NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4885197|ref|NP_005218|]
View 

ephrin-A4 isoform a precursor [Homo sapiens]

Protein Classification

ephrin-A( domain architecture ID 10179613)

ephrin-A is a cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Ephrin-A_Ectodomain cd10425
Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell ...
 27-152 6.76e-60

Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin As contain a highly conserved receptor binding ectodomain described by this model. Although ephrin As do not have a cytoplasmic tail (in contrast to ephrin Bs), they are still capable of downstream activation of Src family kinases and phosphoinositide-3-kinases, most likely involving coreceptors such as neurotrophin receptors.


:

Pssm-ID: 259896  Cd Length: 130  Bit Score: 183.28  E-value: 6.76e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885197   27 RHVVYWNSSNPRLLRGDAVVELGLNDYLDIVCPHYEGPGPPEGPE-TFALYMVDWPGYESCQAeGPRAYKRWVCSLPF-- 103
Cdd:cd10425   2 RHAVYWNSSNNRFLRGDYTVQVQINDYLDILCPHYESSDPAGEEMeRYILYMVSEEGYETCSH-TDKGFKRWECNRPFap 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4885197  104 -GHVQFSEKIQRFTPFSLGFEFLPGETYYYISVPTPESSGQCLRLQVSVC 152
Cdd:cd10425  81 hGPIKFSEKFQRFTPFSLGFEFRPGHEYYYISKPIHNHRRSCLRLKVFVE 130
 
Name Accession Description Interval E-value
Ephrin-A_Ectodomain cd10425
Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell ...
 27-152 6.76e-60

Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin As contain a highly conserved receptor binding ectodomain described by this model. Although ephrin As do not have a cytoplasmic tail (in contrast to ephrin Bs), they are still capable of downstream activation of Src family kinases and phosphoinositide-3-kinases, most likely involving coreceptors such as neurotrophin receptors.


Pssm-ID: 259896  Cd Length: 130  Bit Score: 183.28  E-value: 6.76e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885197   27 RHVVYWNSSNPRLLRGDAVVELGLNDYLDIVCPHYEGPGPPEGPE-TFALYMVDWPGYESCQAeGPRAYKRWVCSLPF-- 103
Cdd:cd10425   2 RHAVYWNSSNNRFLRGDYTVQVQINDYLDILCPHYESSDPAGEEMeRYILYMVSEEGYETCSH-TDKGFKRWECNRPFap 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4885197  104 -GHVQFSEKIQRFTPFSLGFEFLPGETYYYISVPTPESSGQCLRLQVSVC 152
Cdd:cd10425  81 hGPIKFSEKFQRFTPFSLGFEFRPGHEYYYISKPIHNHRRSCLRLKVFVE 130
Ephrin pfam00812
Ephrin;
24-151 6.36e-53

Ephrin;


Pssm-ID: 459947  Cd Length: 139  Bit Score: 165.93  E-value: 6.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885197     24 SSLRHVVYWNSSNPRLLRGDAVVELGLNDYLDIVCPHYEGPGPPEGPE-TFALYMVDWPGYESCQAEGPrAYKRWVCSLP 102
Cdd:pfam00812   1 SADRHTVYWNSSNPRFRNGDYVIYVQIGDYLDIICPHYEPSGVGEANGeYYKLYLVSKEQYDTCTPTSK-DNKRWECDRP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885197    103 FGHVQFSEKIQRFTPFSLGFEFLPGETYYYISVPTPESSG-----------QCLRLQVSV 151
Cdd:pfam00812  80 DAPHKFTEKFQEFSPFPLGFEFQPGHDYYYISTSDGTLEGidsqhggvcetQNMKLKVKV 139
 
Name Accession Description Interval E-value
Ephrin-A_Ectodomain cd10425
Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell ...
 27-152 6.76e-60

Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin As contain a highly conserved receptor binding ectodomain described by this model. Although ephrin As do not have a cytoplasmic tail (in contrast to ephrin Bs), they are still capable of downstream activation of Src family kinases and phosphoinositide-3-kinases, most likely involving coreceptors such as neurotrophin receptors.


Pssm-ID: 259896  Cd Length: 130  Bit Score: 183.28  E-value: 6.76e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885197   27 RHVVYWNSSNPRLLRGDAVVELGLNDYLDIVCPHYEGPGPPEGPE-TFALYMVDWPGYESCQAeGPRAYKRWVCSLPF-- 103
Cdd:cd10425   2 RHAVYWNSSNNRFLRGDYTVQVQINDYLDILCPHYESSDPAGEEMeRYILYMVSEEGYETCSH-TDKGFKRWECNRPFap 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4885197  104 -GHVQFSEKIQRFTPFSLGFEFLPGETYYYISVPTPESSGQCLRLQVSVC 152
Cdd:cd10425  81 hGPIKFSEKFQRFTPFSLGFEFRPGHEYYYISKPIHNHRRSCLRLKVFVE 130
Ephrin pfam00812
Ephrin;
24-151 6.36e-53

Ephrin;


Pssm-ID: 459947  Cd Length: 139  Bit Score: 165.93  E-value: 6.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885197     24 SSLRHVVYWNSSNPRLLRGDAVVELGLNDYLDIVCPHYEGPGPPEGPE-TFALYMVDWPGYESCQAEGPrAYKRWVCSLP 102
Cdd:pfam00812   1 SADRHTVYWNSSNPRFRNGDYVIYVQIGDYLDIICPHYEPSGVGEANGeYYKLYLVSKEQYDTCTPTSK-DNKRWECDRP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885197    103 FGHVQFSEKIQRFTPFSLGFEFLPGETYYYISVPTPESSG-----------QCLRLQVSV 151
Cdd:pfam00812  80 DAPHKFTEKFQEFSPFPLGFEFQPGHDYYYISTSDGTLEGidsqhggvcetQNMKLKVKV 139
Ephrin_ectodomain cd02675
Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell ...
 27-152 1.40e-33

Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrins contain a highly conserved ectodomain for receptor binding, which is characterized by this domain hierarchy.


Pssm-ID: 259861  Cd Length: 136  Bit Score: 116.61  E-value: 1.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885197   27 RHVVYWNSSNPRLLRGDAVVELGLNDYLDIVCPHYEGPGPPEGPETFALYMVDWPGYESCQAEgPRAYKRWVCSLPFGHV 106
Cdd:cd02675   1 LPPIYWNSTNPIFDNGDYVIEVNIGDKLDIICPRYESGTESEEYEYYKIYMVSKDGYDSCRLN-TRSRLLLRCDRPYKEK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4885197  107 QFSEKIQRFTPFSLGFEFLPGETYYYISVPTPESSG-----------QCLRLQVSVC 152
Cdd:cd02675  80 KFTILFQEFSPIPGGLEFQPGKDYYFISTSTGTEEGldntsgglcssHNMKLAIKVC 136
Ephrin-B_Ectodomain cd10426
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ...
 30-156 2.24e-12

Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in their cytoplasmic PDZ-like domain, which are important for signal transduction. Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin Bs contain a highly conserved receptor binding ectodomain described in this model.


Pssm-ID: 259897  Cd Length: 137  Bit Score: 61.69  E-value: 2.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885197   30 VYWNSSNPRLLRGDAVV---ELGlnDYLDIVCPHyEGPGPPEGPETFALYMVDWPGYESCQAEGPRAyKRWVCSLPFGHV 106
Cdd:cd10426   5 IYWNSSNPKFLPGQGLVlypQIG--DKLDIICPK-VDSKTVGQYEYYKLYMVDKDQADRCSIKKDPN-PLLTCAKPDQDV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4885197  107 QFSEKIQRFTPFSLGFEFLPGETYYYISvpTPESSGQCLRLQVSVCCKER 156
Cdd:cd10426  81 RFTIKFQEFSPNLWGLEFQKNKDYYIIS--TSNGTLEGLENQEGGVCQTR 128
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH