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 mouse EphA5 cDNA encodes an 877 amino acid
(aa) precursor that includes a 26 aa signal sequence, a 386 aa extracellular domain (ECD), a
21 aa transmembrane segment, and a 444 aa cytoplasmic domain. The ECD contains an
Nterminal globular domain, a cysteine-rich 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). Taking into account differences in splice variants between species, comparable
regions of the mouse EphA5 ECD share greater than 97% aa sequence identity with bovine,
human, and rat EphA5, and 27-43% aa identity withmouse EphA1, 2, 3, 4, 6, 7, and 8. Multiple
EphA5 splice variants exist and differ in their extracellular and intracellular sequences. Mouse
EphA5 is expressed exclusively in brain with the highest levels in the hippocampus and limbic
system. During embryonal development, EphA5 is preferentially expressed in neurons
migrating away from the ventricular zone. The interaction of EphA5 with its ligands is also
involved in the topographic projection of hippocampal, olfactory, and retinotectal neurons.
Interference in this system by the transgenic expression of soluble EphA5 implicates
hippocampal postsynaptic areas for native EphA5 function.
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 mouse EphA5 cDNA encodes an 877 amino acid
(aa) precursor that includes a 26 aa signal sequence, a 386 aa extracellular domain (ECD), a
21 aa transmembrane segment, and a 444 aa cytoplasmic domain. The ECD contains an
Nterminal globular domain, a cysteine-rich 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). Taking into account differences in splice variants between species, comparable
regions of the mouse EphA5 ECD share greater than 97% aa sequence identity with bovine,
human, and rat EphA5, and 27-43% aa identity withmouse EphA1, 2, 3, 4, 6, 7, and 8. Multiple
EphA5 splice variants exist and differ in their extracellular and intracellular sequences. Mouse
EphA5 is expressed exclusively in brain with the highest levels in the hippocampus and limbic
system. During embryonal development, EphA5 is preferentially expressed in neurons
migrating away from the ventricular zone. The interaction of EphA5 with its ligands is also
involved in the topographic projection of hippocampal, olfactory, and retinotectal neurons.
Interference in this system by the transgenic expression of soluble EphA5 implicates
hippocampal postsynaptic areas for native EphA5 function.
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