programmed cell death 1 ligand 2 isoform X1 [Homo sapiens]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
IgV_PD-L2 | cd20983 | Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here ... |
20-119 | 7.96e-69 | |||
Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). Receptor-binding domain of PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients. : Pssm-ID: 409575 Cd Length: 100 Bit Score: 208.19 E-value: 7.96e-69
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IgC1_PD-L2 | cd20986 | Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here ... |
127-208 | 4.87e-60 | |||
Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients. : Pssm-ID: 409578 Cd Length: 82 Bit Score: 185.24 E-value: 4.87e-60
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Name | Accession | Description | Interval | E-value | |||
IgV_PD-L2 | cd20983 | Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here ... |
20-119 | 7.96e-69 | |||
Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). Receptor-binding domain of PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients. Pssm-ID: 409575 Cd Length: 100 Bit Score: 208.19 E-value: 7.96e-69
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IgC1_PD-L2 | cd20986 | Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here ... |
127-208 | 4.87e-60 | |||
Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients. Pssm-ID: 409578 Cd Length: 82 Bit Score: 185.24 E-value: 4.87e-60
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IG_like | smart00410 | Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG. |
35-119 | 2.11e-04 | |||
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: 39.41 E-value: 2.11e-04
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C2-set_2 | pfam08205 | CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily. |
138-194 | 4.10e-04 | |||
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily. Pssm-ID: 400489 Cd Length: 89 Bit Score: 38.55 E-value: 4.10e-04
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Ig_3 | pfam13927 | Immunoglobulin domain; This family contains immunoglobulin-like domains. |
22-103 | 1.61e-03 | |||
Immunoglobulin domain; This family contains immunoglobulin-like domains. Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 36.77 E-value: 1.61e-03
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Name | Accession | Description | Interval | E-value | |||
IgV_PD-L2 | cd20983 | Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here ... |
20-119 | 7.96e-69 | |||
Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). Receptor-binding domain of PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients. Pssm-ID: 409575 Cd Length: 100 Bit Score: 208.19 E-value: 7.96e-69
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IgC1_PD-L2 | cd20986 | Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here ... |
127-208 | 4.87e-60 | |||
Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients. Pssm-ID: 409578 Cd Length: 82 Bit Score: 185.24 E-value: 4.87e-60
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IgV_PDl1 | cd20947 | Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ... |
23-119 | 1.78e-23 | |||
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells. Pssm-ID: 409539 Cd Length: 110 Bit Score: 91.92 E-value: 1.78e-23
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IgV_B7-H3 | cd20934 | Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ... |
25-104 | 2.37e-05 | |||
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail. Pssm-ID: 409528 Cd Length: 115 Bit Score: 42.59 E-value: 2.37e-05
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IgC1 | cd00098 | Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ... |
136-193 | 3.26e-05 | |||
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, classical Ig-like domains resembling the antibody constant domain. Members of the IgC1 family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, while the IgC domain is involved in oligomerization and molecular interactions. 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 strands by G, F, C, and C'. Pssm-ID: 409354 Cd Length: 95 Bit Score: 41.68 E-value: 3.26e-05
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IgI_3_Contactin | cd04968 | Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ... |
23-103 | 8.54e-05 | |||
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains. Pssm-ID: 409357 [Multi-domain] Cd Length: 88 Bit Score: 40.61 E-value: 8.54e-05
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IG_like | smart00410 | Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG. |
35-119 | 2.11e-04 | |||
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: 39.41 E-value: 2.11e-04
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IgV_B7-H4 | cd20984 | Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ... |
35-105 | 2.16e-04 | |||
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer. Pssm-ID: 409576 Cd Length: 110 Bit Score: 39.89 E-value: 2.16e-04
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IgC1_Tapasin_R | cd05771 | Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ... |
138-199 | 3.02e-04 | |||
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain on Tapasin-R. Tapasin is a V-C1 (variable-constant) immunoglobulin superfamily molecule present in the endoplasmic reticulum (ER), where it links MHC class I molecules to the transporter associated with antigen processing (TAP). Tapasin-R is a tapasin-related protein that contains similar structural motifs to Tapasin, with some marked differences, especially in the V domain, transmembrane and cytoplasmic regions. The majority of Tapasin-R is located within the ER; however, there may be some expression of Tapasin-R at the cell surface. Tapasin-R lacks an obvious ER retention signal. Pssm-ID: 409428 Cd Length: 100 Bit Score: 39.40 E-value: 3.02e-04
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C2-set_2 | pfam08205 | CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily. |
138-194 | 4.10e-04 | |||
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily. Pssm-ID: 400489 Cd Length: 89 Bit Score: 38.55 E-value: 4.10e-04
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IgC1_2_Nectin-2_Necl-5_like | cd07703 | Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ... |
142-219 | 4.76e-04 | |||
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'. Pssm-ID: 409500 Cd Length: 97 Bit Score: 38.54 E-value: 4.76e-04
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IgV_MOG_like | cd05713 | Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ... |
70-119 | 8.55e-04 | |||
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM). Pssm-ID: 409378 Cd Length: 114 Bit Score: 38.33 E-value: 8.55e-04
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Ig_3 | pfam13927 | Immunoglobulin domain; This family contains immunoglobulin-like domains. |
22-103 | 1.61e-03 | |||
Immunoglobulin domain; This family contains immunoglobulin-like domains. Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 36.77 E-value: 1.61e-03
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IgC2_D1_D2_LILR_KIR_like | cd16843 | Immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer ... |
32-110 | 1.68e-03 | |||
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. Pssm-ID: 409518 [Multi-domain] Cd Length: 90 Bit Score: 36.97 E-value: 1.68e-03
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Ig_3 | pfam13927 | Immunoglobulin domain; This family contains immunoglobulin-like domains. |
133-196 | 2.27e-03 | |||
Immunoglobulin domain; This family contains immunoglobulin-like domains. Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 36.39 E-value: 2.27e-03
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Blast search parameters | ||||
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