First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62944694  32 AVITLQPPWASIFQKENVTLWCEGPHLPGDSSTQWFINGTVVQTSTPSYSISVASFQDSGEYRCQIGSSVPSDPVQLQI 110
Cdd:cd05752   1 AVVSLDPPWTTVFQGEKVTLTCQGFYSPEQNSTQWYHNGTLISSTSSSYRIVAATVNDSGEYRCQTQGSSLSDPVHLEV 79

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62944694  32 AVITLQPPWASIFQKENVTLWCEGPHLPGDSSTQWFINGTVVQTSTPSYSISVASFQDSGEYRCQIGSSVPSDPVQLQI 110
Cdd:cd05752   1 AVVSLDPPWTTVFQGEKVTLTCQGFYSPEQNSTQWYHNGTLISSTSSSYRIVAATVNDSGEYRCQTQGSSLSDPVHLEV 79

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 62944694   205 ASVSSPFPEGSLVTLNCETNLllQRPGLQLYFSFYVGSKIL-------EYRNTSSEYHIARAEREDAGFYWCEVATEDSS 277
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSAST--GSPGPDVTWSKEGGTLIEslkvkhdNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79

                  .
gi 62944694   278 V 278
Cdd:pfam00047  80 A 80

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62944694    213 EGSLVTLNCETN------LLLQRPGLQLyfSFYVGSKILEYRNTSSEYHIARAEREDAGFYWCEV 271
Cdd:smart00410   8 EGESVTLSCEASgspppeVTWYKQGGKL--LAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAA 70

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62944694  32 AVITLQPPWASIFQKENVTLWCEGPHLPGDSSTQWFINGTVVQTSTPSYSISVASFQDSGEYRCQIGSSVPSDPVQLQI 110
Cdd:cd05752   1 AVVSLDPPWTTVFQGEKVTLTCQGFYSPEQNSTQWYHNGTLISSTSSSYRIVAATVNDSGEYRCQTQGSSLSDPVHLEV 79

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 62944694   205 ASVSSPFPEGSLVTLNCETNLllQRPGLQLYFSFYVGSKIL-------EYRNTSSEYHIARAEREDAGFYWCEVATEDSS 277
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSAST--GSPGPDVTWSKEGGTLIEslkvkhdNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79

                  .
gi 62944694   278 V 278
Cdd:pfam00047  80 A 80

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62944694    33 VITLQPPWASIFQKENVTLWCEGPHLPgDSSTQWFINGTVVQT----------STPSYSISVASFQDSGEYRCQ 96
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSP-PPTITWYKNGEPISSgstrsrslsgSNSTLTISNVTRSDAGTYTCV 75

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 first and second immunoglobulin (Ig)-like domains 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 62944694  47 ENVTLWCEGPhlPGDSSTQWFING--TVVQTSTPSYSISVASF-------QDSGEYRCQIGS----SVPSDPVQL 108
Cdd:cd16843  16 ENVTIRCQGP--PEAVLFQLYKEGnsLSQGTVREKEPQNKAEFyiphmdrNHAGRYRCRYRSgtlwSEPSDPLEL 88