Q91571 (EPB1A_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Tyrosine-protein kinase receptor XEK

Gene names

Name:	ephb1-a
Synonyms:	xek

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	985 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. Ref.2
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.
Developmental stage	Maternally expressed, it decreases at mid blastula transition and reappears at late neurulation. Expressed at higher levels in the anterior and dorsal regions of embryonic stages 16, 24 and 37. In adult it appears to be ubiquitously expressed with higher expression in brain and ovary. Expression in the brain, brachial arches, trigeminal facial ganglion, and the retina of swimming tadpole stage of development.
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 Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
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
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 985	966	Ephrin type-B receptor 1-A		PRO_0000016826
Regions
	Topological domain	20 – 542	523	Extracellular Potential
	Transmembrane	543 – 563	21	Helical; Potential
	Topological domain	564 – 985	422	Cytoplasmic Potential
	Domain	21 – 203	183	Eph LBD
	Domain	325 – 426	102	Fibronectin type-III 1
	Domain	436 – 527	92	Fibronectin type-III 2
	Domain	620 – 883	264	Protein kinase
	Domain	912 – 976	65	SAM
	Nucleotide binding	626 – 634	9	ATP By similarity
	Motif	983 – 985	3	PDZ-binding Potential
	Compositional bias	185 – 321	137	Cys-rich
Sites
	Active site	745	1	Proton acceptor By similarity
	Binding site	652	1	ATP By similarity
Amino acid modifications
	Glycosylation	336	1	N-linked (GlcNAc...) Potential
	Glycosylation	428	1	N-linked (GlcNAc...) Potential
	Glycosylation	482	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q91571 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BE72CD1BFF51E623	FASTA	985	110,104
	10 20 30 40 50 60 MELNVLLLLL CLSGGQVGAV EETLMDTRTA TAELGWTANP SSGWEEVSGY DENLNTIRTY 70 80 90 100 110 120 QVCNVFGPKQ NNWLLTTFIP RRGAHRVYVE MRFTVRDCSS LPNVPGSCKE TFNLYYYETD 130 140 150 160 170 180 SNIENKISTF WNESPYLKVD TIAADESFSQ VDFGGRLMKV NTEVRSFGPL TRSGFYLAFQ 190 200 210 220 230 240 DYGACMSLLS VRVFFKEMPS VVQNLLVFPE TMTGAESTSL VIARGTCIPN AEEVDVPIKL 250 260 270 280 290 300 YCNGDGEWMV PIGKCTCKAG YEPENHVVCK ACPAAMFKAN QGMGICAQCP ANSRSTSEAS 310 320 330 340 350 360 PICICRNGYY RADFDTPEAP CTSVPSGPRN VISIVNETAI TLEWHPPRET GGRDDVDYNI 370 380 390 400 410 420 VCKKCRADRR ACSRCDDNVD FVPRQLGLTD TRVFISNLWA HTPYTFETQA VNGVTNKSPF 430 440 450 460 470 480 PPQHVSVNIT TNQAAPSSVP IMHQVKATMK SITLSWPQQE QPNGIILDYE IRYYEKDHHE 490 500 510 520 530 540 FNSSLARSQT NTARRTGGRV WMFMSVQVRA RTVAGYGKFS SKCGFQTLTA EDYKSELREQ 550 560 570 580 590 600 LPLTGSAAAG VVFIVSLVAI SIVCSRKRTY SKEAVYSDKL QHYSTGRGSP GMKIYIDPFT 610 620 630 640 650 660 YEDPNEAVRE FAKEIDVSFV KIEEVIGAGE FGEVYKGRLK LPSKREISVA IKTLKAGYSE 670 680 690 700 710 720 KQRRDFLSEA SIMGQFDHPN IIRLEGVVTK SRPVMIITEF MENGALDSFL RQNDGQFTVI 730 740 750 760 770 780 QLVGMLRGIA AGMKYLSEMN YVHRDLAARN ILVNSNLVCK VSDFGLSRYL QDDTSDPTYT 790 800 810 820 830 840 SSLGGKIPVR WTAQEAIAYR KFTSASDVWS YGIVMWEVMS YGERPYWTMS NQDVINAIEQ 850 860 870 880 890 900 DYRLPPPMDC PAALHQLMLD CWQKDRNSRP RLAEIVNTLR PMIRNPASLK TVATIPAVPS 910 920 930 940 950 960 QPLLDRSIPD ISAFTSVDDW LSAIKMGQYR DNFLSSGFTS LQLVAQMTSE DLLRIGITLA 970 980 GHQKKILNSI QSMRVQITQS PTSIA

References

[1]	"Expression of an amphibian homolog of the Eph family of receptor tyrosine kinases is developmentally regulated." Jones T.L., Karavanova I., Maeno M., Ong R.C., Kung H.-F., Daar I.O. Oncogene 10:1111-1117(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand regulate targeted migration of branchial neural crest cells." Smith A., Robinson V., Patel K., Wilkinson D.G. Curr. Biol. 7:561-570(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TARGETED CELL MIGRATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14164 mRNA. Translation: AAA74888.1.
PIR	I51672.
RefSeq	NP_001084070.1. NM_001090601.1.
UniGene	Xl.1028.
3D structure databases
ProteinModelPortal	Q91571.
SMR	Q91571. Positions 20-199, 438-529, 593-890, 901-985.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	399288.
KEGG	xla:399288.
Organism-specific databases
CTD	2047.
Xenbase	XB-GENE-865799. ephb1.
Phylogenomic databases
HOVERGEN	HBG062180.
KO	K05110.
Enzyme and pathway databases
BRENDA	2.7.10.1. 6726.
Family and domain databases
Gene3D	1.10.150.50. 1 hit. 2.60.40.10. 2 hits.
InterPro	IPR001090. Ephrin_rcpt_lig-bd_dom. IPR003961. Fibronectin_type3. IPR008979. Galactose-bd-like. IPR009030. Growth_fac_rcpt. IPR013783. Ig-like_fold. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001660. SAM. IPR013761. SAM/pointed. IPR011510. SAM_2. 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]
Pfam	PF01404. Ephrin_lbd. 1 hit. PF00041. fn3. 2 hits. PF07714. Pkinase_Tyr. 1 hit. PF07647. SAM_2. 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. SSF57184. Grow_fac_recept. 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. False negative. PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit. PS50105. SAM_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EPB1A_XENLA

Accession

Primary (citable) accession number: Q91571

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program