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Q07498 (EPHB3_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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·Alt products·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):
EPH-like kinase 10
Short name=EK10
Short name=cEK10
Gene names
Name:EPHB3
Synonyms:CEK10
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length988 AA.
Sequence statusFragment.
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

Present in 10-day embryonic brain and body tissues. Prominent expression in kidney. Lower expression in lung, and barely detectable in brain, liver, heart, skeletal muscle and thymus.

Post-translational modification

Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-604 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
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
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 development

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

ephrin receptor signaling pathway

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 component of 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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q07498-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: Q07498-2)

The sequence of this isoform differs from the canonical sequence as follows:
     558-572: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 988›988Ephrin type-B receptor 3
PRO_0000160276

Regions

Topological domain‹1 – 534›534Extracellular Potential
Transmembrane535 – 55521Helical; Potential
Topological domain556 – 988433Cytoplasmic Potential
Domain11 – 189179Eph LBD
Domain311 – 424114Fibronectin type-III 1
Domain425 – 52298Fibronectin type-III 2
Domain623 – 886264Protein kinase
Domain915 – 97965SAM
Nucleotide binding629 – 6379ATP By similarity
Motif986 – 9883PDZ-binding Potential
Compositional bias171 – 308138Cys-rich

Sites

Active site7481Proton acceptor By similarity
Binding site6551ATP By similarity

Amino acid modifications

Modified residue6041Phosphotyrosine; by autocatalysis By similarity
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation4181N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 171 By similarity

Natural variations

Alternative sequence558 – 57215Missing in isoform Short.
VSP_003019

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EEA0D39C03FFD3C8

FASTA988109,579
        10         20         30         40         50         60 
GVSSRARRPP GSSRSSRRGV TSELAWTTHP ETGWEEVSGY DEAMNPIRTY QVCNVREANQ 

        70         80         90        100        110        120 
NNWLRTKFIQ RQDVQRVYVE LKFTVRDCNS IPNIPGSCKE TFNLFYYESD TDSASANSPF 

       130        140        150        160        170        180 
WMENPYIKVD TIAPDESFSK LESGRVNTKV RSFGPLSKNG FYLAFQDLGA CMSLISVRAF 

       190        200        210        220        230        240 
YKKCSNTIAG FAIFPETLTG AEPTSLVIAP GTCIPNAVEV SVPLKLYCNG DGEWMVPVGA 

       250        260        270        280        290        300 
CTCAAGYEPA MKDTQCQACG PGTFKSKQGE GPCSPCPPNS RTTAGAATVC ICRSGFFRAD 

       310        320        330        340        350        360 
ADPADSACTS VPSAPRSVIS NVNETSLVLE WSEPQDAGGR DDLLYNVICK KCSVERRLCS 

       370        380        390        400        410        420 
RCDDNVEFVP RQLGLTGLTE RRIYISKVMA HPQYTFEIQA VNGISSKSPY PPHFASVNIT 

       430        440        450        460        470        480 
TNQAAPSAVP TMHLHSSTGN SMTLSWTPPE RPNGIILDYE IKYSEKQGQG DGIANTVTSQ 

       490        500        510        520        530        540 
KNSVRLDGLK ANARYMVQVR ARTVAGYGRY SLPTEFQTTA EDGSTSKTFQ ELPLIVGSAT 

       550        560        570        580        590        600 
AGLLFVIVVV IIAIVCFRKG MVTEQLLSSP LGRKQRNSTD PEYTEKLQQY VTPGMKVYID 

       610        620        630        640        650        660 
PFTYEDPNEA VREFAKEIDI SCVKIEEVIG AGEFGEVCRG RLKLPGRREI FVAIKTLKVG 

       670        680        690        700        710        720 
YTERQRRDFL SEASIMGQFD HPNIIHLEGV VTKSRPVMII TEFMENCALD SFLRLNDGQF 

       730        740        750        760        770        780 
TVIQLVGMLR GIAAGMKYLS EMNYVHRDLA ARNILVNSNL VCKVSDFGLS RFLEDDPADP 

       790        800        810        820        830        840 
TYTSSLGGKI PIRWTAPEAI AYRKFTSASD VWSYGIVMWE VMSYGERPYW DMSNQDVINA 

       850        860        870        880        890        900 
VEQDYRLPPP MDCPTALHQL MLDCWVRDRN LRPKFAQIVN TLDKLIRNAA SLKVIASVQS 

       910        920        930        940        950        960 
GVSQPLLDRT VPDYTTFTTV GDWLDAIKMG RYKENFVNAG FASFDLVAQM TAEDLLRIGV 

       970        980 
TLAGHQKKIL SSIQDMRLQM NQTLPVQV 

« Hide

Isoform Short [UniParc].

Checksum: 533459035D7F9200
Show »

FASTA973107,981

References

[1]"Five novel avian Eph-related tyrosine kinases are differentially expressed."
Sajjadi F.G., Pasquale E.B.
Oncogene 8:1807-1813(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z19061 mRNA. Translation: CAA79511.1.
PIRI50611.
UniGeneGga.3053.

3D structure databases

ProteinModelPortalQ07498.
SMRQ07498. Positions 21-184, 596-893, 904-983.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000013896.

Proteomic databases

PaxDbQ07498.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
PhylomeDBQ07498.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 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]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
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_CHICK
AccessionPrimary (citable) accession number: Q07498
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 133 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