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Conserved domains on  [gi|1002341772|ref|NP_001307535|]
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intercellular adhesion molecule 3 isoform 3 [Homo sapiens]

Protein Classification

Ig_2 and Ig domain-containing protein( domain architecture ID 10310089)

protein containing domains Ig, and Ig_2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
40-134 2.72e-46

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 cd05755:

Pssm-ID: 472250  Cd Length: 101  Bit Score: 155.80  E-value: 2.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002341772  40 PERVELAPLPPWQPVGQNFTLRCQVEDGSPRTSLTVVLLRWEEELSRQPAVE-----EPAEVTATVLASRDDHGAPFSCR 114
Cdd:cd05755     2 PERVELTPLPSWQPVGKNFTLRCRVPGGAPRASLTLVLLRGNETLHRETFGGaapapQPAEATFTVLARREDHGANFSCL 81
                          90       100
                  ....*....|....*....|
gi 1002341772 115 TELDMQPQGLGLFVNTSAPR 134
Cdd:cd05755    82 AELDLRPQGLNLFHNHSAPR 101
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1-37 2.32e-18

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 cd20997:

Pssm-ID: 472250  Cd Length: 85  Bit Score: 79.66  E-value: 2.32e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1002341772   1 MGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVY 37
Cdd:cd20997    49 MGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVY 85
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
240-319 1.93e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


:

Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 40.07  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002341772 240 PIVNLSEPTAHEGSTVTVSCMAGAR--VQVTLDGVPAAAPGQPAQLqLNATESDDGRSFFCSATLEVDGEflhRNSSVQL 317
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCSAPGNppPSYTWYKDGSAISSSPNFF-TLSVSAEDSGTYTCVARNGRGGK---VSNPVEL 77

                  ..
gi 1002341772 318 RV 319
Cdd:pfam13895  78 TV 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
343-392 8.05e-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: 38.08  E-value: 8.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002341772 343 VLQCQARGNPYPELRCLKEGSSREVPVGIPFF------------VNVTHNGTYQCQASSSRG 392
Cdd:cd00096     2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRselgngtltisnVTLEDSGTYTCVASNSAG 63
 
Name Accession Description Interval E-value
IgC2_2_ICAM-1_like cd05755
Second immunoglobulin (Ig)-like C2-set domain of intercellular cell adhesion molecule 1 ...
40-134 2.72e-46

Second immunoglobulin (Ig)-like C2-set domain of intercellular cell adhesion molecule 1 (ICAM-1), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of intercellular cell adhesion molecule 1 (ICAM-1; also known as domain of cluster of differentiation (CD) 54) and similar proteins. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. ICAM-1 may be involved in organ targeted tumor metastasis. The interaction of ICAM-1 with leukocyte function-associated antigen-1 (LFA-1) plays a part in leukocyte-endothelial cell recognition. This group also contains ICAM-2 which also interacts with LFA-1. Transmigration of immature dendritic cells across resting endothelium is dependent on the interaction of ICAM-2 with, yet unidentified, ligand(s) on the dendritic cells. ICAM-1 has five Ig-like domains and ICAM-2 has two. ICAM-1 may also act as host receptor for viruses and parasites. The structures of this group show that the second Ig domain lacks a D strand and thus belonging to the C2-set of the IgSF


Pssm-ID: 409413  Cd Length: 101  Bit Score: 155.80  E-value: 2.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002341772  40 PERVELAPLPPWQPVGQNFTLRCQVEDGSPRTSLTVVLLRWEEELSRQPAVE-----EPAEVTATVLASRDDHGAPFSCR 114
Cdd:cd05755     2 PERVELTPLPSWQPVGKNFTLRCRVPGGAPRASLTLVLLRGNETLHRETFGGaapapQPAEATFTVLARREDHGANFSCL 81
                          90       100
                  ....*....|....*....|
gi 1002341772 115 TELDMQPQGLGLFVNTSAPR 134
Cdd:cd05755    82 AELDLRPQGLNLFHNHSAPR 101
IgI_N_ICAM-3 cd20997
N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-3 (Cluster of ...
1-37 2.32e-18

N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-3 (Cluster of Differentiation 50 or CD50); member of the I-set of IgSF domains; The members here are composed of the N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-3 (Cluster of Differentiation 50 or CD50). The intercellular adhesion molecules ICAM-1 (Cluster of Differentiation 54 or CD54), ICAM-2 (Cluster of Differentiation 102 or CD102) and ICAM-3 mediate a variety of critical intercellular adhesion events in the immune system through interactions with their counter-receptors, the beta2-integrins LFA-1 (CD11a/CD18), Mac-1 (CD11b/CD18), p150,95 (CD11c/CD18), and CD11d/CD18. The ICAMs are type I transmembrane glycoproteins belonging to the immunoglobulin superfamily (IgSF). The binding of the ICAM family members with the beta2-integrins physically stabilizes interactions between pairs of T and B cells, T cells and antigen-presenting cells (APCs), and brings effector cells such as cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells into close proximity to their target cells. All three ICAMs share a common polypeptide homology and structural motif, and the ability to bind LFA-1. The distinct functional role of each ICAM is affected by their relative affinities for LFA-1 (ICAM-1 > ICAM-2 > ICAM-3). ICAM-1 is expressed in most tissues at low levels, and expression is increased by inflammatory cytokines. In contrast, ICAM-2 is expressed predominantly on endothelium and leukocytes (except neutrophils), and its expression generally is not responsive to cytokines. ICAM-3 is expressed on leukocytes and Langerhans cells, but not on resting, cytokine-induced endothelium, or nonhematopoietic tissues.


Pssm-ID: 409589  Cd Length: 85  Bit Score: 79.66  E-value: 2.32e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1002341772   1 MGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVY 37
Cdd:cd20997    49 MGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVY 85
ICAM_N pfam03921
Intercellular adhesion molecule (ICAM), N-terminal domain; ICAMs normally functions to promote ...
1-37 1.27e-14

Intercellular adhesion molecule (ICAM), N-terminal domain; ICAMs normally functions to promote intercellular adhesion and signalling. However, The N-terminal domain of the receptor binds to the rhinovirus 'canyon' surrounding the icosahedral 5-fold axes, during the viral attachment process. This family is a family that is part of the Ig superfamily and is therefore related to the family ig (pfam00047).


Pssm-ID: 397829  Cd Length: 86  Bit Score: 69.09  E-value: 1.27e-14
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1002341772   1 MGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVY 37
Cdd:pfam03921  50 QGWKAFELSNVSEDSVPLCHFNCSGKQSSASSNITVY 86
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
240-319 1.93e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 40.07  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002341772 240 PIVNLSEPTAHEGSTVTVSCMAGAR--VQVTLDGVPAAAPGQPAQLqLNATESDDGRSFFCSATLEVDGEflhRNSSVQL 317
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCSAPGNppPSYTWYKDGSAISSSPNFF-TLSVSAEDSGTYTCVARNGRGGK---VSNPVEL 77

                  ..
gi 1002341772 318 RV 319
Cdd:pfam13895  78 TV 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
343-392 8.05e-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: 38.08  E-value: 8.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002341772 343 VLQCQARGNPYPELRCLKEGSSREVPVGIPFF------------VNVTHNGTYQCQASSSRG 392
Cdd:cd00096     2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRselgngtltisnVTLEDSGTYTCVASNSAG 63
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
40-114 7.65e-03

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 35.86  E-value: 7.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002341772  40 PERVELAPLPPWQpvGQNFTLRCQVEDGSPRTSLTvvllrWEEELSRQPAVEEPAEV-----------TATVLASRDDHG 108
Cdd:pfam08205   1 PTIEPPASLLEGE--GPEVVATCSSAGGKPAPRIT-----WYLDGKPLEAAETSSEQdpesglvtvtsELKLVPSRSDHG 73

                  ....*.
gi 1002341772 109 APFSCR 114
Cdd:pfam08205  74 QSLTCQ 79
 
Name Accession Description Interval E-value
IgC2_2_ICAM-1_like cd05755
Second immunoglobulin (Ig)-like C2-set domain of intercellular cell adhesion molecule 1 ...
40-134 2.72e-46

Second immunoglobulin (Ig)-like C2-set domain of intercellular cell adhesion molecule 1 (ICAM-1), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of intercellular cell adhesion molecule 1 (ICAM-1; also known as domain of cluster of differentiation (CD) 54) and similar proteins. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. ICAM-1 may be involved in organ targeted tumor metastasis. The interaction of ICAM-1 with leukocyte function-associated antigen-1 (LFA-1) plays a part in leukocyte-endothelial cell recognition. This group also contains ICAM-2 which also interacts with LFA-1. Transmigration of immature dendritic cells across resting endothelium is dependent on the interaction of ICAM-2 with, yet unidentified, ligand(s) on the dendritic cells. ICAM-1 has five Ig-like domains and ICAM-2 has two. ICAM-1 may also act as host receptor for viruses and parasites. The structures of this group show that the second Ig domain lacks a D strand and thus belonging to the C2-set of the IgSF


Pssm-ID: 409413  Cd Length: 101  Bit Score: 155.80  E-value: 2.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002341772  40 PERVELAPLPPWQPVGQNFTLRCQVEDGSPRTSLTVVLLRWEEELSRQPAVE-----EPAEVTATVLASRDDHGAPFSCR 114
Cdd:cd05755     2 PERVELTPLPSWQPVGKNFTLRCRVPGGAPRASLTLVLLRGNETLHRETFGGaapapQPAEATFTVLARREDHGANFSCL 81
                          90       100
                  ....*....|....*....|
gi 1002341772 115 TELDMQPQGLGLFVNTSAPR 134
Cdd:cd05755    82 AELDLRPQGLNLFHNHSAPR 101
IgI_N_ICAM-3 cd20997
N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-3 (Cluster of ...
1-37 2.32e-18

N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-3 (Cluster of Differentiation 50 or CD50); member of the I-set of IgSF domains; The members here are composed of the N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-3 (Cluster of Differentiation 50 or CD50). The intercellular adhesion molecules ICAM-1 (Cluster of Differentiation 54 or CD54), ICAM-2 (Cluster of Differentiation 102 or CD102) and ICAM-3 mediate a variety of critical intercellular adhesion events in the immune system through interactions with their counter-receptors, the beta2-integrins LFA-1 (CD11a/CD18), Mac-1 (CD11b/CD18), p150,95 (CD11c/CD18), and CD11d/CD18. The ICAMs are type I transmembrane glycoproteins belonging to the immunoglobulin superfamily (IgSF). The binding of the ICAM family members with the beta2-integrins physically stabilizes interactions between pairs of T and B cells, T cells and antigen-presenting cells (APCs), and brings effector cells such as cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells into close proximity to their target cells. All three ICAMs share a common polypeptide homology and structural motif, and the ability to bind LFA-1. The distinct functional role of each ICAM is affected by their relative affinities for LFA-1 (ICAM-1 > ICAM-2 > ICAM-3). ICAM-1 is expressed in most tissues at low levels, and expression is increased by inflammatory cytokines. In contrast, ICAM-2 is expressed predominantly on endothelium and leukocytes (except neutrophils), and its expression generally is not responsive to cytokines. ICAM-3 is expressed on leukocytes and Langerhans cells, but not on resting, cytokine-induced endothelium, or nonhematopoietic tissues.


Pssm-ID: 409589  Cd Length: 85  Bit Score: 79.66  E-value: 2.32e-18
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1002341772   1 MGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVY 37
Cdd:cd20997    49 MGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVY 85
ICAM_N pfam03921
Intercellular adhesion molecule (ICAM), N-terminal domain; ICAMs normally functions to promote ...
1-37 1.27e-14

Intercellular adhesion molecule (ICAM), N-terminal domain; ICAMs normally functions to promote intercellular adhesion and signalling. However, The N-terminal domain of the receptor binds to the rhinovirus 'canyon' surrounding the icosahedral 5-fold axes, during the viral attachment process. This family is a family that is part of the Ig superfamily and is therefore related to the family ig (pfam00047).


Pssm-ID: 397829  Cd Length: 86  Bit Score: 69.09  E-value: 1.27e-14
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1002341772   1 MGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVY 37
Cdd:pfam03921  50 QGWKAFELSNVSEDSVPLCHFNCSGKQSSASSNITVY 86
IgI_N_ICAM1-2-3 cd20944
N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-1 (Cluster of ...
1-37 1.46e-14

N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-1 (Cluster of Differentiation 54 or CD54), ICAM-2 (CD102) and ICAM-3 (CD50); members of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain found in the N-terminus of the intercellular adhesion molecules ICAM-1 (Cluster of Differentiation 54 or CD54), ICAM-2 (CD102), and ICAM-3 (CD50). ICAM-1, ICAM-2, and ICAM-3 mediate a variety of critical intercellular adhesion events in the immune system through interactions with their counter-receptors, the beta2-integrins LFA-1 (CD11a/CD18), Mac-1 (CD11b/CD18), p150,95 (CD11c/CD18), and CD11d/CD18. The ICAMs are type I transmembrane glycoproteins belonging to the immunoglobulin superfamily (IgSF). The binding of the ICAM family members with the beta2-integrins physically stabilizes interactions between pairs of T and B cells, T cells and antigen-presenting cells (APCs), and brings effector cells such as cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells into close proximity to their target cells. All three ICAMs share a common polypeptide homology and structural motif, and the ability to bind LFA-1. The distinct functional role of each ICAM is affected by their relative affinities for LFA-1 (ICAM-1 > ICAM-2 > ICAM-3). ICAM-1 is expressed in most tissues at low levels, and expression is increased by inflammatory cytokines. In contrast, ICAM-2 is expressed predominantly on endothelium and leukocytes (except neutrophils), and its expression generally is not responsive to cytokines. ICAM-3 is expressed on leukocytes and Langerhans cells, but not on resting, cytokine-induced endothelium, or nonhematopoietic tissues.


Pssm-ID: 409537  Cd Length: 81  Bit Score: 68.80  E-value: 1.46e-14
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1002341772   1 MGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVY 37
Cdd:cd20944    45 GNWKVYELSNVQEDSQPMCYSNCPGGQSTAKSNLTVY 81
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
240-319 1.93e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 40.07  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002341772 240 PIVNLSEPTAHEGSTVTVSCMAGAR--VQVTLDGVPAAAPGQPAQLqLNATESDDGRSFFCSATLEVDGEflhRNSSVQL 317
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCSAPGNppPSYTWYKDGSAISSSPNFF-TLSVSAEDSGTYTCVARNGRGGK---VSNPVEL 77

                  ..
gi 1002341772 318 RV 319
Cdd:pfam13895  78 TV 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
343-392 8.05e-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: 38.08  E-value: 8.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002341772 343 VLQCQARGNPYPELRCLKEGSSREVPVGIPFF------------VNVTHNGTYQCQASSSRG 392
Cdd:cd00096     2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRselgngtltisnVTLEDSGTYTCVASNSAG 63
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
344-392 1.68e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 37.92  E-value: 1.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002341772 344 LQCQARGNPYPELRCLKEGSSRE------------VPVGIPFFVNVTHN-------GTYQCQASSSRG 392
Cdd:cd07693    20 LNCKAEGRPTPTIQWLKNGQPLEtdkddprshrivLPSGSLFFLRVVHGrkgrsdeGVYVCVAHNSLG 87
IgI_N_ICAM-1 cd20996
N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-1 (Cluster of ...
3-37 2.75e-03

N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-1 (Cluster of Differentiation 54 or CD54); member of the I-set of IgSF domains; The members here are composed of the N-terminal immunoglobulin domain of the intercellular adhesion molecules ICAM-1 (Cluster of Differentiation 54 or CD54). The intercellular adhesion molecules ICAM-1, ICAM-2 (Cluster of Differentiation 102 or CD102) and ICAM-3 (Cluster of Differentiation 50 or CD50) mediate a variety of critical intercellular adhesion events in the immune system through interactions with their counter-receptors, the beta2-integrins LFA-1 (CD11a/CD18), Mac-1 (CD11b/CD18), p150,95 (CD11c/CD18), and CD11d/CD18. The ICAMs are type I transmembrane glycoproteins belonging to the immunoglobulin superfamily (IgSF). The binding of the ICAM family members with the beta2-integrins physically stabilizes interactions between pairs of T and B cells, T cells and antigen-presenting cells (APCs), and brings effector cells such as cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells into close proximity to their target cells. All three ICAMs share a common polypeptide homology and structural motif, and the ability to bind LFA-1. The distinct functional role of each ICAM is affected by their relative affinities for LFA-1 (ICAM-1 > ICAM-2 > ICAM-3). ICAM-1 is expressed in most tissues at low levels, and expression is increased by inflammatory cytokines. In contrast, ICAM-2 is expressed predominantly on endothelium and leukocytes (except neutrophils), and its expression generally is not responsive to cytokines. ICAM-3 is expressed on leukocytes and Langerhans cells, but not on resting, cytokine-induced endothelium, or nonhematopoietic tissues.


Pssm-ID: 409588  Cd Length: 82  Bit Score: 36.75  E-value: 2.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1002341772   3 WAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVY 37
Cdd:cd20996    48 WKVFELSNVQEDSQPMCYSNCPDGQSSASTFLTVY 82
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
40-114 7.65e-03

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 35.86  E-value: 7.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002341772  40 PERVELAPLPPWQpvGQNFTLRCQVEDGSPRTSLTvvllrWEEELSRQPAVEEPAEV-----------TATVLASRDDHG 108
Cdd:pfam08205   1 PTIEPPASLLEGE--GPEVVATCSSAGGKPAPRIT-----WYLDGKPLEAAETSSEQdpesglvtvtsELKLVPSRSDHG 73

                  ....*.
gi 1002341772 109 APFSCR 114
Cdd:pfam08205  74 QSLTCQ 79
 
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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