Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q91735 (EPHB3_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length974 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 projectiondendrite 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 processNeurogenesis
   Cellular componentCell membrane
Cell projection
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Gene Ontology (GO)
   Biological processaxon 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 componentdendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 974958Ephrin type-B receptor 3
PRO_0000016833

Regions

Topological domain17 – 534518Extracellular Potential
Transmembrane535 – 55521Helical; Potential
Topological domain556 – 974419Cytoplasmic Potential
Domain18 – 196179Eph LBD
Domain319 – 418100Fibronectin type-III 1
Domain424 – 51895Fibronectin type-III 2
Domain609 – 872264Protein kinase
Domain901 – 96565SAM
Nucleotide binding615 – 6239ATP By similarity
Motif972 – 9743PDZ-binding Potential
Compositional bias178 – 315138Cys-rich

Sites

Active site7341Proton acceptor By similarity
Binding site6411ATP By similarity

Amino acid modifications

Modified residue5901Phosphotyrosine; by autocatalysis By similarity
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation4201N-linked (GlcNAc...) Potential
Disulfide bond60 ↔ 178 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91735 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F881412E86628533

FASTA974108,264
        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 

« Hide

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.
RefSeqNP_001081434.1. NM_001087965.1.
UniGeneXl.1027.

3D structure databases

ProteinModelPortalQ91735.
SMRQ91735. Positions 17-193, 582-879, 890-969.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397834.
KEGGxla:397834.

Organism-specific databases

CTD2049.

Phylogenomic databases

HOVERGENHBG062180.

Enzyme and pathway databases

BRENDA2.7.10.1. 6726.

Family and domain databases

InterProIPR001090. 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]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 2 hits.
G3DSA:1.10.150.50. SAM_type. 1 hit.
KOK05112.
PfamPF01404. 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]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. 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.
PROSITEPS51550. 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]
ProtoNetSearch...

Entry information

Entry nameEPHB3_XENLA
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families