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Conserved domains on  [gi|755516069|ref|XP_011239505|]
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ephrin type-A receptor 1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
 28-204 6.23e-139

Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA1 is downregulated in some advanced colorectal and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion.


:

Pssm-ID: 198447  Cd Length: 177  Bit Score: 401.33  E-value: 6.23e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPPETGWSEVQQMLNGTPLYMYQDCPIQEGGDTDHWLRSNWIYRGEEASRIYVELQFTVRDC 107
Cdd:cd10479    1 EVTLMDTSTAQGELGWLLDPPEVGWSEVQQMLNGTPLYMYQDCPVQSEGDTDHWLRSNWIYRGEEASRIYVELQFTVRDC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 108 KSFPGGAGPLGCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAFH 187
Cdd:cd10479   81 KSFPGGAGPLGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRGLYLAFH 160

                        170
                 ....*....|....*..
gi 755516069 188 NPGSCVALVSVRVFYQR 204
Cdd:cd10479  161 NPGACVALVSVRVFYQR 177
fn3 pfam00041
Fibronectin type III domain;
335-426 9.14e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 9.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  335 SAPQNLSFS-TSGTQLSLRWEPPRDTGGrHDIRYSVECLQCRGIaqdggpcqpcGKGVHFSPAAsglTTSTVQVQGLEPY 413
Cdd:pfam00041   1 SAPSNLTVTdVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSG----------EPWNEITVPG---TTTSVTLTGLKPG 66

                          90
                  ....*....|...
gi 755516069  414 ANYTFTVKSQNRV 426
Cdd:pfam00041  67 TEYEVRVQAVNGG 79
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 454-536 1.31e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 454 LKLVKKEPRQLELTWagSRPRNPGGNL-SYELHVLNQDE-EWHQM----VLEPRVLLTKLQPDTTYIVRVRTLTPLGPGP 527
Cdd:cd00063    7 LRVTDVTSTSVTLSW--TPPEDDGGPItGYVVEYREKGSgDWKEVevtpGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84


                 ....*....
gi 755516069 528 FSPDHEFRT 536
Cdd:cd00063   85 PSESVTVTT 93
TM_EphA1 cd12841
Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) ...
 537-554 7.80e-06

Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) comprise the largest subfamily of receptor PTKs, and are classified into two classes (EphA and EphB), corresponding to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphA1 has been associated with late-onset Alzheimer's disease and certain cancers such as colorectal and gastric carcinomas. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a single-span transmembrane (TM) domain, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The TM domain mediates dimerization.


:

Pssm-ID: 214014  Cd Length: 38  Bit Score: 43.12  E-value: 7.80e-06
                         10
                 ....*....|....*...
gi 755516069 537 SPPVSRSLTGGEIVAVIF 554
Cdd:cd12841    1 SPPVSRGLTGGEIVAIIF 18
TNFRSF super family cl22855
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 252-320 7.17e-05

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


The actual alignment was detected with superfamily member cd15834:

Pssm-ID: 473981 [Multi-domain]  Cd Length: 150  Bit Score: 43.25  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 252 PDGEWLVPVGQC--QCEPGY---EESSG---NVGCTACPTGFYRVDMN----TLRCLKC-PQHSIAES----EGSTICTC 314
Cdd:cd15834    2 LDSEYLSENGICcnKCHPGYklkEECTApgeRSQCTPCPEGTYLEQINyspnCRRCTLCkVKNEEEVSpckkSSNTVCRC 81


                 ....*.
gi 755516069 315 ENGHYR 320
Cdd:cd15834   82 KKGYYK 87
 
Name Accession Description Interval E-value
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
 28-204 6.23e-139

Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA1 is downregulated in some advanced colorectal and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion.


Pssm-ID: 198447  Cd Length: 177  Bit Score: 401.33  E-value: 6.23e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPPETGWSEVQQMLNGTPLYMYQDCPIQEGGDTDHWLRSNWIYRGEEASRIYVELQFTVRDC 107
Cdd:cd10479    1 EVTLMDTSTAQGELGWLLDPPEVGWSEVQQMLNGTPLYMYQDCPVQSEGDTDHWLRSNWIYRGEEASRIYVELQFTVRDC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 108 KSFPGGAGPLGCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAFH 187
Cdd:cd10479   81 KSFPGGAGPLGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRGLYLAFH 160

                        170
                 ....*....|....*..
gi 755516069 188 NPGSCVALVSVRVFYQR 204
Cdd:cd10479  161 NPGACVALVSVRVFYQR 177
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
28-204 3.38e-87

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 268.38  E-value: 3.38e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069    28 EVTLMDTSTAQGELGWLLDPPEtGWSEVQQM-LNGTPLYMYQDCPIQEGgDTDHWLRSNWIYRGEeASRIYVELQFTVRD 106
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPE-GWEEVSGMdENGTPIRTYQVCNVQEG-NQNNWLRTNFIRRRG-AQRIYVELKFTVRD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069   107 CKSFPGGAGPlgCKETFNLFYMESDQDVGIQ----LRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGL 182
Cdd:smart00615  78 CSSLPGVGGS--CKETFNLYYYESDTDTATNtlpnWMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGF 155

                          170       180
                   ....*....|....*....|..
gi 755516069   183 YLAFHNPGSCVALVSVRVFYQR 204
Cdd:smart00615 156 YLAFQDQGACVALVSVRVFYKK 177
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
 29-205 1.73e-75

Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are a large family of receptor tyrosine kinases. This family represents the amino terminal domain which binds the ephrin ligand.


Pssm-ID: 460198  Cd Length: 177  Bit Score: 237.95  E-value: 1.73e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069   29 VTLMDTSTAQGELGWLLDPPETGWSEVQQM-LNGTPLYMYQDCPIQEGgDTDHWLRSNWIYRGEeASRIYVELQFTVRDC 107
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPYDGGWEEVSGLdENGRTIRTYQVCNVEEP-NQNNWLRTPFIPRGG-ASRVYVELKFTVRDC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  108 KSFPGGAGPlgCKETFNLFYMESDQDVGI----QLRRPLFQKVTTVAADQSFTIRDlASGSVKLNVERCSLGHLTRRGLY 183
Cdd:pfam01404  79 SSIPGVSGT--CKETFNLYYYESDADAATatppAWRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFY 155

                         170       180
                  ....*....|....*....|..
gi 755516069  184 LAFHNPGSCVALVSVRVFYQRC 205
Cdd:pfam01404 156 LAFQDQGACIALLSVRVFYKKC 177
fn3 pfam00041
Fibronectin type III domain;
335-426 9.14e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 9.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  335 SAPQNLSFS-TSGTQLSLRWEPPRDTGGrHDIRYSVECLQCRGIaqdggpcqpcGKGVHFSPAAsglTTSTVQVQGLEPY 413
Cdd:pfam00041   1 SAPSNLTVTdVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSG----------EPWNEITVPG---TTTSVTLTGLKPG 66

                          90
                  ....*....|...
gi 755516069  414 ANYTFTVKSQNRV 426
Cdd:pfam00041  67 TEYEVRVQAVNGG 79
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 334-425 9.75e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.58  E-value: 9.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 334 PSAPQNLSFS-TSGTQLSLRWEPPRDTGGRHDiRYSVECLQCrgiaqDGGPCQPCGKGVHfspaasglTTSTVQVQGLEP 412
Cdd:cd00063    1 PSPPTNLRVTdVTSTSVTLSWTPPEDDGGPIT-GYVVEYREK-----GSGDWKEVEVTPG--------SETSYTLTGLKP 66

                         90
                 ....*....|...
gi 755516069 413 YANYTFTVKSQNR 425
Cdd:cd00063   67 GTEYEFRVRAVNG 79
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 454-536 1.31e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 454 LKLVKKEPRQLELTWagSRPRNPGGNL-SYELHVLNQDE-EWHQM----VLEPRVLLTKLQPDTTYIVRVRTLTPLGPGP 527
Cdd:cd00063    7 LRVTDVTSTSVTLSW--TPPEDDGGPItGYVVEYREKGSgDWKEVevtpGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84


                 ....*....
gi 755516069 528 FSPDHEFRT 536
Cdd:cd00063   85 PSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 334-426 5.38e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.39  E-value: 5.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069   334 PSAPQNLSFS-TSGTQLSLRWEPPRDTGGRHDI-RYSVEclqcrgiaqdggpcqPCGKGVHFSPAASGLTTSTVQVQGLE 411
Cdd:smart00060   1 PSPPSNLRVTdVTSTSVTLSWEPPPDDGITGYIvGYRVE---------------YREEGSEWKEVNVTPSSTSYTLTGLK 65

                           90
                   ....*....|....*
gi 755516069   412 PYANYTFTVKSQNRV 426
Cdd:smart00060  66 PGTEYEFRVRAVNGA 80
fn3 pfam00041
Fibronectin type III domain;
461-529 2.94e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 2.94e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755516069  461 PRQLELTWagSRPRNPGGNL-SYELHVLNQDEE--WHQMVL---EPRVLLTKLQPDTTYIVRVRTLTPLGPGPFS 529
Cdd:pfam00041  13 STSLTVSW--TPPPDGNGPItGYEVEYRPKNSGepWNEITVpgtTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 454-526 3.36e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.38  E-value: 3.36e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755516069   454 LKLVKKEPRQLELTWagSRPRNPGGN---LSYELHVLNQDEEWHQM---VLEPRVLLTKLQPDTTYIVRVRTLTPLGPG 526
Cdd:smart00060   7 LRVTDVTSTSVTLSW--EPPPDDGITgyiVGYRVEYREEGSEWKEVnvtPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
TM_EphA1 cd12841
Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) ...
 537-554 7.80e-06

Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) comprise the largest subfamily of receptor PTKs, and are classified into two classes (EphA and EphB), corresponding to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphA1 has been associated with late-onset Alzheimer's disease and certain cancers such as colorectal and gastric carcinomas. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a single-span transmembrane (TM) domain, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The TM domain mediates dimerization.


Pssm-ID: 214014  Cd Length: 38  Bit Score: 43.12  E-value: 7.80e-06
                         10
                 ....*....|....*...
gi 755516069 537 SPPVSRSLTGGEIVAVIF 554
Cdd:cd12841    1 SPPVSRGLTGGEIVAIIF 18
TNFRSF1A_teleost cd15834
Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) in teleosts; also known as ...
 252-320 7.17e-05

Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) in teleosts; also known as TNFR1; This subfamily of TNFRSF1 ((also known as type I TNFR, TNFR1, DR1, TNFRSF1A, CD120a, p55) is found in teleosts. It binds TNF-alpha, through the death domain (DD), and activates NF-kappaB, mediates apoptosis and activates signaling pathways controlling inflammatory, immune, and stress responses. It mediates signal transduction by interacting with antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRAF2 and TRADD that play regulatory roles. The human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS), or periodic fever syndrome, is associated with germline mutations of the extracellular domains of this receptor, possibly due to impaired receptor clearance. Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder, and high levels are also associated with cognitive impairment and dementia. Knockout studies in zebrafish embryos have shown that a signaling balance between TNFRSF1A and TNFRSF1B is required for endothelial cell integrity. TNFRSF1A signals apoptosis through caspase-8, whereas TNFRSF1B signals survival via NF-kappaB in endothelial cells. Thus, this apoptotic pathway seems to be evolutionarily conserved, as TNFalpha promotes apoptosis of human endothelial cells and triggers caspase-2 and P53 activation in these cells via TNFRSF1A.


Pssm-ID: 276930 [Multi-domain]  Cd Length: 150  Bit Score: 43.25  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 252 PDGEWLVPVGQC--QCEPGY---EESSG---NVGCTACPTGFYRVDMN----TLRCLKC-PQHSIAES----EGSTICTC 314
Cdd:cd15834    2 LDSEYLSENGICcnKCHPGYklkEECTApgeRSQCTPCPEGTYLEQINyspnCRRCTLCkVKNEEEVSpckkSSNTVCRC 81


                 ....*.
gi 755516069 315 ENGHYR 320
Cdd:cd15834   82 KKGYYK 87
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
310-518 2.48e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 40.76  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 310 TICTCENGHYRAPGEGPQV-ACTRPPSAPQNLSF-STSGTQLSLRWEPPRDTGGRhdiRYSVEclqcRGIAQDGGpcqpc 387
Cdd:COG3401  208 RVAATDTGGESAPSNEVSVtTPTTPPSAPTGLTAtADTPGSVTLSWDPVTESDAT---GYRVY----RSNSGDGP----- 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 388 gkgvhFSPAASgLTTSTVQVQGLEPYANYTFTVKSQNrvsgldssspssaslsinmgHAESLSGLS-------------- 453
Cdd:COG3401  276 -----FTKVAT-VTTTSYTDTGLTNGTTYYYRVTAVD--------------------AAGNESAPSnvvsvttdltppaa 329

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755516069 454 ---LKLVKKEPRQLELTWAGSrprnPGGNL-SYELH-VLNQDEEWHQM---VLEPRVLLTKLQPDTTYIVRVR 518
Cdd:COG3401  330 psgLTATAVGSSSITLSWTAS----SDADVtGYNVYrSTSGGGTYTKIaetVTTTSYTDTGLTPGTTYYYKVT 398
 
Name Accession Description Interval E-value
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
 28-204 6.23e-139

Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA1 is downregulated in some advanced colorectal and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion.


Pssm-ID: 198447  Cd Length: 177  Bit Score: 401.33  E-value: 6.23e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPPETGWSEVQQMLNGTPLYMYQDCPIQEGGDTDHWLRSNWIYRGEEASRIYVELQFTVRDC 107
Cdd:cd10479    1 EVTLMDTSTAQGELGWLLDPPEVGWSEVQQMLNGTPLYMYQDCPVQSEGDTDHWLRSNWIYRGEEASRIYVELQFTVRDC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 108 KSFPGGAGPLGCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAFH 187
Cdd:cd10479   81 KSFPGGAGPLGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRGLYLAFH 160

                        170
                 ....*....|....*..
gi 755516069 188 NPGSCVALVSVRVFYQR 204
Cdd:cd10479  161 NPGACVALVSVRVFYQR 177
EphR_LBD_A cd10473
Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the ...
 28-204 6.01e-103

Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.


Pssm-ID: 198441  Cd Length: 173  Bit Score: 308.98  E-value: 6.01e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPPEtGWSEVQQMLNG-TPLYMYQDCPIQEGgDTDHWLRSNWIYRGEeASRIYVELQFTVRD 106
Cdd:cd10473    1 EVVLLDSKTAQGELGWITYPPN-GWEEISEMDEDyTPIRTYQVCNVMEP-NQNNWLRTNWIYRGE-AQRIYIELKFTLRD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 107 CKSFPGGAGplGCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAF 186
Cdd:cd10473   78 CNSFPGVLG--TCKETFNLYYMESDLDLGRNIRENQFTKIDTIAADESFTQGDLGDRIMKLNTEVREVGPLTKKGFYLAF 155

                        170
                 ....*....|....*...
gi 755516069 187 HNPGSCVALVSVRVFYQR 204
Cdd:cd10473  156 QDVGACVALVSVRVYYKK 173
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
28-204 3.38e-87

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 268.38  E-value: 3.38e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069    28 EVTLMDTSTAQGELGWLLDPPEtGWSEVQQM-LNGTPLYMYQDCPIQEGgDTDHWLRSNWIYRGEeASRIYVELQFTVRD 106
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPE-GWEEVSGMdENGTPIRTYQVCNVQEG-NQNNWLRTNFIRRRG-AQRIYVELKFTVRD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069   107 CKSFPGGAGPlgCKETFNLFYMESDQDVGIQ----LRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGL 182
Cdd:smart00615  78 CSSLPGVGGS--CKETFNLYYYESDTDTATNtlpnWMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGF 155

                          170       180
                   ....*....|....*....|..
gi 755516069   183 YLAFHNPGSCVALVSVRVFYQR 204
Cdd:smart00615 156 YLAFQDQGACVALVSVRVFYKK 177
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
 29-205 1.73e-75

Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are a large family of receptor tyrosine kinases. This family represents the amino terminal domain which binds the ephrin ligand.


Pssm-ID: 460198  Cd Length: 177  Bit Score: 237.95  E-value: 1.73e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069   29 VTLMDTSTAQGELGWLLDPPETGWSEVQQM-LNGTPLYMYQDCPIQEGgDTDHWLRSNWIYRGEeASRIYVELQFTVRDC 107
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPYDGGWEEVSGLdENGRTIRTYQVCNVEEP-NQNNWLRTPFIPRGG-ASRVYVELKFTVRDC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  108 KSFPGGAGPlgCKETFNLFYMESDQDVGI----QLRRPLFQKVTTVAADQSFTIRDlASGSVKLNVERCSLGHLTRRGLY 183
Cdd:pfam01404  79 SSIPGVSGT--CKETFNLYYYESDADAATatppAWRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFY 155

                         170       180
                  ....*....|....*....|..
gi 755516069  184 LAFHNPGSCVALVSVRVFYQRC 205
Cdd:pfam01404 156 LAFQDQGACIALLSVRVFYKKC 177
EphR_LBD_A2 cd10480
Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of ...
 28-205 3.80e-71

Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA2 negatively regulates cell differentiation and has been shown to be overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion.


Pssm-ID: 198448  Cd Length: 174  Bit Score: 226.65  E-value: 3.80e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPPETGWSEVQQMLNGTPLYMYQDCPIQEgGDTDHWLRSNWIYRGeEASRIYVELQFTVRDC 107
Cdd:cd10480    1 EVVLLDFAAAGGELGWLTHPYGKGWDLMQNVMNDSPIYMYSVCNVMS-GEQDNWLRTNWIYRS-EAERIFIELKFTVRDC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 108 KSFPGGAGplGCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAFH 187
Cdd:cd10480   79 NSFPGGAG--SCKETFNLYYAESDVDYGTNFQKRQFRKIDTIAPDEITVSSDFETRNVKLNVEERSVGPLTRKGFYLAFQ 156

                        170
                 ....*....|....*...
gi 755516069 188 NPGSCVALVSVRVFYQRC 205
Cdd:cd10480  157 DIGACVALLSVRVYYKKC 174
EphR_LBD cd10319
Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest ...
 29-202 7.78e-58

Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). They are subdivided into 2 groups, A and B type receptors, depending on their ligand ephrin-A or ephrin-B, respectively. In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.


Pssm-ID: 198439  Cd Length: 177  Bit Score: 191.85  E-value: 7.78e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  29 VTLMDTSTAQGELGWLLDPP-ETGWSEVQ-QMLNGTPLYMYQDCPIQEGGdTDHWLRSNWIYRGEeASRIYVELQFTVRD 106
Cdd:cd10319    1 VVLLDTTLATSDLGWLTYPYgHGGWDEESgLDPDGANIRTYVVCNVAMPN-QDNWLRTPFIERRG-AQRIYVELKFTVRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 107 CKSFPGGAGplGCKETFNLFYMESDQD----VGIQLRRPLFQKVTTVAADQSFTIRDlASGSVKLNVERCSLGHLTRRGL 182
Cdd:cd10319   79 CESFPGNAR--SCKETFNLYYYESDHDtatkEFPPWNEDPYTKIDTIAADESFKSSN-EDTTEKLNTETRSIGPLTKRGF 155

                        170       180
                 ....*....|....*....|
gi 755516069 183 YLAFHNPGSCVALVSVRVFY 202
Cdd:cd10319  156 YLAFQDQGACMSLLSVKVYY 175
EphR_LBD_A10 cd10487
Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the ...
 28-204 8.78e-56

Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction results in cell-cell repulsion or adhesion.


Pssm-ID: 198455  Cd Length: 173  Bit Score: 186.38  E-value: 8.78e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLlDPPETGWSEVQQM-LNGTPLYMYQDCPIQEGgDTDHWLRSNWIYRGEeASRIYVELQFTVRD 106
Cdd:cd10487    1 EVVLLDSKESQAELGWT-SLPSNGWEEISGVdEHYKPIRTYQVCNVMEP-NQNNWLQTGWISRGR-GQRIFIELQFTLRD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 107 CKSFPGGAGPlgCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAF 186
Cdd:cd10487   78 CNSIPGVAGT--CKETFNLYYAESDADLGRRLRESRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGHLSRRGFHLAF 155

                        170
                 ....*....|....*...
gi 755516069 187 HNPGSCVALVSVRVFYQR 204
Cdd:cd10487  156 QDVGACVALVSVRVYYKQ 173
EphR_LBD_A7 cd10485
Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the ...
 26-205 2.29e-55

Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA7 has been implicated in various cancers, including prostate, gastic and colorectal cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198453  Cd Length: 177  Bit Score: 185.24  E-value: 2.29e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  26 AEEVTLMDTSTAQGELGWLLDPPeTGWSEVQQM-LNGTPLYMYQDCPIQEGgDTDHWLRSNWIYRGeEASRIYVELQFTV 104
Cdd:cd10485    1 AKEVILLDSKAQQTELEWISSPP-SGWEEISGLdENYTPIRTYQVCQVMEP-NQNNWLRTNWISKG-NAQRIFVELKFTL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 105 RDCKSFPGGAGPlgCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYL 184
Cdd:cd10485   78 RDCNSLPGVLGT--CKETFNLYYYETDYDTGRNIRENQYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYL 155

                        170       180
                 ....*....|....*....|.
gi 755516069 185 AFHNPGSCVALVSVRVFYQRC 205
Cdd:cd10485  156 AFQDVGACIALVSVKVYYKKC 176
EphR_LBD_A8 cd10486
Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the ...
 28-204 9.34e-55

Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA8 has been implicated in various cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198454  Cd Length: 173  Bit Score: 183.69  E-value: 9.34e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPPEtGWSEVQQMLNG-TPLYMYQDCPIQEGgDTDHWLRSNWIYRgEEASRIYVELQFTVRD 106
Cdd:cd10486    1 EVNLLDTSTISGDWGWLTYPSH-GWDSINEMDEYfSPIHTYQVCNVMSP-NQNNWLRTNWVQR-DGARRVYAEIKFTLRD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 107 CKSFPGGAGPlgCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAF 186
Cdd:cd10486   78 CNSMPGVLGT--CKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAF 155

                        170
                 ....*....|....*...
gi 755516069 187 HNPGSCVALVSVRVFYQR 204
Cdd:cd10486  156 QDIGACIAIVSVRVYYKK 173
EphR_LBD_A4 cd10482
Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the ...
 28-204 1.02e-54

Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. A loss of EphA4, as well as EphB2, precedes memory decline in a murine model of Alzheimers disease. EphA4 has been shown to have a negative effect on axon regeneration and functional restoration in corticospinal lesions and is downregulated in some cervical cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198450  Cd Length: 174  Bit Score: 183.71  E-value: 1.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPPETGWSEVQQM-LNGTPLYMYQDCPIQEGGDtDHWLRSNWIYRGEeASRIYVELQFTVRD 106
Cdd:cd10482    1 EVTLLDSRSVQGELGWIASPLEGGWEEVSIMdEKNTPIRTYQVCNVMEPSQ-NNWLRTDWIPREG-AQRVYIEIKFTLRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 107 CKSFPGGAGPlgCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAF 186
Cdd:cd10482   79 CNSLPGVMGT--CKETFNLYYYESNNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEVRDVGPLSKKGFYLAF 156

                        170
                 ....*....|....*...
gi 755516069 187 HNPGSCVALVSVRVFYQR 204
Cdd:cd10482  157 QDVGACIALVSVRVFYKK 174
EphR_LBD_A3 cd10481
Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the ...
 28-204 7.46e-54

Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA3 has been implicated in leukemia, lung and other cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion.


Pssm-ID: 198449  Cd Length: 173  Bit Score: 181.41  E-value: 7.46e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLlDPPETGWSEVQQM-LNGTPLYMYQDCPIQEGgDTDHWLRSNWIYRgEEASRIYVELQFTVRD 106
Cdd:cd10481    1 EVNLLDSKAIQGELGWI-SYPSHGWEEISGVdEHYTPIRTYQVCNVMDH-SQNNWLRTNWIPR-NSAQKIYVELKFTLRD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 107 CKSFPGGAGPlgCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAF 186
Cdd:cd10481   78 CNSIPLVLGT--CKETFNLYYMESDEDQGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSKKGFYLAF 155

                        170
                 ....*....|....*...
gi 755516069 187 HNPGSCVALVSVRVFYQR 204
Cdd:cd10481  156 QDVGACVALVSVRVYFKK 173
EphR_LBD_A5 cd10483
Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the ...
 28-204 2.21e-52

Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA5 is almost exclusively expressed in the nervous system. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198451  Cd Length: 173  Bit Score: 177.14  E-value: 2.21e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLdPPETGWSEVQQM-LNGTPLYMYQDCPIQEGgDTDHWLRSNWIyRGEEASRIYVELQFTVRD 106
Cdd:cd10483    1 EVNLLDSRSVMGDLGWIA-YPKNGWEEIGEVdENYAPIHTYQVCKVMEQ-NQNNWLLTSWI-SNEGASRIFIELKFTLRD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 107 CKSFPGGAGPlgCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLAF 186
Cdd:cd10483   78 CNSLPGGLGT--CKETFNVYYFESNDEDGRNIRENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLTKKGFYLAF 155

                        170
                 ....*....|....*...
gi 755516069 187 HNPGSCVALVSVRVFYQR 204
Cdd:cd10483  156 QDLGACIALVSVRVYYKK 173
EphR_LBD_A6 cd10484
Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the ...
 28-204 4.47e-51

Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA6, like other Eph receptors and their ephrin ligands, seems to play a role in neural development, underlying learning and memory. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198452  Cd Length: 173  Bit Score: 173.67  E-value: 4.47e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPPeTGWSEVQQM--LNgTPLYMYQDCPIQEGgDTDHWLRSNWIYRgEEASRIYVELQFTVR 105
Cdd:cd10484    1 QVVLLDTTMVLGELNWKTYPC-NGWDAITEMdeYN-RPIHTYQVCNVMEP-NQNNWLRTNWISR-DAAQKIYVEMKFTLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 106 DCKSFPGGAGPlgCKETFNLFYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYLA 185
Cdd:cd10484   77 DCNSIPWVVGT--CKETFNLHYMESDEAHAVKFKPNQYSKIDTIAADESFTQMDLGDRILKLNTEVREVGPITRKGFYLA 154

                        170
                 ....*....|....*....
gi 755516069 186 FHNPGSCVALVSVRVFYQR 204
Cdd:cd10484  155 FQDIGACIALVSVRVYYKK 173
EphR_LBD_B cd10472
Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the ...
 30-204 2.68e-48

Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. They play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphB receptors are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.


Pssm-ID: 198440  Cd Length: 176  Bit Score: 166.59  E-value: 2.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  30 TLMDTSTAQGELGWLLDPpETGWSEVQ---QMLNgtPLYMYQDCPIQEGgDTDHWLRSNWIYRgEEASRIYVELQFTVRD 106
Cdd:cd10472    2 TLMDTRTATAELGWTAHP-PSGWEEVSgydENMN--TIRTYQVCNVFES-NQNNWLRTKFIRR-RGAHRVYVEMKFTVRD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 107 CKSFPGGAGplGCKETFNLFYMESDQDVGIQLRRPLFQ----KVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGL 182
Cdd:cd10472   77 CSSIPNVPG--SCKETFNLYYYESDSDIATKTSPFWMEnpyvKVDTIAADESFSQVDLGGRVMKVNTEVRSFGPLSRNGF 154

                        170       180
                 ....*....|....*....|..
gi 755516069 183 YLAFHNPGSCVALVSVRVFYQR 204
Cdd:cd10472  155 YLAFQDYGACMSLISVRVFYKK 176
EphR_LBD_B3 cd10478
Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the ...
 28-204 1.42e-44

Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB3 plays a role in cell positioning in the gastrointestinal tract by being preferentially expressed in Paneth cells. It also has been implicated in early colorectal cancer and early stage squamous cell lung cancer. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198446  Cd Length: 173  Bit Score: 156.32  E-value: 1.42e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPpETGWSEVQ---QMLNgtPLYMYQDCPIQEGgDTDHWLRSNWIYRgEEASRIYVELQFTV 104
Cdd:cd10478    1 EETLMDTKWVTSELAWTTHP-ESGWEEVSgydEAMN--PIRTYQVCNVRES-NQNNWLRTGFIPR-RDVQRVYVELKFTV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 105 RDCKSFPGGAGplGCKETFNLFYMESDQDVGIQLRRPLFQ----KVTTVAADQSFTIRDlaSGSVKLNVErcSLGHLTRR 180
Cdd:cd10478   76 RDCNSIPNIPG--SCKETFNLFYYESDSDSASASSPFWMEnpyvKVDTIAPDESFSRLD--SGRVNTKVR--SFGPLSKA 149

                        170       180
                 ....*....|....*....|....
gi 755516069 181 GLYLAFHNPGSCVALVSVRVFYQR 204
Cdd:cd10478  150 GFYLAFQDLGACMSLISVRAFFKK 173
EphR_LBD_B2 cd10477
Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the ...
 28-204 4.82e-44

Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB2 plays a role in cell positioning in the gastrointestinal tract by being expressed in proliferating progenitor cells. It also has been implicated in colorectal cancer. A loss of EphB2, as well as EphA4, also precedes memory decline in a murine model of Alzheimers disease. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198445  Cd Length: 178  Bit Score: 155.22  E-value: 4.82e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPPeTGWSEVQQM-LNGTPLYMYQDCPIQEGgDTDHWLRSNWIYRgEEASRIYVELQFTVRD 106
Cdd:cd10477    2 EETLMDSTTATAELGWMVHPP-SGWEEVSGYdENMNTIRTYQVCNVFES-SQNNWLRTKYIRR-RGAHRIHVEMKFSVRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 107 CKSFPGGAGplGCKETFNLFYMESDQDVGIQLRRPLFQ----KVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGL 182
Cdd:cd10477   79 CSSIPSVPG--SCKETFNLYYYESDFDSATKTFPNWMEnpwvKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRNGF 156

                        170       180
                 ....*....|....*....|..
gi 755516069 183 YLAFHNPGSCVALVSVRVFYQR 204
Cdd:cd10477  157 YLAFQDYGGCMSLIAVRVFYRK 178
EphR_LBD_B1 cd10476
Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the ...
 30-204 3.94e-41

Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. Using EphB1 knockout-mice, EphB1 has been shown to be essential to the development of long-term potentiation (LTP), a cellular model of synaptic plasticity, learning and memory formation. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198444  Cd Length: 176  Bit Score: 147.13  E-value: 3.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  30 TLMDTSTAQGELGWLLDPpETGWSEVQQM-LNGTPLYMYQDCPIQEGgDTDHWLRSNWIYRgEEASRIYVELQFTVRDCK 108
Cdd:cd10476    2 TLMDTRTATAELGWTANP-ASGWEEVSGYdENLNTIRTYQVCNVFEP-NQNNWLLTTFINR-RGAHRIYTEMRFTVRDCS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 109 SFPGGAGplGCKETFNLFYMESDQDVGIQLR----RPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRGLYL 184
Cdd:cd10476   79 SLPNVPG--SCKETFNLYYYETDSVIATKKSafwtEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYL 156

                        170       180
                 ....*....|....*....|
gi 755516069 185 AFHNPGSCVALVSVRVFYQR 204
Cdd:cd10476  157 AFQDYGACMSLLSVRVFFKK 176
EphR_LBD_B4 cd10474
Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the ...
 28-204 2.02e-40

Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB4 plays a role in osteoblast differentiation and has been linked to multiple myeloma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198442  Cd Length: 180  Bit Score: 145.10  E-value: 2.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  28 EVTLMDTSTAQGELGWLLDPPETG-WSEVQQMLN-GTPLYMYQDCPIQEGGDTDHWLRSNWIYRGEeASRIYVELQFTVR 105
Cdd:cd10474    1 EETLLNTKLETADLKWVTYPQVDGqWEELSGLDEeQHSVRTYEVCDAQRAGGQAHWLRTGWVPRRG-AVHVYATLRFTML 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 106 DCKSFPGGAgpLGCKETFNLFYMESDQDVGIQLRRPLFQ----KVTTVAADQSFTIRDLASGSVKLNVERCSLGHLTRRG 181
Cdd:cd10474   80 ECLSLPRAG--RSCKETFTVFYYESDADTATAHTPAWMEnpyiKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAG 157

                        170       180
                 ....*....|....*....|...
gi 755516069 182 LYLAFHNPGSCVALVSVRVFYQR 204
Cdd:cd10474  158 FYLAFQDQGACMALLSLHLFYKK 180
fn3 pfam00041
Fibronectin type III domain;
335-426 9.14e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 9.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069  335 SAPQNLSFS-TSGTQLSLRWEPPRDTGGrHDIRYSVECLQCRGIaqdggpcqpcGKGVHFSPAAsglTTSTVQVQGLEPY 413
Cdd:pfam00041   1 SAPSNLTVTdVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSG----------EPWNEITVPG---TTTSVTLTGLKPG 66

                          90
                  ....*....|...
gi 755516069  414 ANYTFTVKSQNRV 426
Cdd:pfam00041  67 TEYEVRVQAVNGG 79
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 334-425 9.75e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.58  E-value: 9.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 334 PSAPQNLSFS-TSGTQLSLRWEPPRDTGGRHDiRYSVECLQCrgiaqDGGPCQPCGKGVHfspaasglTTSTVQVQGLEP 412
Cdd:cd00063    1 PSPPTNLRVTdVTSTSVTLSWTPPEDDGGPIT-GYVVEYREK-----GSGDWKEVEVTPG--------SETSYTLTGLKP 66

                         90
                 ....*....|...
gi 755516069 413 YANYTFTVKSQNR 425
Cdd:cd00063   67 GTEYEFRVRAVNG 79
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 454-536 1.31e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 454 LKLVKKEPRQLELTWagSRPRNPGGNL-SYELHVLNQDE-EWHQM----VLEPRVLLTKLQPDTTYIVRVRTLTPLGPGP 527
Cdd:cd00063    7 LRVTDVTSTSVTLSW--TPPEDDGGPItGYVVEYREKGSgDWKEVevtpGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84


                 ....*....
gi 755516069 528 FSPDHEFRT 536
Cdd:cd00063   85 PSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 334-426 5.38e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.39  E-value: 5.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069   334 PSAPQNLSFS-TSGTQLSLRWEPPRDTGGRHDI-RYSVEclqcrgiaqdggpcqPCGKGVHFSPAASGLTTSTVQVQGLE 411
Cdd:smart00060   1 PSPPSNLRVTdVTSTSVTLSWEPPPDDGITGYIvGYRVE---------------YREEGSEWKEVNVTPSSTSYTLTGLK 65

                           90
                   ....*....|....*
gi 755516069   412 PYANYTFTVKSQNRV 426
Cdd:smart00060  66 PGTEYEFRVRAVNGA 80
fn3 pfam00041
Fibronectin type III domain;
461-529 2.94e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 2.94e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755516069  461 PRQLELTWagSRPRNPGGNL-SYELHVLNQDEE--WHQMVL---EPRVLLTKLQPDTTYIVRVRTLTPLGPGPFS 529
Cdd:pfam00041  13 STSLTVSW--TPPPDGNGPItGYEVEYRPKNSGepWNEITVpgtTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 454-526 3.36e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.38  E-value: 3.36e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755516069   454 LKLVKKEPRQLELTWagSRPRNPGGN---LSYELHVLNQDEEWHQM---VLEPRVLLTKLQPDTTYIVRVRTLTPLGPG 526
Cdd:smart00060   7 LRVTDVTSTSVTLSW--EPPPDDGITgyiVGYRVEYREEGSEWKEVnvtPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
TM_EphA1 cd12841
Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) ...
 537-554 7.80e-06

Transmembrane domain of Ephrin Receptor A1 Protein Tyrosine Kinase; Ephrin receptors (EphRs) comprise the largest subfamily of receptor PTKs, and are classified into two classes (EphA and EphB), corresponding to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphA1 has been associated with late-onset Alzheimer's disease and certain cancers such as colorectal and gastric carcinomas. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a single-span transmembrane (TM) domain, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The TM domain mediates dimerization.


Pssm-ID: 214014  Cd Length: 38  Bit Score: 43.12  E-value: 7.80e-06
                         10
                 ....*....|....*...
gi 755516069 537 SPPVSRSLTGGEIVAVIF 554
Cdd:cd12841    1 SPPVSRGLTGGEIVAIIF 18
TNFRSF1A_teleost cd15834
Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) in teleosts; also known as ...
 252-320 7.17e-05

Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) in teleosts; also known as TNFR1; This subfamily of TNFRSF1 ((also known as type I TNFR, TNFR1, DR1, TNFRSF1A, CD120a, p55) is found in teleosts. It binds TNF-alpha, through the death domain (DD), and activates NF-kappaB, mediates apoptosis and activates signaling pathways controlling inflammatory, immune, and stress responses. It mediates signal transduction by interacting with antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRAF2 and TRADD that play regulatory roles. The human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS), or periodic fever syndrome, is associated with germline mutations of the extracellular domains of this receptor, possibly due to impaired receptor clearance. Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder, and high levels are also associated with cognitive impairment and dementia. Knockout studies in zebrafish embryos have shown that a signaling balance between TNFRSF1A and TNFRSF1B is required for endothelial cell integrity. TNFRSF1A signals apoptosis through caspase-8, whereas TNFRSF1B signals survival via NF-kappaB in endothelial cells. Thus, this apoptotic pathway seems to be evolutionarily conserved, as TNFalpha promotes apoptosis of human endothelial cells and triggers caspase-2 and P53 activation in these cells via TNFRSF1A.


Pssm-ID: 276930 [Multi-domain]  Cd Length: 150  Bit Score: 43.25  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 252 PDGEWLVPVGQC--QCEPGY---EESSG---NVGCTACPTGFYRVDMN----TLRCLKC-PQHSIAES----EGSTICTC 314
Cdd:cd15834    2 LDSEYLSENGICcnKCHPGYklkEECTApgeRSQCTPCPEGTYLEQINyspnCRRCTLCkVKNEEEVSpckkSSNTVCRC 81


                 ....*.
gi 755516069 315 ENGHYR 320
Cdd:cd15834   82 KKGYYK 87
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 501-536 9.41e-04

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 38.54  E-value: 9.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755516069  501 RVLLTKLQPDTTYIVRVRTltplGPGPFSPDHEFRT 536
Cdd:pfam16656  62 RATLTGLEPGTTYYYRVGD----DNGGWSEVYSFTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
310-518 2.48e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 40.76  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 310 TICTCENGHYRAPGEGPQV-ACTRPPSAPQNLSF-STSGTQLSLRWEPPRDTGGRhdiRYSVEclqcRGIAQDGGpcqpc 387
Cdd:COG3401  208 RVAATDTGGESAPSNEVSVtTPTTPPSAPTGLTAtADTPGSVTLSWDPVTESDAT---GYRVY----RSNSGDGP----- 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516069 388 gkgvhFSPAASgLTTSTVQVQGLEPYANYTFTVKSQNrvsgldssspssaslsinmgHAESLSGLS-------------- 453
Cdd:COG3401  276 -----FTKVAT-VTTTSYTDTGLTNGTTYYYRVTAVD--------------------AAGNESAPSnvvsvttdltppaa 329

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755516069 454 ---LKLVKKEPRQLELTWAGSrprnPGGNL-SYELH-VLNQDEEWHQM---VLEPRVLLTKLQPDTTYIVRVR 518
Cdd:COG3401  330 psgLTATAVGSSSITLSWTAS----SDADVtGYNVYrSTSGGGTYTKIaetVTTTSYTDTGLTPGTTYYYKVT 398
 
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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