描述:
EphA5, also known as Ehk1, Bsk, Cek7, Hek7, and Rek7, is a member of the Eph receptor
tyrosine kinase family which binds members of the Ephrin ligand family. The A and B class
Eph proteins have a common structural organization. Activation of kinase activity occurs after
membranebound or clustered ligand recognition and binding. Reverse signaling is propagated
through the Ephrin ligand. The human EphA5 cDNA encodes a 1037 amino acid (aa) precursor
including a 24 aa signal sequence, a 549 aa extracellular domain (ECD), a 21 aa transmembrane
segment, and a 443 aa cytoplasmic domain. The ECD contains an N-terminal globular domain,
a cysteinerich domain, and two fibronectin type III domains. The cytoplasmic domain contains
a juxtamembrane motif with two tyrosine residues, which are the major autophosphorylation
sites, a kinase domain, and a conserved sterile alpha motif (SAM). Multiple splice variants of
human EphA5 are produced in brain and differ in their extracellular and cytoplasmic sequences.
Taking into account differences in splice variants between species, comparable regions of the
human EphA5 ECD share greater than 96% aa sequence identity with bovine, mouse, and rat
EphA5, approximately 40% aa identity with human EphA1 and EphA2, and 54-61% aa identity
with human EphA3, 4, 7, and 8. EphA5 is widely expressed in neurons of the adult human CNS,
with the exception of few areas such as the substantia nigra. In rat, the expression of EphA5
during embryogenesis suggests a role in the development of CNS neurons.
原厂资料:
EphA5, also known as Ehk1, Bsk, Cek7, Hek7, and Rek7, is a member of the Eph receptor
tyrosine kinase family which binds members of the Ephrin ligand family. The A and B class
Eph proteins have a common structural organization. Activation of kinase activity occurs after
membranebound or clustered ligand recognition and binding. Reverse signaling is propagated
through the Ephrin ligand. The human EphA5 cDNA encodes a 1037 amino acid (aa) precursor
including a 24 aa signal sequence, a 549 aa extracellular domain (ECD), a 21 aa transmembrane
segment, and a 443 aa cytoplasmic domain. The ECD contains an N-terminal globular domain,
a cysteinerich domain, and two fibronectin type III domains. The cytoplasmic domain contains
a juxtamembrane motif with two tyrosine residues, which are the major autophosphorylation
sites, a kinase domain, and a conserved sterile alpha motif (SAM). Multiple splice variants of
human EphA5 are produced in brain and differ in their extracellular and cytoplasmic sequences.
Taking into account differences in splice variants between species, comparable regions of the
human EphA5 ECD share greater than 96% aa sequence identity with bovine, mouse, and rat
EphA5, approximately 40% aa identity with human EphA1 and EphA2, and 54-61% aa identity
with human EphA3, 4, 7, and 8. EphA5 is widely expressed in neurons of the adult human CNS,
with the exception of few areas such as the substantia nigra. In rat, the expression of EphA5
during embryogenesis suggests a role in the development of CNS neurons.