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Ephrin type-B receptor 1 (EC 2.7.10.1) (ELK) (Tyrosine-protein kinase receptor EPH-2)

 EPHB1_RAT               Reviewed;         984 AA.
P09759;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 2.
23-MAY-2018, entry version 189.
RecName: Full=Ephrin type-B receptor 1;
EC=2.7.10.1;
AltName: Full=ELK;
AltName: Full=Tyrosine-protein kinase receptor EPH-2;
Flags: Precursor;
Name=Ephb1; Synonyms=Elk, Epth2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AUTOPHOSPHORYLATION, AND TISSUE
SPECIFICITY.
STRAIN=Wistar; TISSUE=Brain;
PubMed=2017163; DOI=10.1128/MCB.11.5.2496;
Lhotak V., Greer P., Letwin K., Pawson T.;
"Characterization of elk, a brain-specific receptor tyrosine kinase.";
Mol. Cell. Biol. 11:2496-2502(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 605-984.
STRAIN=Wistar; TISSUE=Brain;
PubMed=2485255;
Letwin K., Yee S.P., Pawson T.;
"Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned
using anti-phosphotyrosine antibody.";
Oncogene 3:621-627(1988).
-!- 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. Cognate/functional ephrin ligands for this receptor
include EFNB1, EFNB2 and EFNB3. During nervous system development,
regulates retinal axon guidance redirecting ipsilaterally
ventrotemporal retinal ganglion cells axons at the optic chiasm
midline. This probably requires repulsive interaction with EFNB2.
In the adult nervous system together with EFNB3, regulates
chemotaxis, proliferation and polarity of the hippocampus neural
progenitors. 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 synapse
formation. May also regulate angiogenesis. More generally, may
play a role in targeted cell migration and adhesion. Upon
activation by EFNB1 and probably other ephrin-B ligands activates
the MAPK/ERK and the JNK signaling cascades to regulate cell
migration and adhesion respectively (By similarity). Involved in
the maintenance of the pool of satellite cells (muscle stem cells)
by promoting their self-renewal and reducing their activation and
differentiation (By similarity). {ECO:0000250|UniProtKB:P54762,
ECO:0000250|UniProtKB:Q8CBF3}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: 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. Interacts with EPHB6; transphosphorylates EPHB6 to form
an active signaling complex. Interacts with PICK1. Interacts
(through Tyr-594) with NCK1 (via SH2 domain); activates the JUN
cascade to regulate cell adhesion. The ligand-activated form
interacts (through Tyr-928) with GRB7 and GRB10 (via SH2 domains).
The ligand-activated form interacts (residues within the catalytic
domain) with GRB2 (via SH2 domain). Interacts with GRB2, SHC1 and
SRC; activates the MAPK/ERK cascade to regulate cell migration.
Interacts with CBL; regulates receptor degradation through
ubiquitination. Interacts with ACP1 (By similarity).
{ECO:0000250|UniProtKB:P54762, ECO:0000250|UniProtKB:Q8CBF3}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P54762}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P54762}. Early endosome membrane
{ECO:0000250|UniProtKB:P54762}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q8CBF3}.
-!- TISSUE SPECIFICITY: Restricted to brain and testes.
{ECO:0000269|PubMed:2017163}.
-!- PTM: Phosphorylated. Autophosphorylation is stimulated by the
ligand EFNB1. Required for interaction with SH2 domain-containing
interactors, for activation of the MAPK/ERK and JUN signaling
cascades and for ubiquitination by CBL (By similarity).
{ECO:0000250|UniProtKB:P54762}.
-!- PTM: Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-
ubiquitination by CBL is regulated by SRC and leads to lysosomal
degradation. {ECO:0000250|UniProtKB:P54762,
ECO:0000250|UniProtKB:Q8CBF3}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M59814; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; X13411; CAA31777.1; -; mRNA.
PIR; A39753; A39753.
RefSeq; NP_001097998.1; NM_001104528.1.
RefSeq; XP_017450939.1; XM_017595450.1.
UniGene; Rn.46606; -.
ProteinModelPortal; P09759; -.
SMR; P09759; -.
BioGrid; 246515; 2.
CORUM; P09759; -.
DIP; DIP-138N; -.
STRING; 10116.ENSRNOP00000010634; -.
GuidetoPHARMACOLOGY; 1830; -.
iPTMnet; P09759; -.
PhosphoSitePlus; P09759; -.
SwissPalm; P09759; -.
PaxDb; P09759; -.
PRIDE; P09759; -.
Ensembl; ENSRNOT00000010634; ENSRNOP00000010634; ENSRNOG00000007865.
GeneID; 24338; -.
KEGG; rno:24338; -.
UCSC; RGD:2556; rat.
CTD; 2047; -.
RGD; 2556; Ephb1.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; P09759; -.
KO; K05110; -.
OMA; KACPAGM; -.
OrthoDB; EOG091G00W0; -.
PhylomeDB; P09759; -.
TreeFam; TF315608; -.
BRENDA; 2.7.10.1; 5301.
Reactome; R-RNO-2682334; EPH-Ephrin signaling.
Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
Reactome; R-RNO-3928664; Ephrin signaling.
Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
PRO; PR:P09759; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000007865; -.
Genevisible; P09759; RN.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008046; F:axon guidance receptor activity; IEA:Ensembl.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
GO; GO:0021952; P:central nervous system projection neuron axonogenesis; ISS:UniProtKB.
GO; GO:0060996; P:dendritic spine development; IGI:MGI.
GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
GO; GO:0001771; P:immunological synapse formation; IGI:MGI.
GO; GO:1902725; P:negative regulation of satellite cell differentiation; ISS:UniProtKB.
GO; GO:1902723; P:negative regulation of skeletal muscle satellite cell proliferation; ISS:UniProtKB.
GO; GO:0061351; P:neural precursor cell proliferation; ISS:UniProtKB.
GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
GO; GO:0021631; P:optic nerve morphogenesis; IEA:Ensembl.
GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
GO; GO:1901214; P:regulation of neuron death; IEA:Ensembl.
GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:UniProtKB.
GO; GO:0014719; P:skeletal muscle satellite cell activation; ISS:UniProtKB.
CDD; cd10476; EphR_LBD_B1; 1.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034231; EphB1_rcpt_lig-bd.
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
Pfam; PF14575; EphA2_TM; 1.
Pfam; PF01404; Ephrin_lbd; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00536; SAM_1; 1.
PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00615; EPH_lbd; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00060; FN3; 2.
SMART; SM00454; SAM; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS51550; EPH_LBD; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
ATP-binding; Cell adhesion; Cell membrane; Cell projection;
Complete proteome; Endosome; Glycoprotein; Kinase; Membrane;
Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 984 Ephrin type-B receptor 1.
/FTId=PRO_0000016825.
TOPO_DOM 18 540 Extracellular. {ECO:0000255}.
TRANSMEM 541 563 Helical. {ECO:0000255}.
TOPO_DOM 564 984 Cytoplasmic. {ECO:0000255}.
DOMAIN 19 201 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 322 432 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 433 528 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 619 882 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 911 975 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 625 633 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 982 984 PDZ-binding. {ECO:0000255}.
COMPBIAS 183 319 Cys-rich.
ACT_SITE 744 744 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 651 651 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 600 600 Phosphotyrosine.
{ECO:0000250|UniProtKB:P54753}.
MOD_RES 928 928 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
CARBOHYD 334 334 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 426 426 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 480 480 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 984 AA; 109883 MW; 521EAC240D8FB91A CRC64;
MALDCLLLFL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE NLNTIRTYQV
CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP NVPGSCKETF NLYYYETDSV
IATKKSAFWS EAPYLKVDTI AADESFSQVD FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY
GACMSLLSVR VFFKKCPSIV QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC
NGDGEWMVPI GRCTCKAGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPSEASPI
CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG RDDVTYNIIC
KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT PYTFDIQAIN GVSSKSPFPP
QHVSVNITTN QAAPSTVPIM HQVSATMRSI TLSWPQPEQP NGIILDYEIR YYEKEHNEFN
SSMARSQTNT ARIDGLRPGM VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP
LIAGSAAAGV VFVVSLVAIS IVCSRKRAYS KEAVYSDKLQ HYSTGRGSPG MKIYIDPFTY
EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI KTLKAGYSEK
QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM ENGALDSFLR QNDGQFTVIQ
LVGMLRGIAA GMKYLSEMNY VHRDLAARNI LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS
SLGGKIPVRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD
YRLPPPMDCP AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ
PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED LLRIGVTLAG
HQKKILSSIH SMRVQMNQSP SVMA


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