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Conserved domains on  [gi|767910105|ref|XP_011508155|]
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hyaluronan and proteoglycan link protein 2 isoform X1 [Homo sapiens]

Protein Classification

Link_domain_HAPLN_module_1 and Link_domain_HAPLN_module_2 domain-containing protein( domain architecture ID 10308845)

protein containing domains Ig, Link_domain_HAPLN_module_1, and Link_domain_HAPLN_module_2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 148-241 1.83e-60

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239595  Cd Length: 95  Bit Score: 188.79  E-value: 1.83e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 148 VVFPYQPSRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGRGR-PGIRSY 226
Cdd:cd03518    1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTvPGLRSY 80

                         90
                 ....*....|....*
gi 767910105 227 GPRDRMRDRYDAFCF 241
Cdd:cd03518   81 GERDKMLSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 250-337 4.59e-49

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239596  Cd Length: 91  Bit Score: 159.51  E-value: 4.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 250 FFVPGRLTLSEAHAACRRRGAVVAKVGHLYAAWKFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPdPGVRSFGFPRPQQ 329
Cdd:cd03519    5 LLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLE-PGVRSFGFPDKKH 83


                 ....*...
gi 767910105 330 AAYGTYCY 337
Cdd:cd03519   84 KLYGVYCY 91
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 45-150 6.97e-43

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 cd05877:

Pssm-ID: 472250  Cd Length: 117  Bit Score: 144.39  E-value: 6.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  45 IHSHRGATATLPCVL-----GTTPPSYKVRWSKVEPGELRETLILITNGLHARGYGPLGGRARMRRGHRLDASLVIAGVR 119
Cdd:cd05877    7 VFSHRGGNVTLPCRYhyepeLSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDASLVITDLR 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767910105 120 LEDEGRYRCELINGIEDESVALTLSLEGVVF 150
Cdd:cd05877   87 LEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
 
Name Accession Description Interval E-value
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 148-241 1.83e-60

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239595  Cd Length: 95  Bit Score: 188.79  E-value: 1.83e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 148 VVFPYQPSRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGRGR-PGIRSY 226
Cdd:cd03518    1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTvPGLRSY 80

                         90
                 ....*....|....*
gi 767910105 227 GPRDRMRDRYDAFCF 241
Cdd:cd03518   81 GERDKMLSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 250-337 4.59e-49

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 159.51  E-value: 4.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 250 FFVPGRLTLSEAHAACRRRGAVVAKVGHLYAAWKFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPdPGVRSFGFPRPQQ 329
Cdd:cd03519    5 LLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLE-PGVRSFGFPDKKH 83


                 ....*...
gi 767910105 330 AAYGTYCY 337
Cdd:cd03519   84 KLYGVYCY 91
Xlink pfam00193
Extracellular link domain;
148-241 4.25e-43

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 143.87  E-value: 4.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  148 VVFPYQpSRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGrGRPGIRSYG 227
Cdd:pfam00193   1 GVFHLE-SPGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGG-NMPGVRQYG 78

                          90
                  ....*....|....
gi 767910105  228 PRDRMRDRYDAFCF 241
Cdd:pfam00193  79 FRDPLSERYDAYCY 92
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 45-150 6.97e-43

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: 144.39  E-value: 6.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  45 IHSHRGATATLPCVL-----GTTPPSYKVRWSKVEPGELRETLILITNGLHARGYGPLGGRARMRRGHRLDASLVIAGVR 119
Cdd:cd05877    7 VFSHRGGNVTLPCRYhyepeLSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDASLVITDLR 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767910105 120 LEDEGRYRCELINGIEDESVALTLSLEGVVF 150
Cdd:cd05877   87 LEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
LINK smart00445
Link (Hyaluronan-binding);
146-242 1.07e-34

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 122.07  E-value: 1.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105   146 EGVVFPYQPsRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGrGRPGIRS 225
Cdd:smart00445   1 DGGVFHVEK-NGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG-NLPGVRQ 78

                           90
                   ....*....|....*..
gi 767910105   226 YGPRDRmRDRYDAFCFT 242
Cdd:smart00445  79 YGFPDP-TSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
249-337 1.62e-33

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 119.21  E-value: 1.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  249 VFFVPGR----LTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSFGF 324
Cdd:pfam00193   2 VFHLESPgrykLTFQEAQAACAALGATLATPEQLYAAWK-AGLDTCDAGWLADGTVRYPITTPRPNCGG-NMPGVRQYGF 79

                          90
                  ....*....|...
gi 767910105  325 PRPQQAAYGTYCY 337
Cdd:pfam00193  80 RDPLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
247-338 7.06e-31

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 112.05  E-value: 7.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105   247 GQVFFV----PGRLTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSF 322
Cdd:smart00445   2 GGVFHVekngRYKLTFAEAREACRAQGATLATVGQLYAAWQ-DGFDTCDAGWLADGSVRYPIITPRPRCGG-NLPGVRQY 79

                           90
                   ....*....|....*.
gi 767910105   323 GFPRPqQAAYGTYCYA 338
Cdd:smart00445  80 GFPDP-TSRYDAYCFN 94
IGv smart00406
Immunoglobulin V-Type;
52-129 2.39e-09

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 53.54  E-value: 2.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105    52 TATLPC-VLGTTPPSYKVRWSKVEPGELREtlILITNGLHARGYGPLGGRARM---RRGHRLDASLVIAGVRLEDEGRYR 127
Cdd:smart00406   1 SVTLSCkFSGSTFSSYYVSWVRQPPGKGLE--WLGYIGSNGSSYYQESYKGRFtisKDTSKNDVSLTISNLRVEDTGTYY 78


                   ..
gi 767910105   128 CE 129
Cdd:smart00406  79 CA 80
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 43-132 1.10e-07

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: 49.38  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105   43 EVIHSHRGATATLPCVL--GTTPPSYKVRWSKVEPGELRETLILITNglhaRGYGPLGGRARMR-RGH--RLDASLVIAG 117
Cdd:pfam07686   4 REVTVALGGSVTLPCTYssSMSEASTSVYWYRQPPGKGPTFLIAYYS----NGSEEGVKKGRFSgRGDpsNGDGSLTIQN 79

                          90
                  ....*....|....*
gi 767910105  118 VRLEDEGRYRCELIN 132
Cdd:pfam07686  80 LTLSDSGTYTCAVIP 94
 
Name Accession Description Interval E-value
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 148-241 1.83e-60

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239595  Cd Length: 95  Bit Score: 188.79  E-value: 1.83e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 148 VVFPYQPSRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGRGR-PGIRSY 226
Cdd:cd03518    1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTvPGLRSY 80

                         90
                 ....*....|....*
gi 767910105 227 GPRDRMRDRYDAFCF 241
Cdd:cd03518   81 GERDKMLSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 250-337 4.59e-49

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 159.51  E-value: 4.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 250 FFVPGRLTLSEAHAACRRRGAVVAKVGHLYAAWKFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPdPGVRSFGFPRPQQ 329
Cdd:cd03519    5 LLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLE-PGVRSFGFPDKKH 83


                 ....*...
gi 767910105 330 AAYGTYCY 337
Cdd:cd03519   84 KLYGVYCY 91
Xlink pfam00193
Extracellular link domain;
148-241 4.25e-43

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 143.87  E-value: 4.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  148 VVFPYQpSRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGrGRPGIRSYG 227
Cdd:pfam00193   1 GVFHLE-SPGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGG-NMPGVRQYG 78

                          90
                  ....*....|....
gi 767910105  228 PRDRMRDRYDAFCF 241
Cdd:pfam00193  79 FRDPLSERYDAYCY 92
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 45-150 6.97e-43

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: 144.39  E-value: 6.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  45 IHSHRGATATLPCVL-----GTTPPSYKVRWSKVEPGELRETLILITNGLHARGYGPLGGRARMRRGHRLDASLVIAGVR 119
Cdd:cd05877    7 VFSHRGGNVTLPCRYhyepeLSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDASLVITDLR 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767910105 120 LEDEGRYRCELINGIEDESVALTLSLEGVVF 150
Cdd:cd05877   87 LEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 148-241 9.20e-42

The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It is found in the CD44 receptor and in human TSG-6. TSG-6 is the protein product of the tumor necrosis factor-stimulated gene-6. TSG-6 has a strong anti-inflammatory effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. This group also contains the link domains of the chondroitin sulfate proteoglycan core proteins (CSPG) including aggrecan, versican, neurocan, and brevican and the link domains of the vertebrate HAPLN (HA and proteoglycan binding link) protein family. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates in which other CSPGs substitute for aggregan might contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN gene family are physically linked adjacent to CSPG genes. TSG-6 contains a single link module which supports high affinity binding with HA. The functional HA-binding domain of CD44 is an extended domain comprised of a link module flanked with N-and C- extensions. These extensions are essential for folding and functional activity. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of the CSPG aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) which contains link modules 3 and 4 which lack HA-binding activity. HAPLNs contain two contiguous link modules.


Pssm-ID: 238534  Cd Length: 92  Bit Score: 140.63  E-value: 9.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 148 VVFPYQPSRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGRgRPGIRSYG 227
Cdd:cd01102    1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGR-NPGVRSYG 79

                         90
                 ....*....|....
gi 767910105 228 PRDrMRDRYDAFCF 241
Cdd:cd01102   80 NPA-PSGRYDAYCF 92
LINK smart00445
Link (Hyaluronan-binding);
146-242 1.07e-34

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 122.07  E-value: 1.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105   146 EGVVFPYQPsRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGrGRPGIRS 225
Cdd:smart00445   1 DGGVFHVEK-NGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG-NLPGVRQ 78

                           90
                   ....*....|....*..
gi 767910105   226 YGPRDRmRDRYDAFCFT 242
Cdd:smart00445  79 YGFPDP-TSRYDAYCFN 94
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 248-337 7.63e-34

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan 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: 239597  Cd Length: 96  Bit Score: 120.11  E-value: 7.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 248 QVFFV--PGRLTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSF--- 322
Cdd:cd03520    1 EVFYAtaPEKFTFQEARAECRSLGAVLATTGQLYAAWR-QGLDQCDPGWLADGSVRYPISTPRPQCGG-GLPGVRTLyrf 78

                         90
                 ....*....|....*....
gi 767910105 323 ----GFPRPqQAAYGTYCY 337
Cdd:cd03520   79 pnqtGFPDP-HSRFDAYCF 96
Xlink pfam00193
Extracellular link domain;
249-337 1.62e-33

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 119.21  E-value: 1.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  249 VFFVPGR----LTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSFGF 324
Cdd:pfam00193   2 VFHLESPgrykLTFQEAQAACAALGATLATPEQLYAAWK-AGLDTCDAGWLADGTVRYPITTPRPNCGG-NMPGVRQYGF 79

                          90
                  ....*....|...
gi 767910105  325 PRPQQAAYGTYCY 337
Cdd:pfam00193  80 RDPLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
247-338 7.06e-31

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 112.05  E-value: 7.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105   247 GQVFFV----PGRLTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSF 322
Cdd:smart00445   2 GGVFHVekngRYKLTFAEAREACRAQGATLATVGQLYAAWQ-DGFDTCDAGWLADGSVRYPIITPRPRCGG-NLPGVRQY 79

                           90
                   ....*....|....*.
gi 767910105   323 GFPRPqQAAYGTYCYA 338
Cdd:smart00445  80 GFPDP-TSRYDAYCFN 94
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 256-337 1.02e-26

The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It is found in the CD44 receptor and in human TSG-6. TSG-6 is the protein product of the tumor necrosis factor-stimulated gene-6. TSG-6 has a strong anti-inflammatory effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. This group also contains the link domains of the chondroitin sulfate proteoglycan core proteins (CSPG) including aggrecan, versican, neurocan, and brevican and the link domains of the vertebrate HAPLN (HA and proteoglycan binding link) protein family. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates in which other CSPGs substitute for aggregan might contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN gene family are physically linked adjacent to CSPG genes. TSG-6 contains a single link module which supports high affinity binding with HA. The functional HA-binding domain of CD44 is an extended domain comprised of a link module flanked with N-and C- extensions. These extensions are essential for folding and functional activity. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of the CSPG aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) which contains link modules 3 and 4 which lack HA-binding activity. HAPLNs contain two contiguous link modules.


Pssm-ID: 238534  Cd Length: 92  Bit Score: 101.34  E-value: 1.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 256 LTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSFGFPRPQQaAYGTY 335
Cdd:cd01102   14 LTFAEAALACKARGAHLATPGQLEAAWQ-DGFDVCTAGWLADGSVRYPIVTSRPNCGG-RNPGVRSYGNPAPSG-RYDAY 90


                 ..
gi 767910105 336 CY 337
Cdd:cd01102   91 CF 92
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 148-241 9.24e-25

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with 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: 239594  Cd Length: 95  Bit Score: 95.94  E-value: 9.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 148 VVFPYQPSRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGG--RGRPGIRS 225
Cdd:cd03517    1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGdmDGFPGVRN 80

                         90
                 ....*....|....*.
gi 767910105 226 YGPRDrMRDRYDAFCF 241
Cdd:cd03517   81 YGVRD-PDELYDVYCY 95
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 149-241 1.35e-24

This is the extracellular link domain of the type found in human TSG-6. The link domain is a hyaluronan (HA)-binding domain. TSG-6 is the protein product of tumor necrosis factor-stimulated gene-6. TSG-6 is up-regulated in inflammatory lesions and in the ovary during ovulation. It has a strong anti-inflammatory and chondroprotective effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. Also included in this group are the stabilins: stabilin-1 (FEEL-1, CLEVER-1) and stabilin-2 (FEEL-2). Stabilin-2 functions as the major liver and lymph node-scavenging receptor for HA and related glycosaminoglycans. Stabilin-2 is a scavenger receptor with a broad range of ligands including advanced glycation end (AGE) products, acetylated low density lipoprotein and procollagen peptides. In contrast, stabilin-1 does not bind HA, but binds acetylated low density lipoprotein and AGEs with lower affinity. As AGEs accumulate in vascular tissues during aging and diabetes, these receptors may be implicated in the pathologies of these states. Both stabilins are present in the early endocytic pathway in hepatic sinusoidal epithelium associating with clathrin/AP-2. Stabilin-1 is expressed in macrophages. Stabilin-2 is absent from the latter. In macrophages: stabilin-1 is involved in trafficking between early/sorting endosomes and the trans-Golgi network. Stabilin-1 has also been implicated in angiogenesis and possibly leucocyte trafficking. Both stabilins bind gram-positive and gram-negative bacteria. TSG-6 and stabilins contain a single link module which supports high affinity binding to HA.


Pssm-ID: 239592  Cd Length: 93  Bit Score: 95.61  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 149 VFPYQPSRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGrGRPGIRSYGP 228
Cdd:cd03515    2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGF-GHVGIVDYGP 80

                         90
                 ....*....|...
gi 767910105 229 RDRMRDRYDAFCF 241
Cdd:cd03515   81 RLNLSERWDAYCY 93
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 160-241 1.97e-24

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan 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: 239597  Cd Length: 96  Bit Score: 95.07  E-value: 1.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 160 QFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGrGRPGIRS-YGPRDRM-----R 233
Cdd:cd03520   10 KFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGG-GLPGVRTlYRFPNQTgfpdpH 88


                 ....*...
gi 767910105 234 DRYDAFCF 241
Cdd:cd03520   89 SRFDAYCF 96
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 256-337 4.03e-21

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with 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: 239594  Cd Length: 95  Bit Score: 86.31  E-value: 4.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 256 LTLSEAHAACRRRGAVVAKVGHLYAAWkFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPD--PGVRSFGfPRPQQAAYG 333
Cdd:cd03517   14 LTFPRAQRACLDISAQIATPEQLLAAY-EDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDgfPGVRNYG-VRDPDELYD 91


                 ....
gi 767910105 334 TYCY 337
Cdd:cd03517   92 VYCY 95
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 45-150 2.18e-20

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: 85.34  E-value: 2.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  45 IHSHRGATATLPCVLGTTPPSY-------KVRWSKVE--PGELRETLILITNGLHARGYGPLGGRARM--RRGHRLDASL 113
Cdd:cd05714    7 VFSHLGGNVTLPCKFYRDPTAFgsgihkiRIKWTKLTsdSGYLKEVDVLVAMGNVVYHKKTYGGRVSVplKPGSDSDASL 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767910105 114 VIAGVRLEDEGRYRCELINGIEDESVALTLSLEGVVF 150
Cdd:cd05714   87 VITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 147-241 4.20e-20

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 83.63  E-value: 4.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 147 GVVFPYQPSRgryqFNYYEAKQACEEQDGRLATYSQLYQAWT-EGLDWCNAGWLLEGSVRYPVLTARAPCGGRgRPGIRS 225
Cdd:cd03519    1 GVFYLLHPGK----LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPL-EPGVRS 75

                         90
                 ....*....|....*.
gi 767910105 226 YGPRDRMRDRYDAFCF 241
Cdd:cd03519   76 FGFPDKKHKLYGVYCY 91
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 45-150 2.90e-12

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. 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, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. 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: 409482  Cd Length: 128  Bit Score: 63.06  E-value: 2.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  45 IHSHRGATATLPC---VLGTTPPSY-------KVRWSKVEPG----ELRETLILIT-NGLHARGYGPLGGRARMRRGHRL 109
Cdd:cd05901    7 VHGSLSGSVVLPCrfsTLPTLPPSYnitseflRIKWTKIQVDkngkDHKETTVLVAqNGIIKIGQEYMGRVSVPSHPEDQ 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767910105 110 -DASLVIAGVRLEDEGRYRCELINGIEDESVALTLSLEGVVF 150
Cdd:cd05901   87 gDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 50-150 6.79e-12

Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core protein (CSPG); The members here are composed of the immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core proteins (CSPGs). Included in this group are the Ig domains of other CSPGs: 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. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409462  Cd Length: 125  Bit Score: 61.87  E-value: 6.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  50 GATATLPCVLGTTP---PSY------KVRWSKVE--PGELRETLILITNGLHARGYGPLGGRARM-----RRGhrlDASL 113
Cdd:cd05878   12 GTSVTLPCYFIDPPhpvTPStaplapRIKWSKVSvdGKKEKEVVLLVATEGRVRVNSAYQGRVSLpnypaIPS---DATL 88

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767910105 114 VIAGVRLEDEGRYRCELINGIEDESVALTLSLEGVVF 150
Cdd:cd05878   89 EVQSLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF 125
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 52-150 2.56e-11

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. 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, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Unlike aggrecan which is widely distributed 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. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409483  Cd Length: 121  Bit Score: 60.23  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  52 TATLPCVLgTTPPSY-------KVRWSKVEPGELRETL-ILITNGLHARGYGPLGGRARM--RRGHRLDASLVIAGVRLE 121
Cdd:cd05902   14 SVLLPCVF-TLPPSAssppegpRIKWTKLSTSGGQQQRpVLVARDNVVRVAKAFQGRVSLpgYPKNRYNASLVLSRLRYS 92

                         90       100
                 ....*....|....*....|....*....
gi 767910105 122 DEGRYRCELINGIEDESVALTLSLEGVVF 150
Cdd:cd05902   93 DSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 34-150 2.92e-10

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: 57.26  E-value: 2.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  34 PHYLLPPIHEVihshrgatatlPCVLGTTPPSYKVRWSKVEPGelRETLILITNGlhargygplgGRARMRRGHR----- 108
Cdd:cd05900   18 PCYFQDPIAKD-----------PGAPTVAPLSPRIKWSFISKE--KESVLLVATE----------GKVRVNTEYLdrvsl 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767910105 109 -------LDASLVIAGVRLEDEGRYRCELINGIEDESVALTLSLEGVVF 150
Cdd:cd05900   75 pnypaipSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 255-337 6.96e-10

This is the extracellular link domain of the type found in human TSG-6. The link domain is a hyaluronan (HA)-binding domain. TSG-6 is the protein product of tumor necrosis factor-stimulated gene-6. TSG-6 is up-regulated in inflammatory lesions and in the ovary during ovulation. It has a strong anti-inflammatory and chondroprotective effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. Also included in this group are the stabilins: stabilin-1 (FEEL-1, CLEVER-1) and stabilin-2 (FEEL-2). Stabilin-2 functions as the major liver and lymph node-scavenging receptor for HA and related glycosaminoglycans. Stabilin-2 is a scavenger receptor with a broad range of ligands including advanced glycation end (AGE) products, acetylated low density lipoprotein and procollagen peptides. In contrast, stabilin-1 does not bind HA, but binds acetylated low density lipoprotein and AGEs with lower affinity. As AGEs accumulate in vascular tissues during aging and diabetes, these receptors may be implicated in the pathologies of these states. Both stabilins are present in the early endocytic pathway in hepatic sinusoidal epithelium associating with clathrin/AP-2. Stabilin-1 is expressed in macrophages. Stabilin-2 is absent from the latter. In macrophages: stabilin-1 is involved in trafficking between early/sorting endosomes and the trans-Golgi network. Stabilin-1 has also been implicated in angiogenesis and possibly leucocyte trafficking. Both stabilins bind gram-positive and gram-negative bacteria. TSG-6 and stabilins contain a single link module which supports high affinity binding to HA.


Pssm-ID: 239592  Cd Length: 93  Bit Score: 55.16  E-value: 6.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 255 RLTLSEAHAACRRRGAVVAKVGHLYAAWKFsGLDQCDGGWLADGSVRFPITTPRPRCgGLPDPGVRSFGFPRPQQAAYGT 334
Cdd:cd03515   13 KLTYTEAKAACEAEGAHLATYSQLSAAQQL-GFHLCAAGWLAKGRVGYPIVFPSANC-GFGHVGIVDYGPRLNLSERWDA 90


                 ...
gi 767910105 335 YCY 337
Cdd:cd03515   91 YCY 93
IGv smart00406
Immunoglobulin V-Type;
52-129 2.39e-09

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 53.54  E-value: 2.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105    52 TATLPC-VLGTTPPSYKVRWSKVEPGELREtlILITNGLHARGYGPLGGRARM---RRGHRLDASLVIAGVRLEDEGRYR 127
Cdd:smart00406   1 SVTLSCkFSGSTFSSYYVSWVRQPPGKGLE--WLGYIGSNGSSYYQESYKGRFtisKDTSKNDVSLTISNLRVEDTGTYY 78


                   ..
gi 767910105   128 CE 129
Cdd:smart00406  79 CA 80
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 157-243 5.16e-08

This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It also plays an important role in arteriogenesis. The functional HA-binding domain of CD44 is an extended domain comprised of a single link module flanked with N-and C- extensions. These extensions are essential for folding and for functional activity. This group also contains the cell surface retention sequence (CRS) binding protein-1 (CRSBP-1) and lymph vessel endothelial receptor-1 (LYVE-1). CRSBP-1 is a cell surface binding protein for the CRS motif of PDGF-BB (platelet-derived growth factor-BB) and is responsible for the cell surface retention of PDGF-BB in SSV-transformed cells. CRSBP-1 may play a role in autocrine regulation of cell growth mediated by CRS containing growth regulators. LYVE-1 is preferentially expressed on the lymphatic endothelium and is used as a molecular marker for the detection and characterization of lymphatic vessels in tumors.


Pssm-ID: 239593  Cd Length: 144  Bit Score: 51.31  E-value: 5.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 157 GRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGRGRpGIrsYGPRDRMRDRY 236
Cdd:cd03516   15 GRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNGT-GV--YILNSNLSSRY 91


                 ....*..
gi 767910105 237 DAFCFTS 243
Cdd:cd03516   92 DAYCYNS 98
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 43-132 1.10e-07

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: 49.38  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105   43 EVIHSHRGATATLPCVL--GTTPPSYKVRWSKVEPGELRETLILITNglhaRGYGPLGGRARMR-RGH--RLDASLVIAG 117
Cdd:pfam07686   4 REVTVALGGSVTLPCTYssSMSEASTSVYWYRQPPGKGPTFLIAYYS----NGSEEGVKKGRFSgRGDpsNGDGSLTIQN 79

                          90
                  ....*....|....*
gi 767910105  118 VRLEDEGRYRCELIN 132
Cdd:pfam07686  80 LTLSDSGTYTCAVIP 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 50-144 5.85e-07

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: 46.73  E-value: 5.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105    50 GATATLPCVLgTTPPSYKVRWSKVEPGELREtlilitnglhargygplGGRARMRRGHRlDASLVIAGVRLEDEGRYRCE 129
Cdd:smart00410   9 GESVTLSCEA-SGSPPPEVTWYKQGGKLLAE-----------------SGRFSVSRSGS-TSTLTISNVTPEDSGTYTCA 69

                           90
                   ....*....|....*
gi 767910105   130 LINGIEDESVALTLS 144
Cdd:smart00410  70 ATNSSGSASSGTTLT 84
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 49-128 6.43e-05

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: 41.55  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  49 RGATATLPCVLGTTPPSYKVRWSKVEPGELRETLILITNGLHARGYGPlGGRARMRRGHRLDASLVIAGVRLEDEGRYRC 128
Cdd:cd00099   12 EGESVTLSCEVSSSFSSTYIYWYRQKPGQGPEFLIYLSSSKGKTKGGV-PGRFSGSRDGTSSFSLTISNLQPEDSGTYYC 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 53-140 9.36e-05

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: 40.01  E-value: 9.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  53 ATLPCVLgTTPPSYKVRWSKvepgelretlilitNGlhargyGPLGGRARMRRGHRL-DASLVIAGVRLEDEGRYRCELI 131
Cdd:cd00096    1 VTLTCSA-SGNPPPTITWYK--------------NG------KPLPPSSRDSRRSELgNGTLTISNVTLEDSGTYTCVAS 59


                 ....*....
gi 767910105 132 NGIEDESVA 140
Cdd:cd00096   60 NSAGGSASA 68
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 50-132 2.61e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.09  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105   50 GATATLPC-VLGTTPPSYkvRWSKvepgelretlilitNGLHargygPLGGRARMRRGHRLDASLVIAGVRLEDEGRYRC 128
Cdd:pfam13927  16 GETVTLTCeATGSPPPTI--TWYK--------------NGEP-----ISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTC 74


                  ....
gi 767910105  129 ELIN 132
Cdd:pfam13927  75 VASN 78
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 50-130 4.18e-04

Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409373  Cd Length: 105  Bit Score: 39.37  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  50 GATATLPCVL-GTTPPSYKVRWSKVEPGELRETLILITN----GLHARGYGPLGGRarmrrghrlDASLVIAGVRLEDEG 124
Cdd:cd04984   13 GETVTITCTGsSGNISGNYVNWYQQKPGSAPRYLIYEDKhrpsGIPDRFSGSKSGN---------TASLTISGAQTEDEA 83


                 ....*.
gi 767910105 125 RYRCEL 130
Cdd:cd04984   84 DYYCQV 89
IgV_B7-H6 cd20981
Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the ...
 47-131 1.14e-03

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: 38.36  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  47 SHRGATATLPCVLGTTPP----SYKVRWSKVEPGELRETLILITNGLHARGYGPlGGRARMRRGHRLDASLVIAGVRLED 122
Cdd:cd20981   13 TPLNDNVTIFCNIFYSQPlnitSMGITWFRKSLTFDKEVKVFEFFGDHQKAFRP-GAIVSPWRLKSGDASLQLPGVQLEE 91


                 ....*....
gi 767910105 123 EGRYRCELI 131
Cdd:cd20981   92 AGEYRCEVV 100
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 49-134 1.18e-03

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 37.68  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  49 RGATATLPC-VLGTTPPSykVRWSKV---EPGELRETLILITNGLHARGygplggrarmrrghrldaSLVIAGVRLEDEG 124
Cdd:cd20954   15 AGQDVMLHCqADGFPTPT--VTWKKAtgsTPGEYKDLLYDPNVRILPNG------------------TLVFGHVQKENEG 74

                         90
                 ....*....|
gi 767910105 125 RYRCELINGI 134
Cdd:cd20954   75 HYLCEAKNGI 84
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 50-134 1.36e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) 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, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), 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 Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 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 the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 37.37  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  50 GATATLPCVLGTTPPSyKVRWSKvEPGELretlilitnglhargygPLGgRARMRRghrlDASLVIAGVRLEDEGRYRCE 129
Cdd:cd05725   12 DDSAEFQCEVGGDPVP-TVRWRK-EDGEL-----------------PKG-RYEILD----DHSLKIRKVTAGDMGSYTCV 67


                 ....*
gi 767910105 130 LINGI 134
Cdd:cd05725   68 AENMV 72
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 50-130 1.54e-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: 37.81  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  50 GATATLPCVLGTTPPSY--KVRWSKVEPGElrETLILI---TNGLHARGygPLGGRARMRRGHRL--DASLVIAGVRLED 122
Cdd:cd05718   14 GGSVTLPCSLTSPGTTKitQVTWMKIGAGS--SQNVAVfhpQYGPSVPN--PYAERVEFLAARLGlrNATLRIRNLRVED 89


                 ....*...
gi 767910105 123 EGRYRCEL 130
Cdd:cd05718   90 EGNYICEF 97
IgV_PD1 cd16088
Immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1); The members here are ...
 50-131 2.06e-03

Immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1); The members here are composed of the immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1; also known as CD279/cluster of differentiation 279). PD1 is a cell surface receptor that is expressed on T cells and pro-B cells. The protein's structure includes an extracellular IgV domain followed by a transmembrane region and an intracellular tail. Activation of CD4+ T cells, CD8+ T cells, NKT cells, B cells, and monocytes induces PD-1 expression, immediately after which it binds two distinct ligands, PD-L1 (also known as B7-H1 or CD274/cluster of differentiation 274) and PD-L2, also known as B7-DC. PD-1 plays an important role in down regulating the immune system by preventing the activation of T-cells, reducing autoimmunity and promoting self-tolerance. The inhibitory effect of PD-1 is accomplished by promoting apoptosis in antigen specific T-cells in lymph nodes while simultaneously reducing apoptosis in regulatory T cells. A class of drugs that target PD-1, known as the PD-1 inhibitors, activate the immune system to attack tumors and treat cancer. Comparisons between the mouse PD-1 (mPD-1) and human PD-1 (hPD-1) reveals that unlike the mPD-1 which has a conventional IgSF V-set domain, hPD-1 lacks a C" strand, and instead the C' and D strands are connected by a long and flexible loop. In addition, the BC loop is not stabilized by disulfide bonding to the F strand of the ligand binding beta sheet. These differences result in different binding affinities of human and mouse PD-1 for their ligands.


Pssm-ID: 409509  Cd Length: 112  Bit Score: 37.49  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  50 GATATLPCVLGTTPPSYKVRWSKVEPGELRETLILITNGLHARGYgplggRARMR-----RGHRLDASLVIAgvRLEDEG 124
Cdd:cd16088   14 GANATFTCSFSNTSESFVLNWYRLSPSNQTDKLAAFPEDRSQPGQ-----DWRFRvtqlpNGRDFHMSVVRA--RRNDSG 86


                 ....*..
gi 767910105 125 RYRCELI 131
Cdd:cd16088   87 TYLCGAI 93
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 256-337 2.84e-03

This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It also plays an important role in arteriogenesis. The functional HA-binding domain of CD44 is an extended domain comprised of a single link module flanked with N-and C- extensions. These extensions are essential for folding and for functional activity. This group also contains the cell surface retention sequence (CRS) binding protein-1 (CRSBP-1) and lymph vessel endothelial receptor-1 (LYVE-1). CRSBP-1 is a cell surface binding protein for the CRS motif of PDGF-BB (platelet-derived growth factor-BB) and is responsible for the cell surface retention of PDGF-BB in SSV-transformed cells. CRSBP-1 may play a role in autocrine regulation of cell growth mediated by CRS containing growth regulators. LYVE-1 is preferentially expressed on the lymphatic endothelium and is used as a molecular marker for the detection and characterization of lymphatic vessels in tumors.


Pssm-ID: 239593  Cd Length: 144  Bit Score: 37.82  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105 256 LTLSEAHAACRRRGAVVAKVGHLYAAWKFsGLDQCDGGWLADGSVRFPITTPRPRCGGlpdPGVRSFGFPRPQQAAYGTY 335
Cdd:cd03516   19 LNFTEAKEACRALGLTLASKAQVETALKF-GFETCRYGWVEDGFVVIPRIDPNPLCGK---NGTGVYILNSNLSSRYDAY 94


                 ..
gi 767910105 336 CY 337
Cdd:cd03516   95 CY 96
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
 53-145 3.02e-03

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. 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. The first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.


Pssm-ID: 409538  Cd Length: 102  Bit Score: 36.75  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  53 ATLPCVLGTTPPSYKVRWSKVepGELRETLILITNGLHargyGPLGGRARMrrghrLDASLVIAGVRLEDEGRYRCELI- 131
Cdd:cd20946   17 VILSCKTPKKTSSPRVEWKKL--QRDVTFVVFQNNKIQ----GDYKGRAEI-----LGTNITIKNVTRSDSGKYRCEVSa 85

                         90
                 ....*....|....*.
gi 767910105 132 --NGIEDESVALTLSL 145
Cdd:cd20946   86 rsDGQNLGEVTVTLEV 101
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 39-128 3.53e-03

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: 36.61  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910105  39 PPIHEVIHSHRGATATLPCVLGTTPPSYKVRWSKVEPgelRETLILITNglhaRGYGPLGgrarmRRGHRLDA-----SL 113
Cdd:cd05716    1 SVGPEVVTGVEGGSVTIQCPYPPKYASSRKYWCKWGS---EGCQTLVSS----EGVVPGG-----RISLTDDPdngvfTV 68

                         90
                 ....*....|....*
gi 767910105 114 VIAGVRLEDEGRYRC 128
Cdd:cd05716   69 TLNQLRKEDAGWYWC 83
 
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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