Ephrin type-B receptor 3

UniProt data

UniProt name: EPHB3_HUMAN (P54753)

Gene name: EPHB3; Synonyms=ETK2, HEK2, TYRO6

Organism: Homo sapiens (Human).

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. {ECO:0000269|PubMed:15536074}.

Subcellular location: Cell membrane {ECO:0000269|PubMed:15536074}; Single-pass type I membrane protein {ECO:0000269|PubMed:15536074}. Cell projection, dendrite {ECO:0000250}.

Transmembrane domains:

  1. 560-580, 21 AA, Helical. {ECO:0000255}.

Sequence: 998 AA

10 20 30 40 50 60 MARARPPPPP SPPPGLLPLL PPLLLLPLLL LPAGCRALEE TLMDTKWVTS ELAWTSHPES 70 80 90 100 110 120 GWEEVSGYDE AMNPIRTYQV CNVRESSQNN WLRTGFIWRR DVQRVYVELK FTVRDCNSIP 130 140 150 160 170 180 NIPGSCKETF NLFYYEADSD VASASSPFWM ENPYVKVDTI APDESFSRLD AGRVNTKVRS 190 200 210 220 230 240 FGPLSKAGFY LAFQDQGACM SLISVRAFYK KCASTTAGFA LFPETLTGAE PTSLVIAPGT 250 260 270 280 290 300 CIPNAVEVSV PLKLYCNGDG EWMVPVGACT CATGHEPAAK ESQCRPCPPG SYKAKQGEGP 310 320 330 340 350 360 CLPCPPNSRT TSPAASICTC HNNFYRADSD SADSACTTVP SPPRGVISNV NETSLILEWS 370 380 390 400 410 420 EPRDLGGRDD LLYNVICKKC HGAGGASACS RCDDNVEFVP RQLGLTERRV HISHLLAHTR 430 440 450 460 470 480 YTFEVQAVNG VSGKSPLPPR YAAVNITTNQ AAPSEVPTLR LHSSSGSSLT LSWAPPERPN 490 500 510 520 530 540 GVILDYEMKY FEKSEGIAST VTSQMNSVQL DGLRPDARYV VQVRARTVAG YGQYSRPAEF 550 560 570 580 590 600 ETTSERGSGA QQLQEQLPLI VGSATAGLVF VVAVVVIAIV CLRKQRHGSD SEYTEKLQQY 610 620 630 640 650 660 IAPGMKVYID PFTYEDPNEA VREFAKEIDV SCVKIEEVIG AGEFGEVCRG RLKQPGRREV 670 680 690 700 710 720 FVAIKTLKVG YTERQRRDFL SEASIMGQFD HPNIIRLEGV VTKSRPVMIL TEFMENCALD 730 740 750 760 770 780 SFLRLNDGQF TVIQLVGMLR GIAAGMKYLS EMNYVHRDLA ARNILVNSNL VCKVSDFGLS 790 800 810 820 830 840 RFLEDDPSDP TYTSSLGGKI PIRWTAPEAI AYRKFTSASD VWSYGIVMWE VMSYGERPYW 850 860 870 880 890 900 DMSNQDVINA VEQDYRLPPP MDCPTALHQL MLDCWVRDRN LRPKFSQIVN TLDKLIRNAA 910 920 930 940 950 960 SLKVIASAQS GMSQPLLDRT VPDYTTFTTV GDWLDAIKMG RYKESFVSAG FASFDLVAQM 970 980 990 TAEDLLRIGV TLAGHQKKIL SSIQDMRLQM NQTLPVQV

CATM prediction

The sequence of EPHB3_HUMAN returned 3 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
     560       570       580 
   |    +    |    +    |   		 (Å) (°) (Å) (°)  
Model 1 LALIVGSATAGLVFVVAVVVIAIVCLR 7.3 -35.0° 5.0 35.0 -21.3
Model 2 LALIVGSATAGLVFVVAVVVIAIVCLR 7.1 -55.0° 0.9 50.0 -10.2
Model 3 LALIVGSATAGLVFVVAVVVIAIVCLR 7.3 -54.0° 3.6 49.1 -9.0
Prolines* LPLIVGSATAGLVFVVAVVVIAIVCLR          

* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


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Download model 1 structure: PDB, PyMOL session