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Protein

Ephrin type-B receptor 3

Gene

ephb3

Organism
Xenopus laevis (African clawed frog)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei641 – 6411ATPPROSITE-ProRule annotation
Active sitei734 – 7341Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi615 – 6239ATPPROSITE-ProRule annotation

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

Enzyme and pathway databases

BRENDAi2.7.10.1. 6725.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 3 (EC:2.7.10.1)
Alternative name(s):
Tyrosine-protein kinase receptor TCK
Gene namesi
Name:ephb3
Synonyms:tck
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 534518ExtracellularSequence analysisAdd
BLAST
Transmembranei535 – 55521HelicalSequence analysisAdd
BLAST
Topological domaini556 – 974419CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 974958Ephrin type-B receptor 3PRO_0000016833Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi60 ↔ 178By similarity
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence analysis
Glycosylationi420 – 4201N-linked (GlcNAc...)Sequence analysis
Modified residuei590 – 5901Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-590 is required for interaction with SH2 domain-containing proteins (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Expressioni

Tissue specificityi

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 stagei

Expressed during early development.

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

Structurei

3D structure databases

ProteinModelPortaliQ91735.
SMRiQ91735. Positions 17-193, 582-879, 890-969.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 196179Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini318 – 426109Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini427 – 52296Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini609 – 872264Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini901 – 96565SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi972 – 9743PDZ-bindingSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi178 – 315138Cys-richAdd
BLAST

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, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG062180.
KOiK05112.

Family and domain databases

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.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91735-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPAVFVILA LSAVQGLEET LMDTKWTTSE LAWVAYPDSG WEEVSGYDEA
60 70 80 90 100
SNPIRTYQVC NVRDSNQNNW LRTQFIPRQD VQRVYVELKF TVRDCNSLPN
110 120 130 140 150
LRGSCKETFN FFYYESDSDS ASADSPFWME NPYIKVDTIA PDESFSRRDS
160 170 180 190 200
GRVNTKIRSF GPISRAGFYL AFQDLGACVS LISVRVFFKK CPRTTAGFAS
210 220 230 240 250
FPETITGAEP TSLVIAPGTC VPNALEVSVP LKLYCNGDGD WMVPVGACTC
260 270 280 290 300
AAGFEPAGKD TQCQACKRGT YKSKQGEGSC MPCPANSRAI SSAATICSCQ
310 320 330 340 350
NGYYRADGES AETACTSVPS APRQVISNVN ETSVVLEWAE PGHLGGRDDV
360 370 380 390 400
LYNVICKKCL ERLCSRCDDN VQFWPRQLGV TQRLVSVSHL QAHTKYSFEI
410 420 430 440 450
QAVNGVSGKS PHIPNYFTVN ITTNQAAPSS VPMVQSHGSL ANSLTLSWAP
460 470 480 490 500
PESPNGIILD YEIKYYAKGH IGAGNTVTSQ RTTVRMEGMT PDTVYVVQVR
510 520 530 540 550
ARTVAGYGAY SEPREFQTIA EDGDRSSLQE QVPMVVGSVT AGLIFIIAVV
560 570 580 590 600
IIVIVCFSRK QRNDSESEYT EKLQQYMVPG MKLYIDPFTY EDPNEAVRDF
610 620 630 640 650
AKEIDISCVK IEEVIGAGEF GEVCRGKLKQ AGRREQFVAI KTLKAGYTEQ
660 670 680 690 700
QRRDFLGEAS IMGQFDHPNI IRLEGVVTRS RPVMILTEFM ENGALDSFLR
710 720 730 740 750
MNDGQFTVIQ LVGILRGIAS GMKYLSEMNY VHRDLAARNI LVNSNLVCKV
760 770 780 790 800
SDFGLSRFLE NSRSDPTYTS ALGGKIPIRW TAPEAISYRK FTSASDVWSY
810 820 830 840 850
GIVMWEVMSY GERPYWDMSN QDVINAIEQD YRLPPPMDCP SALHQLMLDC
860 870 880 890 900
WLRDRNLRPK FSQIVSSLDK LIRNAASLKV TSPGQAGVSQ QLLDRTVPDY
910 920 930 940 950
TTFPTVSDWL EAIKMGQYQE NFLSAGFTSF HLVAQMTAED LLRIGVTLAG
960 970
HQKKLLNSVQ DMRLQMSQTL PVQV
Length:974
Mass (Da):108,264
Last modified:November 1, 1996 - v1
Checksum:iF881412E86628533
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43620 mRNA. Translation: AAA93526.1.
RefSeqiNP_001081434.1. NM_001087965.1.
UniGeneiXl.1027.

Genome annotation databases

GeneIDi397834.
KEGGixla:397834.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43620 mRNA. Translation: AAA93526.1.
RefSeqiNP_001081434.1. NM_001087965.1.
UniGeneiXl.1027.

3D structure databases

ProteinModelPortaliQ91735.
SMRiQ91735. Positions 17-193, 582-879, 890-969.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397834.
KEGGixla:397834.

Organism-specific databases

CTDi2049.

Phylogenomic databases

HOVERGENiHBG062180.
KOiK05112.

Enzyme and pathway databases

BRENDAi2.7.10.1. 6725.

Family and domain databases

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.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 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_XENLA
AccessioniPrimary (citable) accession number: Q91735
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.