Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132814489 108 WLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKDRKYFHHNSDFHIPKATLKDSGSYFCRGLVGSKNVSSETVN 187
Cdd:cd05753    1 WLLLQAPSAVVFEGEPLTLRCHGWKDKKVHKVTYYKDGKALKFSYENSNFSIPQATLSDSGSYHCSGTVRIKRRSSESVN 80

                 ...
gi 132814489 188 ITI 190
Cdd:cd05753   81 ITV 83

Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132814489 108 WLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKDRKYFHHNSDFHIPKATLKDSGSYFCRGLVGSKNVSSETVN 187
Cdd:cd05753    1 WLLLQAPSAVVFEGEPLTLRCHGWKDKKVHKVTYYKDGKALKFSYENSNFSIPQATLSDSGSYHCSGTVRIKRRSSESVN 80

                 ...
gi 132814489 188 ITI 190
Cdd:cd05753   81 ITV 83

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 132814489   30 LEPQWYSVLEKDSVTLKCQgAYSPEDNSTQWFHNENLISSQaSSYFIDAATVNDSGEYRCQ---TNLSTLSDPVQLEV 104
Cdd:pfam13895   4 LTPSPTVVTEGEPVTLTCS-APGNPPPSYTWYKDGSAISSS-PNFFTLSVSAEDSGTYTCVarnGRGGKVSNPVELTV 79

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132814489  108 WLLLQAPRWVFKEEDPIHLRCHSWKNtALHKVTYLQNGKDRKYfhhNSDFHIPKATLKDSGSYFCRGLVGSKNVSSETVN 187
Cdd:pfam13895   1 KPVLTPSPTVVTEGEPVTLTCSAPGN-PPPSYTWYKDGSAISS---SPNFFTLSVSAEDSGTYTCVARNGRGGKVSNPVE 76

                  ...
gi 132814489  188 ITI 190
Cdd:pfam13895  77 LTV 79

Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132814489 108 WLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKDRKYFHHNSDFHIPKATLKDSGSYFCRGLVGSKNVSSETVN 187
Cdd:cd05753    1 WLLLQAPSAVVFEGEPLTLRCHGWKDKKVHKVTYYKDGKALKFSYENSNFSIPQATLSDSGSYHCSGTVRIKRRSSESVN 80

                 ...
gi 132814489 188 ITI 190
Cdd:cd05753   81 ITV 83

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 132814489   30 LEPQWYSVLEKDSVTLKCQgAYSPEDNSTQWFHNENLISSQaSSYFIDAATVNDSGEYRCQ---TNLSTLSDPVQLEV 104
Cdd:pfam13895   4 LTPSPTVVTEGEPVTLTCS-APGNPPPSYTWYKDGSAISSS-PNFFTLSVSAEDSGTYTCVarnGRGGKVSNPVELTV 79

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132814489    32 PQWYSVLEKDSVTLKCQGAYSPEDNSTqWFHNENLI-----------SSQASSYFIDAATVNDSGEYRCQTNLS--TLSD 98
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVT-WYKQGGKLlaesgrfsvsrSGSTSTLTISNVTPEDSGTYTCAATNSsgSASS 79

                   ....*.
gi 132814489    99 PVQLEV 104
Cdd:smart00410  80 GTTLTV 85

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132814489  108 WLLLQAPRWVFKEEDPIHLRCHSWKNtALHKVTYLQNGKDRKYfhhNSDFHIPKATLKDSGSYFCRGLVGSKNVSSETVN 187
Cdd:pfam13895   1 KPVLTPSPTVVTEGEPVTLTCSAPGN-PPPSYTWYKDGSAISS---SPNFFTLSVSAEDSGTYTCVARNGRGGKVSNPVE 76

                  ...
gi 132814489  188 ITI 190
Cdd:pfam13895  77 LTV 79

First immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors (LILRs), Natural killer inhibitory receptors (KIRs) and similar domains; member of Immunoglobulin Constant-2 set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors (LILRs) and Natural killer inhibitory receptors (KIRs, also known as also known as cluster of differentiation (CD) 158), and similar proteins. This group includes LILRB1 (also known as LIR-1), LILRA5 (also known as LIR9), an activating natural cytotoxicity receptor NKp46, the immune-type receptor glycoprotein VI (GPVI), and the IgA-specific receptor Fc-alphaRI (also known as cluster of differentiation (CD) 89). LILRs are a family of immunoreceptors expressed on expressed on T and B cells, on monocytes, dendritic cells, and subgroups of natural killer (NK) cells. The human LILR family contains nine proteins (LILRA1-3, and 5, and LILRB1-5). From functional assays, and as the cytoplasmic domains of various LILRs, for example LILRB1, LILRB2 (also known as LIR-2), and LILRB3 (also known as LIR-3) contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs), it is thought that LIR proteins are inhibitory receptors. Of the eight LIR family proteins, only LILRB1, and LILRB2, show detectable binding to class I MHC molecules; ligands for the other members have yet to be determined. The extracellular portions of the different LIR proteins contain different numbers of Ig-like domains for example, four in the case of LILRB1, and LILRB2, and two in the case of LILRB4 (also known as LIR-5). The activating natural cytotoxicity receptor NKp46 is expressed in natural killer cells, and is organized as an extracellular portion having two Ig-like extracellular domains, a transmembrane domain, and a small cytoplasmic portion. GPVI, which also contains two Ig-like domains, participates in the processes of collagen-mediated platelet activation and arterial thrombus formation. Fc-alphaRI is expressed on monocytes, eosinophils, neutrophils, and macrophages; it mediates IgA-induced immune effector responses such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and respiratory burst. Killer cell immunoglobulin-like receptors (KIRs; also known as CD158 for human KIR) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. KIRs are a family of highly polymorphic activating and inhibitory receptors that serve as key regulators of human NK cell function. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The major ligands for KIR are MHC class I (HLA-A, -B or -C) molecules.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132814489  36 SVLEKD-SVTLKCQGaySPEDNSTQWFHNENLISSQ-------ASSYFIDAATVNDSGEYRCQTNLSTL----SDPVQLE 103
Cdd:cd05751   10 SVIPLEkSVTIRCQG--TPEAFLYQLEKEGNSTETVipkkpqkKAEFIIPHMNSRTAGRYRCRYRKGAGwsepSDLLELV 87

                 .
gi 132814489 104 V 104
Cdd:cd05751   88 V 88

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 132814489   30 LEPQWYSVLEKDSVTLKCQGAYSPEDNSTQWFH-NENLISSQ----------ASSYFIDAATVNDSGEYRCQTNlsTLSD 98
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKeGGTLIESLkvkhdngrttQSSLLISNVTKEDAGTYTCVVN--NPGG 78

                  ....*.
gi 132814489   99 PVQLEV 104
Cdd:pfam00047  79 SATLST 84

Immunoglobulin (Ig)-like domain of platelet-derived growth factor (PDGF) receptors (R), alpha and beta; member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of platelet-derived growth factor (PDGF) receptors (R), alpha (also known as cluster of differentiation (CD) 140a), and beta (also known as CD140b). PDGF is a potent mitogen for connective tissue cells. PDGF-stimulated processes are mediated by three different PDGFs (PDGF-A,PDGF-B, and PDGF-C). PDGFRalpha binds to all three PDGFs, whereas the PDGFRbeta binds only to PDGF-B. PDGFRs alpha and beta have similar organization: an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. In mice, PDGFRalpha and PDGFRbeta are essential for normal development.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132814489 111 LQAPRWVFKEEDPIHLRCHSWKNTALH-KVTY--------LQNGKDRK--YFHHNSDFHIPKATLKDSGSYFCRGLVGSK 179
Cdd:cd05861    7 MEAVKTVVRQGETITLMCIVIGNEVVDlEWTYpgkesgrgIEPVEEFKvpPYHLVYTLTIPSATLEDSGTYECAVTEATN 86

                         90
                 ....*....|..
gi 132814489 180 NVSSE-TVNITI 190
Cdd:cd05861   87 DHQDEkKINITV 98

Second immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer inhibitory receptors (KIRs) and similar domains; member of Immunoglobulin Constant-2 set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors (LILRs), Natural killer inhibitory receptors (KIRs, also known as also known as cluster of differentiation (CD) 158), and similar proteins. This group includes LILRB1 (also known as LIR-1), LILRA5 (also known as LIR9), an activating natural cytotoxicity receptor NKp46, the immune-type receptor glycoprotein VI (GPVI), and the IgA-specific receptor Fc-alphaRI (also known as cluster of differentiation (CD) 89). LILRs are a family of immunoreceptors expressed on expressed on T and B cells, on monocytes, dendritic cells, and subgroups of natural killer (NK) cells. The human LILR family contains nine proteins (LILRA1-3, and 5, and LILRB1-5). From functional assays, and as the cytoplasmic domains of various LILRs, for example LILRB1, LILRB2 (also known as LIR-2), and LILRB3 (also known as LIR-3) contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs), it is thought that LIR proteins are inhibitory receptors. Of the eight LIR family proteins, only LILRB1, and LILRB2, show detectable binding to class I MHC molecules; ligands for the other members have yet to be determined. The extracellular portions of the different LIR proteins contain different numbers of Ig-like domains for example, four in the case of LILRB1, and LILRB2, and two in the case of LILRB4 (also known as LIR-5). The activating natural cytotoxicity receptor NKp46 is expressed in natural killer cells, and is organized as an extracellular portion having two Ig-like extracellular domains, a transmembrane domain, and a small cytoplasmic portion. GPVI, which also contains two Ig-like domains, participates in the processes of collagen-mediated platelet activation and arterial thrombus formation. Fc-alphaRI is expressed on monocytes, eosinophils, neutrophils, and macrophages; it mediates IgA-induced immune effector responses such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and respiratory burst. Killer cell immunoglobulin-like receptors (KIRs; also known as CD158 for human KIR) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. KIRs are a family of highly polymorphic activating and inhibitory receptors that serve as key regulators of human NK cell function. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The major ligands for KIR are MHC class I (HLA-A, -B or -C) molecules.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 132814489  43 VTLKCQGAYSPE--------DNSTQWFHnenLISSQASsYFIDAATVNDSGEYRC-------QTNLSTLSDPVQLEV 104
Cdd:cd05711   18 VTLQCHSRIGFDrfilykegRSPLLQFH---GSGFQAS-FPLGPVTPAHAGTYRCygsynhsPYEWSAPSDPLEIVV 90

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132814489 114 PRWVFKEEDPIHLRCHSWKNTALhkVTYLQNGKD-------RKYFHHNSDFHIPKATLKDSGSYFCRglvgSKNVSSETV 186
Cdd:cd04979    4 KQISVKEGDTVILSCSVKSNNAP--VTWIHNGKKvpryrspRLVLKTERGLLIRSAQEADAGVYECH----SGERVLGST 77

                 ....*
gi 132814489 187 NITIT 191
Cdd:cd04979   78 LRSVT 82