General Information of Binding Target of SBP (BTS) (ID: ST00306)
BTS Name
Ephrin type-A receptor 2
Synonyms
EC 2.7.10.1; Epithelial cell kinase; Tyrosine-protein kinase receptor ECK; Tyrosine-protein kinase receptor MPK-5; Tyrosine-protein kinase receptor SEK-2
BTS Type
Protein
Family
Protein kinase superfamily;
Tyr protein kinase family;
Ephrin receptor subfamily
Gene Name
Epha2
Organism
Mus musculus (Mouse)
Function
Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.
UniProt ID
Q03145
UniProt Entry
EPHA2_MOUSE
PFam
PF14575 ; PF01404 ; PF00041 ; PF07714 ; PF00536
Gene ID
13836
Sequence
MELRAVGFCLALLWGCALAAAAAQGKEVVLLDFAAMKGELGWLTHPYGKGWDLMQNIMDD
MPIYMYSVCNVVSGDQDNWLRTNWVYREEAERIFIELKFTVRDCNSFPGGASSCKETFNL
YYAESDVDYGTNFQKRQFTKIDTIAPDEITVSSDFEARNVKLNVEERMVGPLTRKGFYLA
FQDIGACVALLSVRVYYKKCPEMLQSLARFPETIAVAVSDTQPLATVAGTCVDHAVVPYG
GEGPLMHCTVDGEWLVPIGQCLCQEGYEKVEDACRACSPGFFKSEASESPCLECPEHTLP
STEGATSCQCEEGYFRAPEDPLSMSCTRPPSAPNYLTAIGMGAKVELRWTAPKDTGGRQD
IVYSVTCEQCWPESGECGPCEASVRYSEPPHALTRTSVTVSDLEPHMNYTFAVEARNGVS
GLVTSRSFRTASVSINQTEPPKVRLEDRSTTSLSVTWSIPVSQQSRVWKYEVTYRKKGDA
NSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSTEGSANMAVIG
GVAVGVVLLLVLAGVGLFIHRRRRNLRARQSSEDVRFSKSEQLKPLKTYVDPHTYEDPNQ
AVLKFTTEIHPSCVARQKVIGAGEFGEVYKGTLKASSGKKEIPVAIKTLKAGYTEKQRVD
FLSEASIMGQFSHHNIIRLEGVVSKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGM
LRGIASGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKI
PIRWTAPEAISYRKFTSASDVWSYGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTP
MDCPSAIYQLMMQCWQQERSRRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTS
GSEGVPFRTVSEWLESIKMQQYTEHFMVAGYTAIEKVVQMSNEDIKRIGVRLPGHQKRIA
YSLLGLKDQVNTVGIPI
Sequence Length
977
Synthetic Binding Protein (SBP) Targeting This BTS
SBP Name Highest Status Mechanism Affinity Application Details Ref
VNAR anti-EphA2 mmE1 Research Binder Kd: 368 nM Research tool
SBP Info
[1]
VNAR anti-EphA2 mmE2 Research Binder Kd: 482 nM Research tool
SBP Info
[1]
References
1 Shark Attack: high affinity binding proteins derived from shark vNAR domains by stepwise in vitro affinity maturation. J Biotechnol. 2014 Dec 10;191:236-45.