O13147 (EPHB3_DANRE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
EPH-like kinase 3
Tyrosine-protein kinase receptor ZEK3

Gene names

Name:	ephb3
Synonyms:	ek3, zek3

Organism

Danio rerio (Zebrafish) (Brachydanio rerio)

Taxonomic identifier

7955 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length	500 AA.
Sequence status	Fragment.
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. May play a role in early pattern formation within the developing nervous system.
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	Widely expressed in the developing nervous system.
Post-translational modification	Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-168 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 protein kinase domain. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Neurogenesis
Cellular component	Cell membrane Cell projection Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
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
	Chain	‹1 – 500	›500	Ephrin type-B receptor 3		PRO_0000160277
Regions
	Topological domain	‹1 – 113	›113	Extracellular Potential
	Transmembrane	114 – 134	21	Helical; Potential
	Topological domain	135 – 500	366	Cytoplasmic Potential
	Domain	187 – 450	264	Protein kinase
	Domain	421 – 500	80	SAM
	Nucleotide binding	193 – 201	9	ATP By similarity
	Motif	498 – 500	3	PDZ-binding Potential
Sites
	Active site	312	1	Proton acceptor By similarity
	Binding site	219	1	ATP By similarity
Amino acid modifications
	Modified residue	168	1	Phosphotyrosine; by autocatalysis By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	O13147 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: DBEA421E31E693B2	FASTA	500	55,911
	10 20 30 40 50 60 PLLVLDLIIQ ERGESFSHTV TAQHTSAKVE GLKAGTVYSV QVRARTVAGY GRYSNPVDFS 70 80 90 100 110 120 TSLYVCPVSS SSTSMHLRRR EELTTTTTGL KSREERFQKS DDPERSVQDL LPLIVGSASA 130 140 150 160 170 180 GFVVILAMIV IAVVCLRRQR TGSELEYTEK LQQYVSPGVK VYIDPFTYED PNEAVHEFAR 190 200 210 220 230 240 EIDISCVKIE EVIGAGEFGE VCRGRLKQAG RKETTVAIKT LKAGYTEHQR RDFLSEASIM 250 260 270 280 290 300 GQFDHPNVIH LEGVLTRSCP VLIVTEFMEN GALDSFLRLN DGRFTVTQLV GMLRGIAAGM 310 320 330 340 350 360 KYLSDMNYVH RDLAARNVLV NSNLVCKVSD FGLSRFLDDN SSDPTYTSSL GGKIPIRWTA 370 380 390 400 410 420 PEAIAFRKFT SASDVWSYGI VMWEVMSFGE RPYWDMSNQD VMNAVEQDYR LPPPMDCPAV 430 440 450 460 470 480 LHQLMLECWV KERNMRPRFG QIVSTLDKFL RNAASLKVLT STHSGDLCRI GGTLPGHQRK 490 500 SIGDAQDIKQ QMSQTLPIRV

References

[1]	"Novel Eph-family receptor tyrosine kinase is widely expressed in the developing zebrafish nervous system." Bovenkamp D.E., Greer P. Dev. Dyn. 209:166-181(1997) [PubMed: 9186052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U89379 mRNA. Translation: AAC60221.1.
IPI	IPI00860734.
UniGene	Dr.28327.
3D structure databases
ProteinModelPortal	O13147.
SMR	O13147. Positions 160-457.
ModBase	Search...
Protein-protein interaction databases
STRING	O13147.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
ZFIN	ZDB-GENE-990415-60. ephb3a.
Phylogenomic databases
eggNOG	fiNOG12369.
GeneTree	ENSGT00570000078802.
HOVERGEN	HBG062180.
Gene expression databases
ArrayExpress	O13147.
Bgee	O13147.
Family and domain databases
InterPro	IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001660. SAM. IPR001245. Ser-Thr/Tyr_kinase. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
Pfam	PF00041. fn3. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
SMART	SM00060. FN3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50105. SAM_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EPHB3_DANRE

Accession

Primary (citable) accession number: O13147

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 1, 1997
Last modified:	December 14, 2011
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program