLLPALQEDSGTYVCTTRNASYCDKMSIELRV 105
Cdd:smart00410  53 LTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85

hypothetical protein; Provisional

                         10        20        30
                 ....*....|....*....|....*....|.
gi 767919669  75 LLPALQEDSGTYVCTTRNASYCDKMSIELRV 105
Cdd:PHA02633  22 ILNPTQSDSGIYMCITKNETYSDMMKFDLCI 52