EPHB3_HUMAN » Ephrin type-B receptor 3

EPHB3_HUMAN » Ephrin type-B receptor 3
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
EPHB3_HUMAN » Ephrin type-B receptor 3 » EPH-like tyrosine kinase 2;EPH-like kinase 2; Embryonic kinase 2;EK2; hEK2; Tyrosine-protein kinase TYRO6;
Hydrophobic Thickness 35.2 ± 2.0 Å
Tilt Angle 0 ± 2°
ΔGtransfer -48.8 kcal/mol
ΔGfold -19.2 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 559-584 (556-586)
Pathways

Axon guidance (KEGG)

PDB 3p1i (39-211), 3zfy (616-910)
OPM none
Complexes none
Interactions

ALK, Complex: ALK:EPHB3, PubMed

EFNB3, Complex: EPHB3:EFNB3, PubMed

RYK, Complex: RYK:EPHB3, PubMed

Domains

AA: 40-212, PDBID: 3P1I, Subunit A, Seq Identity:100%, Ephrin receptor ligand binding domain

AA: 277-320, Putative ephrin-receptor like

AA: 341-437, PDBID: 4BK4, Subunit A, Seq Identity:48%, Fibronectin type III domain

AA: 454-535, PDBID: 2DJS, Subunit A, Seq Identity:48%, Fibronectin type III domain

AA: 560-630, PDBID: 2VWU, Subunit A, Seq Identity:67%, Ephrin type-A receptor 2 transmembrane domain

AA: 633-892, PDBID: 3ZFY, Subunit B, Seq Identity:100%, Protein tyrosine kinase

AA: 923-987, PDBID: 1SGG, Subunit A, Seq Identity:76%, SAM domain (Sterile alpha motif)

UniProt annotation for EPHB3_HUMAN » Ephrin type-B receptor 3
FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B 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. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt.

CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity).

TISSUE SPECIFICITY: Ubiquitous.

UniProt features for EPHB3_HUMAN » Ephrin type-B receptor 3
SIGNAL 1 33 Potential.
CHAIN 34 998 Ephrin type-B receptor 3.
DOMAIN 39 217 Eph LBD.
DOMAIN 340 443 Fibronectin type-III 1.
DOMAIN 453 544 Fibronectin type-III 2.
DOMAIN 633 896 Protein kinase.
DOMAIN 925 989 SAM.
MOTIF 996 998 PDZ-binding (Potential).
ACT_SITE 758 758 Proton acceptor (By similarity).
DISULFID 81 199
Amino Acid Sequence for EPHB3_HUMAN » Ephrin type-B receptor 3
MARARPPPPP SPPPGLLPLL PPLLLLPLLL LPAGCRALEE TLMDTKWVTS ELAWTSHPES GWEEVSGYDE AMNPIRTYQV CNVRESSQNN WLRTGFIWRR DVQRVYVELK FTVRDCNSIP NIPGSCKETF NLFYYEADSD VASASSPFWM ENPYVKVDTI APDESFSRLD AGRVNTKVRS FGPLSKAGFY LAFQDQGACM SLISVRAFYK KCASTTAGFA LFPETLTGAE PTSLVIAPGT CIPNAVEVSV PLKLYCNGDG EWMVPVGACT CATGHEPAAK ESQCRPCPPG SYKAKQGEGP CLPCPPNSRT TSPAASICTC HNNFYRADSD SADSACTTVP SPPRGVISNV NETSLILEWS EPRDLGGRDD LLYNVICKKC HGAGGASACS RCDDNVEFVP RQLGLTERRV HISHLLAHTR YTFEVQAVNG VSGKSPLPPR YAAVNITTNQ AAPSEVPTLR LHSSSGSSLT LSWAPPERPN GVILDYEMKY FEKSEGIAST VTSQMNSVQL DGLRPDARYV VQVRARTVAG YGQYSRPAEF ETTSERGSGA QQLQEQLPLI VGSATAGLVF VVAVVVIAIV CLRKQRHGSD SEYTEKLQQY IAPGMKVYID PFTYEDPNEA VREFAKEIDV SCVKIEEVIG AGEFGEVCRG RLKQPGRREV FVAIKTLKVG YTERQRRDFL SEASIMGQFD HPNIIRLEGV VTKSRPVMIL TEFMENCALD SFLRLNDGQF TVIQLVGMLR GIAAGMKYLS EMNYVHRDLA ARNILVNSNL VCKVSDFGLS RFLEDDPSDP TYTSSLGGKI PIRWTAPEAI AYRKFTSASD VWSYGIVMWE VMSYGERPYW DMSNQDVINA VEQDYRLPPP MDCPTALHQL MLDCWVRDRN LRPKFSQIVN TLDKLIRNAA SLKVIASAQS GMSQPLLDRT VPDYTTFTTV GDWLDAIKMG RYKESFVSAG FASFDLVAQM TAEDLLRIGV TLAGHQKKIL SSIQDMRLQM NQTLPVQV