Q91735 (EPHB3_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ephrin type-B receptor 3
EC=2.7.10.1

Alternative name(s):
Tyrosine-protein kinase receptor TCK

Gene names

Name:	ephb3
Synonyms:	tck

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	974 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

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. Beside 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. May control other aspects of development through regulation of cell migration and positioning By similarity.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	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.
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity. Cell projection › dendrite By similarity.
Tissue specificity	Expressed in the embryo in pre-somitic mesoderm, caudal somites, midbrain, and cement gland. Most abundant in adult brain, eye, heart, lung and ovary. Lower levels in intestine, kidney, oviduct and pharynx.
Developmental stage	Expressed during early development.
Post-translational modification	Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-590 is required for interaction with SH2 domain-containing proteins By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily. Contains 1 Eph LBD (Eph ligand-binding) domain. Contains 2 fibronectin type-III domains. Contains 1 protein kinase domain. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Neurogenesis
Cellular component	Cell membrane Cell projection Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	axon guidance Inferred from sequence or structural similarity. Source: UniProtKB axonal fasciculation Inferred from sequence or structural similarity. Source: UniProtKB cell migration Inferred from sequence or structural similarity. Source: UniProtKB dendritic spine morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of synapse assembly Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of Cdc42 GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of Rac GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell-cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB substrate adhesion-dependent cell spreading Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	dendrite Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ephrin receptor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Chain	17 – 974	958	Ephrin type-B receptor 3		PRO_0000016833
Regions
	Topological domain	17 – 534	518	Extracellular Potential
	Transmembrane	535 – 555	21	Helical; Potential
	Topological domain	556 – 974	419	Cytoplasmic Potential
	Domain	18 – 196	179	Eph LBD
	Domain	319 – 418	100	Fibronectin type-III 1
	Domain	424 – 518	95	Fibronectin type-III 2
	Domain	609 – 872	264	Protein kinase
	Domain	901 – 965	65	SAM
	Nucleotide binding	615 – 623	9	ATP By similarity
	Motif	972 – 974	3	PDZ-binding Potential
	Compositional bias	178 – 315	138	Cys-rich
Sites
	Active site	734	1	Proton acceptor By similarity
	Binding site	641	1	ATP By similarity
Amino acid modifications
	Modified residue	590	1	Phosphotyrosine; by autocatalysis By similarity
	Glycosylation	330	1	N-linked (GlcNAc...) Potential
	Glycosylation	420	1	N-linked (GlcNAc...) Potential
	Disulfide bond	60 ↔ 178		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q91735 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F881412E86628533	FASTA	974	108,264
	10 20 30 40 50 60 MLPAVFVILA LSAVQGLEET LMDTKWTTSE LAWVAYPDSG WEEVSGYDEA SNPIRTYQVC 70 80 90 100 110 120 NVRDSNQNNW LRTQFIPRQD VQRVYVELKF TVRDCNSLPN LRGSCKETFN FFYYESDSDS 130 140 150 160 170 180 ASADSPFWME NPYIKVDTIA PDESFSRRDS GRVNTKIRSF GPISRAGFYL AFQDLGACVS 190 200 210 220 230 240 LISVRVFFKK CPRTTAGFAS FPETITGAEP TSLVIAPGTC VPNALEVSVP LKLYCNGDGD 250 260 270 280 290 300 WMVPVGACTC AAGFEPAGKD TQCQACKRGT YKSKQGEGSC MPCPANSRAI SSAATICSCQ 310 320 330 340 350 360 NGYYRADGES AETACTSVPS APRQVISNVN ETSVVLEWAE PGHLGGRDDV LYNVICKKCL 370 380 390 400 410 420 ERLCSRCDDN VQFWPRQLGV TQRLVSVSHL QAHTKYSFEI QAVNGVSGKS PHIPNYFTVN 430 440 450 460 470 480 ITTNQAAPSS VPMVQSHGSL ANSLTLSWAP PESPNGIILD YEIKYYAKGH IGAGNTVTSQ 490 500 510 520 530 540 RTTVRMEGMT PDTVYVVQVR ARTVAGYGAY SEPREFQTIA EDGDRSSLQE QVPMVVGSVT 550 560 570 580 590 600 AGLIFIIAVV IIVIVCFSRK QRNDSESEYT EKLQQYMVPG MKLYIDPFTY EDPNEAVRDF 610 620 630 640 650 660 AKEIDISCVK IEEVIGAGEF GEVCRGKLKQ AGRREQFVAI KTLKAGYTEQ QRRDFLGEAS 670 680 690 700 710 720 IMGQFDHPNI IRLEGVVTRS RPVMILTEFM ENGALDSFLR MNDGQFTVIQ LVGILRGIAS 730 740 750 760 770 780 GMKYLSEMNY VHRDLAARNI LVNSNLVCKV SDFGLSRFLE NSRSDPTYTS ALGGKIPIRW 790 800 810 820 830 840 TAPEAISYRK FTSASDVWSY GIVMWEVMSY GERPYWDMSN QDVINAIEQD YRLPPPMDCP 850 860 870 880 890 900 SALHQLMLDC WLRDRNLRPK FSQIVSSLDK LIRNAASLKV TSPGQAGVSQ QLLDRTVPDY 910 920 930 940 950 960 TTFPTVSDWL EAIKMGQYQE NFLSAGFTSF HLVAQMTAED LLRIGVTLAG HQKKLLNSVQ 970 DMRLQMSQTL PVQV

References

[1]	"Novel members of the eph receptor tyrosine kinase subfamily expressed during Xenopus development." Scales J.B., Winning R.S., Renaud C.S., Shea L.J., Sargent T.D. Oncogene 11:1745-1752(1995) [PubMed: 7478602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L43620 mRNA. Translation: AAA93526.1.
RefSeq	NP_001081434.1. NM_001087965.1.
UniGene	Xl.1027.
3D structure databases
ProteinModelPortal	Q91735.
SMR	Q91735. Positions 17-193, 582-879, 890-969.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397834.
KEGG	xla:397834.
Organism-specific databases
CTD	2049.
Phylogenomic databases
HOVERGEN	HBG062180.
Enzyme and pathway databases
BRENDA	2.7.10.1. 6726.
Family and domain databases
InterPro	IPR001090. Ephrin_rcpt_lig-bd. IPR003961. Fibronectin_type3. IPR008979. Galactose-bd-like. IPR009030. Growth_fac_rcpt. IPR013783. Ig-like_fold. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001660. SAM. IPR013761. SAM/pointed. IPR011510. SAM_2. IPR001245. Ser-Thr/Tyr_kinase. IPR011641. Tyr-kin_ephrin_A/B_rcpt-like. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. IPR016257. Tyr_kinase_ephrin_rcpt. IPR001426. Tyr_kinase_rcpt_V_CS. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 2 hits. G3DSA:1.10.150.50. SAM_type. 1 hit.
KO	K05112.
Pfam	PF01404. Ephrin_lbd. 1 hit. PF00041. fn3. 2 hits. PF07699. GCC2_GCC3. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF07647. SAM_2. 1 hit. [Graphical view]
PIRSF	PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTS	PR00109. TYRKINASE.
SMART	SM00615. EPH_lbd. 1 hit. SM00060. FN3. 2 hits. SM00454. SAM. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 2 hits. SSF49785. Gal_bind_like. 1 hit. SSF57184. Grow_fac_recept. 1 hit. SSF56112. Kinase_like. 1 hit. SSF47769. SAM_homology. 1 hit.
PROSITE	PS51550. EPH_LBD. 1 hit. PS50853. FN3. 2 hits. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit. PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit. PS50105. SAM_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EPHB3_XENLA

Accession

Primary (citable) accession number: Q91735

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program