Q07494 (EPHB1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ephrin type-B receptor 1
EC=2.7.10.1

Alternative name(s):
EPH-like kinase 6
Short name=EK6
Short name=cEK6
Tyrosine-protein kinase receptor EPH-2

Gene names

Name:	EPHB1
Synonyms:	CEK6

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	984 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. May play a role in axon guidance during nervous system development. May also play an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. More generally, may play a role in targeted cell migration and adhesion. Upon activation by ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively 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 By similarity; Single-pass type I membrane protein. Early endosome membrane By similarity. Cell projection › dendrite By similarity.
Tissue specificity	Expressed at high levels in the 10-day embryo, and in adult brain, lung, heart and skeletal muscle. Low levels of expression detected in all other adult tissues tested.
Post-translational modification	Phosphorylated. Autophosphorylation is stimulated by ligands 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 process	Cell adhesion Neurogenesis
Cellular component	Cell membrane Cell projection Endosome Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	axon guidance Inferred from sequence or structural similarity. Source: UniProtKB cell chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB cell-substrate adhesion Inferred from sequence or structural similarity. Source: UniProtKB dendritic spine morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB establishment of cell polarity 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 ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB regulation of JNK cascade Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	dendrite Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW transmembrane-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 – 984	›984	Ephrin type-B receptor 1		PRO_0000160274
Regions
	Topological domain	‹1 – 541	›541	Extracellular Potential
	Transmembrane	542 – 562	21	Helical; Potential
	Topological domain	563 – 984	422	Cytoplasmic Potential
	Domain	1 – 182	182	Eph LBD
	Domain	304 – 405	102	Fibronectin type-III 1
	Domain	411 – 525	115	Fibronectin type-III 2
	Domain	619 – 882	264	Protein kinase
	Domain	911 – 975	65	SAM
	Nucleotide binding	625 – 633	9	ATP By similarity
	Motif	982 – 984	3	PDZ-binding Potential
	Compositional bias	164 – 300	137	Cys-rich
Sites
	Active site	744	1	Proton acceptor By similarity
	Binding site	651	1	ATP By similarity
Amino acid modifications
	Glycosylation	315	1	N-linked (GlcNAc...) Potential
	Glycosylation	407	1	N-linked (GlcNAc...) Potential
	Glycosylation	480	1	N-linked (GlcNAc...) Potential
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q07494 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: EF06C83BB63A13A1	FASTA	984	109,558
	10 20 30 40 50 60 ETLMDTRTAT AELGWTANPP SGWEEVSGYD ENLNTIRTYQ VCNVFEPNQN NWLLTTFINR 70 80 90 100 110 120 RGAHRIYTEM RFTVRDCSSL PNVPGSCKET FNLYYYETDS VIATKKSAFW TEAPYLKVDT 130 140 150 160 170 180 IAADESFSQV DFGGRLMKGX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXFFKKCPSV 190 200 210 220 230 240 VQNFAIFPET MTGAESTSLV TARGTCIPNA EEVDVPIKLY CNGDGEWMVP IGRCTCKAGY 250 260 270 280 290 300 EPENNVACRA CPAGTFKASQ GAGLCARCPP NSRSSAEASP LCACRNGYFR ADLDPPTAAC 310 320 330 340 350 360 TSVPSGPRNV ISIVNETSII LEWNPPRETG GRDDVTYNIV CKKCRADRRA CSRCDDNVEF 370 380 390 400 410 420 VPRQLGLTET RVFISSLWAH TPYTFEIQAV NGVSNKSPFP PQHVSVNITT NQAAPSTVPI 430 440 450 460 470 480 MHQVSATMRS ITLSWPQPEQ PNGIILDYEL RYYEKLSRIC TPDVSGTVGS RPAADHNEYN 490 500 510 520 530 540 SSVARSQTNT ARLEGLRPGM VYVVQVRART VAGYGKYSGK MCFQTLTDDD YKSELREQLP 550 560 570 580 590 600 LIAGSAAAGV VFIVSLVAIS IVCSRKRAYS KEVVYSDKLQ HYSTGRGSPG MKIYIDPFTY 610 620 630 640 650 660 EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI KTLKAGYSEK 670 680 690 700 710 720 QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM ENGALDSFLR QNDGQFTVIQ 730 740 750 760 770 780 LVGMLRGIAA GMKYLAEMNY VHRDLAARNI LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS 790 800 810 820 830 840 SLGGKIPVRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD 850 860 870 880 890 900 YRLPPPMDCP AALHQLMLDC WQKDRNTRPR LAEIVNTLDK MIRNPASLKT VATITAVPSQ 910 920 930 940 950 960 PLLDRSIPDF TAFTSVEDWL SAVKMSQYRD NFLSAGFTSL QLVAQMTSED LLRIGVTLAG 970 980 HQKKILNSIQ SMRVQMSQSP TSMA

References

[1]	"Five novel avian Eph-related tyrosine kinases are differentially expressed." Sajjadi F.G., Pasquale E.B. Oncogene 8:1807-1813(1993) [PubMed: 8510926] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z19110 mRNA. Translation: CAA79526.1.
IPI	IPI01017224.
PIR	I50612.
UniGene	Gga.40746.
3D structure databases
ProteinModelPortal	Q07494.
SMR	Q07494. Positions 1-138, 417-528, 592-889, 900-984.
ModBase	Search...
Proteomic databases
PRIDE	Q07494.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	veNOG06887.
HOVERGEN	HBG062180.
Family and domain databases
InterPro	IPR001090. Ephrin_rcpt_lig-bd. IPR003961. Fibronectin_type3. IPR008979. Galactose-bd-like. IPR013783. Ig-like_fold. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001660. SAM. IPR013761. SAM/pointed. IPR021129. SAM_type1. 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]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 2 hits. G3DSA:1.10.150.50. SAM_type. 1 hit.
Pfam	PF01404. Ephrin_lbd. 1 hit. PF00041. fn3. 2 hits. PF07699. GCC2_GCC3. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF00536. SAM_1. 1 hit. [Graphical view]
PIRSF	PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTS	PR00109. TYRKINASE.
SMART	SM00615. EPH_lbd. 1 hit. SM00060. FN3. 2 hits. SM00454. SAM. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 2 hits. SSF49785. Gal_bind_like. 1 hit. SSF56112. Kinase_like. 1 hit. SSF47769. SAM_homology. 1 hit.
PROSITE	PS01186. EGF_2. 1 hit. Uncertain. PS51550. 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. Partial match. PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit. PS50105. SAM_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EPHB1_CHICK

Accession

Primary (citable) accession number: Q07494

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	December 14, 2011
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program