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Conserved domains on  [gi|83287884|sp|Q9NZQ7|]
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RecName: Full=Programmed cell death 1 ligand 1; Short=PD-L1; Short=PDCD1 ligand 1; Short=Programmed death ligand 1; Short=hPD-L1; AltName: Full=B7 homolog 1; Short=B7-H1; AltName: CD_antigen=CD274; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
 21-130 3.58e-81

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: 240.22  E-value: 3.58e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  21 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 100
Cdd:cd20947   1 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 80

                        90       100       110
                ....*....|....*....|....*....|
gi 83287884 101 ITDVKLQDAGVYRCMISYGGADYKRITVKV 130
Cdd:cd20947  81 ITDVKLQDAGVYRCMISYGGADYKRITVKV 110
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 138-211 9.07e-13

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.


The actual alignment was detected with superfamily member cd20986:

Pssm-ID: 472250  Cd Length: 82  Bit Score: 62.74  E-value: 9.07e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83287884 138 NQRILVVdPVTSEHELTCQAEGYPKAEVIWtssdhQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTF 211
Cdd:cd20986   1 DTHILEV-PGTGEVQLTCQARGYPLAEVSW-----QNVSVPANTSHTRTPEGLYQVTSVLRLKPQPGRNFSCMF 68
 
Name Accession Description Interval E-value
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
 21-130 3.58e-81

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: 240.22  E-value: 3.58e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  21 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 100
Cdd:cd20947   1 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 80

                        90       100       110
                ....*....|....*....|....*....|
gi 83287884 101 ITDVKLQDAGVYRCMISYGGADYKRITVKV 130
Cdd:cd20947  81 ITDVKLQDAGVYRCMISYGGADYKRITVKV 110
IgC1_PD-L2 cd20986
Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here ...
 138-211 9.07e-13

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: 62.74  E-value: 9.07e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83287884 138 NQRILVVdPVTSEHELTCQAEGYPKAEVIWtssdhQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTF 211
Cdd:cd20986   1 DTHILEV-PGTGEVQLTCQARGYPLAEVSW-----QNVSVPANTSHTRTPEGLYQVTSVLRLKPQPGRNFSCMF 68
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 135-220 5.22e-07

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 46.64  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884   135 NKINQRILVVDPVTSEHELTCQAE-GYPKAEVIWTSSDhQVLSGKTTTTNSKREEKLFNVTSTLRINTT---TNEIFYCT 210
Cdd:pfam08205   1 PTIEPPASLLEGEGPEVVATCSSAgGKPAPRITWYLDG-KPLEAAETSSEQDPESGLVTVTSELKLVPSrsdHGQSLTCQ 79

                          90
                  ....*....|
gi 83287884   211 FRRLDPEENH 220
Cdd:pfam08205  80 VSYGALRGSI 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 24-130 6.75e-06

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: 43.65  E-value: 6.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884     24 PKDLYVVEyGSNMTIECKFPVEKQLDlaaliVYWEmedKNIIQFVHGEEDLKVQHSSyrqrarllkdqlslGNAALQITD 103
Cdd:smart00410   1 PPSVTVKE-GESVTLSCEASGSPPPE-----VTWY---KQGGKLLAESGRFSVSRSG--------------STSTLTISN 57

                           90       100
                   ....*....|....*....|....*...
gi 83287884    104 VKLQDAGVYRCMISYGGADYKR-ITVKV 130
Cdd:smart00410  58 VTPEDSGTYTCAATNSSGSASSgTTLTV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 23-128 5.72e-05

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.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.03  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884    23 VPKDLYVVEYGSNMTIECK-FPVEKQLDlaaliVYWEMEDKNIIqfvhgeEDLKVQHSSYRQRarllkdqlslgNAALQI 101
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSaSTGSPGPD-----VTWSKEGGTLI------ESLKVKHDNGRTT-----------QSSLLI 58

                          90       100
                  ....*....|....*....|....*...
gi 83287884   102 TDVKLQDAGVYRCMISY-GGADYKRITV 128
Cdd:pfam00047  59 SNVTKEDAGTYTCVVNNpGGSATLSTSL 86
 
Name Accession Description Interval E-value
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
 21-130 3.58e-81

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: 240.22  E-value: 3.58e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  21 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 100
Cdd:cd20947   1 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 80

                        90       100       110
                ....*....|....*....|....*....|
gi 83287884 101 ITDVKLQDAGVYRCMISYGGADYKRITVKV 130
Cdd:cd20947  81 ITDVKLQDAGVYRCMISYGGADYKRITVKV 110
IgV_PD-L2 cd20983
Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here ...
 19-130 1.46e-24

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: 94.94  E-value: 1.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  19 FTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALivywemedKNIIQFVhgEEDLkvqhSSYRQRARLLKDQLSLGNAA 98
Cdd:cd20983   2 FTVTVPKELYTVDHGSNVTLECDFDTGEHVELGAI--------RASLQKV--ENDT----SLHSERATLLEEQLPLGKAL 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 83287884  99 LQITDVKLQDAGVYRCMISYGGA-DYKRITVKV 130
Cdd:cd20983  68 FHIPSVQVRDAGQYRCLIIYGVAwDYKYLTLKV 100
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
 23-134 7.09e-17

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: 74.95  E-value: 7.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  23 VPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMED--KNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 100
Cdd:cd20934   2 VPEDPVVALVGTDATLRCSFSPEPGFSLAQLSVFWQLTDtkQLVHSFTESQDQGRDQGSAYANRTALFPDLLAQGNASLR 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 83287884 101 ITDVKLQDAGVYRCMISYGGADYKRITVKVNAPY 134
Cdd:cd20934  82 LQRVRVADEGSYTCFVSVQDFGSAAVSLQVAAPF 115
IgV_B7-H4 cd20984
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ...
 33-117 3.25e-14

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: 67.62  E-value: 3.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  33 GSNMTIECKFpvEKQLDLAALIVYWEMEDknIIQFVH----GEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQD 108
Cdd:cd20984  12 GEDGILSCTF--TPDIKLSDIVIQWLKEG--DSGLVHefkeGKDELSRQSPMFRGRTSLFADQVHVGNASLRLKNVQLTD 87


                ....*....
gi 83287884 109 AGVYRCMIS 117
Cdd:cd20984  88 AGTYLCIIS 96
IgC1_PD-L2 cd20986
Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here ...
 138-211 9.07e-13

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: 62.74  E-value: 9.07e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83287884 138 NQRILVVdPVTSEHELTCQAEGYPKAEVIWtssdhQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTF 211
Cdd:cd20986   1 DTHILEV-PGTGEVQLTCQARGYPLAEVSW-----QNVSVPANTSHTRTPEGLYQVTSVLRLKPQPGRNFSCMF 68
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 54-117 5.92e-12

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 61.25  E-value: 5.92e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83287884  54 IVYWEMEDKNIiqFVH----GEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMIS 117
Cdd:cd16091  28 VIHWYKQDSDI--KVHsyyyGKDQLESQDQRYRNRTSLFKDQISNGNASLLLRRVQLQDEGRYKCYTS 93
IgV_B7-H2 cd20935
Immunoglobulin Variable (IgV) domain of B7-H2 (B7 homolog 2); The members here are composed of ...
 33-116 8.21e-08

Immunoglobulin Variable (IgV) domain of B7-H2 (B7 homolog 2); The members here are composed of the immunoglobulin variable (IgV) domain of B7-H2 (B7 homolog 2 also known as ICOSL (inducible T cell costimulator ligand) or CD275). B7-H2 is a ligand for the T-cell-specific cell surface receptor ICOS and acts as a costimulatory signal for T-cell proliferation and cytokine secretion. The interaction of ICOS with ICOSL (B7-H2) regulates T cell activation and expansion, is involved in T cell dependent B cell activation, and T-helper cell differentiation. It is a member of the B7 family of immune regulatory proteins and shares homology with other B7 ligands, such as B7-1, B7-2, B7-H1 (PD-L1), PD-L2, and B7-H3. The extracellular domains of B7 proteins contain two Ig-like domains and all members have short cytoplasmic domains. These ligands are typically expressed on antigen presenting cells (such as macrophages, B cells and dendritic cells) and have the ability to regulate T-cell proliferation and function. Tumor cells are also capable of expressing the B7 family members in order to evade immune surveillance.


Pssm-ID: 409529  Cd Length: 113  Bit Score: 49.86  E-value: 8.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  33 GSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQH--SSYRQRARLLKDQLSLGNAALQITDVKLQDAG 110
Cdd:cd20935   8 GSDVELSCICPEGSRFDLNDLYVYWQISESETVVTYHLPQNSSLENvdSHYRNRALLSLDSMKQGDFSLRLFNVTPQDEQ 87


                ....*.
gi 83287884 111 VYRCMI 116
Cdd:cd20935  88 KFHCLV 93
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
 66-114 9.88e-08

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: 49.50  E-value: 9.88e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 83287884  66 QFVH----GEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRC 114
Cdd:cd05713  44 PVVHlyrdGQDQEEEQMPEYRGRTELLKDAIAEGSVALRIHNVRPSDEGQYTC 96
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 135-220 5.22e-07

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 46.64  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884   135 NKINQRILVVDPVTSEHELTCQAE-GYPKAEVIWTSSDhQVLSGKTTTTNSKREEKLFNVTSTLRINTT---TNEIFYCT 210
Cdd:pfam08205   1 PTIEPPASLLEGEGPEVVATCSSAgGKPAPRITWYLDG-KPLEAAETSSEQDPESGLVTVTSELKLVPSrsdHGQSLTCQ 79

                          90
                  ....*....|
gi 83287884   211 FRRLDPEENH 220
Cdd:pfam08205  80 VSYGALRGSI 89
IgV_CD33 cd05712
Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic ...
 19-113 4.93e-06

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 409377  Cd Length: 119  Bit Score: 44.69  E-value: 4.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  19 FTVTVPKDLYVVEyGSNMTIECKF--PVEKQLDlAALIVYW--EMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDqLSL 94
Cdd:cd05712   1 WGLQMPKSVTVQE-GLCVLIPCSFsyPADYWVS-NPVHGYWyrGGPYPKYRPPVATNNRTREVHESTQGRFRLLGD-PGK 77

                        90
                ....*....|....*....
gi 83287884  95 GNAALQITDVKLQDAGVYR 113
Cdd:cd05712  78 KNCSLSISDARPEDSGKYF 96
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 24-130 6.75e-06

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: 43.65  E-value: 6.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884     24 PKDLYVVEyGSNMTIECKFPVEKQLDlaaliVYWEmedKNIIQFVHGEEDLKVQHSSyrqrarllkdqlslGNAALQITD 103
Cdd:smart00410   1 PPSVTVKE-GESVTLSCEASGSPPPE-----VTWY---KQGGKLLAESGRFSVSRSG--------------STSTLTISN 57

                           90       100
                   ....*....|....*....|....*...
gi 83287884    104 VKLQDAGVYRCMISYGGADYKR-ITVKV 130
Cdd:smart00410  58 VTPEDSGTYTCAATNSSGSASSgTTLTV 85
IgV_B7-H6 cd20981
Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the ...
 35-114 2.58e-05

Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H6 (also known as NCR3LG1). B7-H6 contains one IgV domain and one IgC domain (IgV-IgC) and belongs to the B7-family, which consists of structurally related cell-surface protein ligands which bind to receptors on lymphocytes that regulate immune responses. B7-H6 is a ligand of NKp30, which is a member of CD28 family and an activating receptor of natural killer (NK) cells. The expression of NKp30 has been found in most of NK cells, which is involved in the process of tumor cell killing and interaction with antigen presenting cells (APCs) such as dendritic cells. Studies showed that NK cells eliminate B7-H6-expressing tumor cells either directly via cytotoxicity or indirectly by cytokine secretion. For instance, chimeric NKp30-expressing T cells responded to B7-H6(+) tumor cells and those T cells produced IFN-gamma and killed B7-H6-expressing tumor cells in vivo. B7-H6 mRNA is not found in normal cells, while high expression of B7-H6 is found in certain type tumor cells, such as lymphoma, leukemia, ovarian cancer, brain tumors, breast cancers, and various sarcomas. Since B7-H6 can bind NKp30 to exert anti-tumor effects by NK cells, which are able to recognize the difference between cancer cells and normal cells, B7-H6 may serve as a promising target for cancer immunotherapy.


Pssm-ID: 409573  Cd Length: 114  Bit Score: 42.60  E-value: 2.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  35 NMTIECKFPVEKQLDLAALIVYWEMEDKNIiqfvhgEEDLKV------QHSSYRQRARLLKDQLSLGNAALQITDVKLQD 108
Cdd:cd20981  18 NVTIFCNIFYSQPLNITSMGITWFRKSLTF------DKEVKVfeffgdHQKAFRPGAIVSPWRLKSGDASLQLPGVQLEE 91


                ....*.
gi 83287884 109 AGVYRC 114
Cdd:cd20981  92 AGEYRC 97
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 23-128 5.72e-05

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.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.03  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884    23 VPKDLYVVEYGSNMTIECK-FPVEKQLDlaaliVYWEMEDKNIIqfvhgeEDLKVQHSSYRQRarllkdqlslgNAALQI 101
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSaSTGSPGPD-----VTWSKEGGTLI------ESLKVKHDNGRTT-----------QSSLLI 58

                          90       100
                  ....*....|....*....|....*...
gi 83287884   102 TDVKLQDAGVYRCMISY-GGADYKRITV 128
Cdd:pfam00047  59 SNVTKEDAGTYTCVVNNpGGSATLSTSL 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 152-210 8.28e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 40.24  E-value: 8.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83287884   152 ELTCQAEGYPKAEVIWTssdhqvLSGKTTTTNSKREEKLFNVTSTLRINTTTNE---IFYCT 210
Cdd:pfam13927  20 TLTCEATGSPPPTITWY------KNGEPISSGSTRSRSLSGSNSTLTISNVTRSdagTYTCV 75
IgV_CD86 cd16087
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here ...
 40-116 8.98e-05

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409508  Cd Length: 108  Bit Score: 40.77  E-value: 8.98e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83287884  40 CKFPVEKQLDLAALIVYWEMEDKNII-QFVHGEEDLKVQHSSYRQRARLLKDqlslgNAALQITDVKLQDAGVYRCMI 116
Cdd:cd16087  15 CQFKNPQNISLSELVVFWQDQKKLVLyELYLGKEKLDNVNSKYIGRTSFDQE-----NWTLQLHNVQIKDQGTYQCFI 87
IgC1_CD80 cd16083
Immunoglobulin constant (IgC)-like domain of antigen receptor Cluster of Differentiation (CD) ...
 145-221 1.45e-04

Immunoglobulin constant (IgC)-like domain of antigen receptor Cluster of Differentiation (CD) 80; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin constant (IgC)-like domain of the antigen receptor Cluster of Differentiation (CD) 80. CD80 (also known as glycoprotein B7-1) and CD86 (also known as glycoprotein B7-2) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. CD80 contains two Ig-like domains, an amino-terminal immunoglobulin variable (IgV)-like domain characteristic of adhesion molecules, and a membrane proximal immunoglobulin constant (IgC)-like domain similar to the constant domains of antigen receptors. Members of the Ig 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, and the IgC domain is involved in oligomerization and molecular interactions.


Pssm-ID: 409505  Cd Length: 91  Bit Score: 40.14  E-value: 1.45e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83287884 145 DPVTSEHELTCQAEG-YPKAEVIWTSSDhQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHT 221
Cdd:cd16083  11 NPSPNIKRIICSTSGgFPEPRLSWLENG-EELNAINTTVSQDPETELYTVSSELDFNVTYNHSIVCLIKYGDSRVSKN 87
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 24-130 1.46e-04

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggrecan has a wide distribution in connective tissue and extracellular matrices. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409481  Cd Length: 123  Bit Score: 40.69  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  24 PKDLYVVeYGSNMTIECKFPVEKQLDLAALIVY-------WEM--EDKNIIQFVHGEEDLKVQhSSYRQRARLLKDQLSL 94
Cdd:cd05900   4 ESPLRVV-LGSSLLIPCYFQDPIAKDPGAPTVAplsprikWSFisKEKESVLLVATEGKVRVN-TEYLDRVSLPNYPAIP 81

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 83287884  95 GNAALQITDVKLQDAGVYRCMISYGGAD-YKRITVKV 130
Cdd:cd05900  82 SDATLEITELRSNDSGTYRCEVMHGIEDnYDTVEVQV 118
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 23-131 1.53e-04

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.


Pssm-ID: 409381  Cd Length: 100  Bit Score: 40.07  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  23 VPKDLYVVEYGSNMTIECKFPVEKQLDLaaliVYWEMEDKNIIQfvhgeedlKVQHSSYRQRAR--LLKDQLSLGNAALQ 100
Cdd:cd05716   2 VGPEVVTGVEGGSVTIQCPYPPKYASSR----KYWCKWGSEGCQ--------TLVSSEGVVPGGriSLTDDPDNGVFTVT 69

                        90       100       110
                ....*....|....*....|....*....|.
gi 83287884 101 ITDVKLQDAGVYRCMISYGGADYKRITVKVN 131
Cdd:cd05716  70 LNQLRKEDAGWYWCGVGDDGDRGLTVQVKLV 100
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 14-130 2.89e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. 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. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 39.03  E-value: 2.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  14 HLLNAFTVTVpkdlyvvEYGSNMTIECK---FPvekqldlaALIVYWEMEDKNIIQFVHGEEdlkvqhssYRQRARLlkd 90
Cdd:cd20970   5 TPQPSFTVTA-------REGENATFMCRaegSP--------EPEISWTRNGNLIIEFNTRYI--------VRENGTT--- 58

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 83287884  91 qlslgnaaLQITDVKLQDAGVYRCMISYG--GADYKRITVKV 130
Cdd:cd20970  59 --------LTIRNIRRSDMGIYLCIASNGvpGSVEKRITLQV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 20-117 3.51e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.70  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884    20 TVTVPKDLYVVEYGSNMTIECKFpvekqldlaalivywEMEDKNIIQFVHGEEDLKVQHSSYRQrarllkdqLSLGNAAL 99
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEA---------------TGSPPPTITWYKNGEPISSGSTRSRS--------LSGSNSTL 59

                          90
                  ....*....|....*...
gi 83287884   100 QITDVKLQDAGVYRCMIS 117
Cdd:pfam13927  60 TISNVTRSDAGTYTCVAS 77
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 22-130 3.74e-04

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 39.36  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884    22 TVPKDLYVVEyGSNMTIECKFPveKQLDLAALIVYW--EMEDKN----IIQFVHGEedlkvQHSSYRQRARLLKDQlSLG 95
Cdd:pfam07686   1 QTPREVTVAL-GGSVTLPCTYS--SSMSEASTSVYWyrQPPGKGptflIAYYSNGS-----EEGVKKGRFSGRGDP-SNG 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 83287884    96 NAALQITDVKLQDAGVYRCMISYGGADY--KRITVKV 130
Cdd:pfam07686  72 DGSLTIQNLTLSDSGTYTCAVIPSGEGVfgKGTRLTV 108
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 152-210 5.67e-04

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.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 37.69  E-value: 5.67e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83287884 152 ELTCQAEGYPKAEVIWTssdhqvLSGKTTTTNSKREEKLFNVTSTLRINTTTNE---IFYCT 210
Cdd:cd00096   2 TLTCSASGNPPPTITWY------KNGKPLPPSSRDSRRSELGNGTLTISNVTLEdsgTYTCV 57
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 33-122 7.93e-04

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409379  Cd Length: 123  Bit Score: 38.73  E-value: 7.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  33 GSNMTIECKFPVEKQLDLAA---LIVYW------EMEDKNIIQFVHGEEDLKVQhSSYRQRARLLKDQLSLGNAALQITD 103
Cdd:cd05714  12 GGNVTLPCKFYRDPTAFGSGihkIRIKWtkltsdSGYLKEVDVLVAMGNVVYHK-KTYGGRVSVPLKPGSDSDASLVITD 90

                        90
                ....*....|....*....
gi 83287884 104 VKLQDAGVYRCMISYGGAD 122
Cdd:cd05714  91 LTASDYGLYRCEVIEGIED 109
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 99-124 7.94e-04

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 38.47  E-value: 7.94e-04
                        10        20
                ....*....|....*....|....*.
gi 83287884  99 LQITDVKLQDAGVYRCMISYGGADYK 124
Cdd:cd00099  75 LTISNLQPEDSGTYYCAVSESGGTDK 100
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 24-119 8.55e-04

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 38.46  E-value: 8.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  24 PKDLYVVEYGSNMTIECKFPVEKQLDLAALI-VYWEMEDKNIIQfvhgEEDLKV-------QHSSYRQRARLLkdQLSLG 95
Cdd:cd05877   3 VQAKVFSHRGGNVTLPCRYHYEPELSAPRKIrVKWTKLEVDYAK----EEDVLVaigtrhkSYGSYQGRVFLR--RADDL 76

                        90       100
                ....*....|....*....|....
gi 83287884  96 NAALQITDVKLQDAGVYRCMISYG 119
Cdd:cd05877  77 DASLVITDLRLEDYGRYRCEVIDG 100
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 21-114 3.13e-03

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 36.66  E-value: 3.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  21 VTVPKDLYVVeYGSNMTIECKFPVEKQLDLAAliVYWEMEDKNIIQFV---HGEEDLKVQhSSYRQRARLLKDQLSLGNA 97
Cdd:cd05718   3 VQVPTEVTGF-LGGSVTLPCSLTSPGTTKITQ--VTWMKIGAGSSQNVavfHPQYGPSVP-NPYAERVEFLAARLGLRNA 78

                        90
                ....*....|....*..
gi 83287884  98 ALQITDVKLQDAGVYRC 114
Cdd:cd05718  79 TLRIRNLRVEDEGNYIC 95
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 33-129 3.34e-03

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 36.66  E-value: 3.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287884  33 GSNMTIECKF---PVEKQ-LDLAALIVYWEMEDKNIIQ------FVHGEEDLK--VQH-SSYRQrarllkdqlslGNAAL 99
Cdd:cd20960  15 GENVTLPCHHqlgLEDQGtLDIEWLLLPSDKVEKVVITysgdrvYNHYYPALKgrVAFtSNDLS-----------GDASL 83

                        90       100       110
                ....*....|....*....|....*....|.
gi 83287884 100 QITDVKLQDAGVYRCMI-SYGGADYKRITVK 129
Cdd:cd20960  84 NISNLKLSDTGTYQCKVkKAPGYAWSKITLI 114
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 89-117 8.16e-03

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.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 34.61  E-value: 8.16e-03
                        10        20
                ....*....|....*....|....*....
gi 83287884  89 KDQLSLGNAALQITDVKLQDAGVYRCMIS 117
Cdd:cd00096  31 SRRSELGNGTLTISNVTLEDSGTYTCVAS 59
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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