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Protein

Ephrin type-B receptor 3

Gene

EPHB3

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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. 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. May control other aspects of development through regulation of cell migration and positioning (By similarity).By similarity

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei655ATPPROSITE-ProRule annotation1
Active sitei748Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi629 – 637ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:EPHB3
Synonyms:CEK10
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini‹1 – 534ExtracellularSequence analysisAdd BLAST›534
Transmembranei535 – 555HelicalSequence analysisAdd BLAST21
Topological domaini556 – 988CytoplasmicSequence analysisAdd BLAST433

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000160276‹1 – 988Ephrin type-B receptor 3Add BLAST›988

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi53 ↔ 171By similarity
Glycosylationi323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi418N-linked (GlcNAc...)Sequence analysis1
Modified residuei604Phosphotyrosine; by autocatalysisBy similarity1

Post-translational modificationi

Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-604 is required for interaction with SH2 domain-containing proteins (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ07498.

Expressioni

Tissue specificityi

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.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi9031.ENSGALP00000013896.

Structurei

3D structure databases

ProteinModelPortaliQ07498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 189Eph LBDPROSITE-ProRule annotationAdd BLAST179
Domaini311 – 424Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST114
Domaini425 – 522Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST98
Domaini623 – 886Protein kinasePROSITE-ProRule annotationAdd BLAST264
Domaini915 – 979SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi986 – 988PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi171 – 308Cys-richAdd BLAST138

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiQ07498.
PhylomeDBiQ07498.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
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]
PfamiPF14575. 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]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS51550. 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]

Sequences (2)i

Sequence statusi: Fragment.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q07498-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
GVSSRARRPP GSSRSSRRGV TSELAWTTHP ETGWEEVSGY DEAMNPIRTY
60 70 80 90 100
QVCNVREANQ NNWLRTKFIQ RQDVQRVYVE LKFTVRDCNS IPNIPGSCKE
110 120 130 140 150
TFNLFYYESD TDSASANSPF WMENPYIKVD TIAPDESFSK LESGRVNTKV
160 170 180 190 200
RSFGPLSKNG FYLAFQDLGA CMSLISVRAF YKKCSNTIAG FAIFPETLTG
210 220 230 240 250
AEPTSLVIAP GTCIPNAVEV SVPLKLYCNG DGEWMVPVGA CTCAAGYEPA
260 270 280 290 300
MKDTQCQACG PGTFKSKQGE GPCSPCPPNS RTTAGAATVC ICRSGFFRAD
310 320 330 340 350
ADPADSACTS VPSAPRSVIS NVNETSLVLE WSEPQDAGGR DDLLYNVICK
360 370 380 390 400
KCSVERRLCS RCDDNVEFVP RQLGLTGLTE RRIYISKVMA HPQYTFEIQA
410 420 430 440 450
VNGISSKSPY PPHFASVNIT TNQAAPSAVP TMHLHSSTGN SMTLSWTPPE
460 470 480 490 500
RPNGIILDYE IKYSEKQGQG DGIANTVTSQ KNSVRLDGLK ANARYMVQVR
510 520 530 540 550
ARTVAGYGRY SLPTEFQTTA EDGSTSKTFQ ELPLIVGSAT AGLLFVIVVV
560 570 580 590 600
IIAIVCFRKG MVTEQLLSSP LGRKQRNSTD PEYTEKLQQY VTPGMKVYID
610 620 630 640 650
PFTYEDPNEA VREFAKEIDI SCVKIEEVIG AGEFGEVCRG RLKLPGRREI
660 670 680 690 700
FVAIKTLKVG YTERQRRDFL SEASIMGQFD HPNIIHLEGV VTKSRPVMII
710 720 730 740 750
TEFMENCALD SFLRLNDGQF TVIQLVGMLR GIAAGMKYLS EMNYVHRDLA
760 770 780 790 800
ARNILVNSNL VCKVSDFGLS RFLEDDPADP TYTSSLGGKI PIRWTAPEAI
810 820 830 840 850
AYRKFTSASD VWSYGIVMWE VMSYGERPYW DMSNQDVINA VEQDYRLPPP
860 870 880 890 900
MDCPTALHQL MLDCWVRDRN LRPKFAQIVN TLDKLIRNAA SLKVIASVQS
910 920 930 940 950
GVSQPLLDRT VPDYTTFTTV GDWLDAIKMG RYKENFVNAG FASFDLVAQM
960 970 980
TAEDLLRIGV TLAGHQKKIL SSIQDMRLQM NQTLPVQV
Length:988
Mass (Da):109,579
Last modified:November 1, 1996 - v1
Checksum:iEEA0D39C03FFD3C8
GO
Isoform Short (identifier: Q07498-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     558-572: Missing.

Note: No experimental confirmation available.
Show »
Length:973
Mass (Da):107,981
Checksum:i533459035D7F9200
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003019558 – 572Missing in isoform Short. 1 PublicationAdd BLAST15

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19061 mRNA. Translation: CAA79511.1.
PIRiI50611.
UniGeneiGga.3053.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19061 mRNA. Translation: CAA79511.1.
PIRiI50611.
UniGeneiGga.3053.

3D structure databases

ProteinModelPortaliQ07498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000013896.

Proteomic databases

PaxDbiQ07498.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiQ07498.
PhylomeDBiQ07498.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
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]
PfamiPF14575. 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]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS51550. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiEPHB3_CHICK
AccessioniPrimary (citable) accession number: Q07498
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.