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Ephrin type-A receptor 4 (EC 2.7.10.1) (Tyrosine-protein kinase receptor MPK-3) (Tyrosine-protein kinase receptor SEK-1)

 EPHA4_MOUSE             Reviewed;         986 AA.
Q03137; Q80VZ2;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
20-JUN-2018, entry version 194.
RecName: Full=Ephrin type-A receptor 4;
EC=2.7.10.1;
AltName: Full=Tyrosine-protein kinase receptor MPK-3;
AltName: Full=Tyrosine-protein kinase receptor SEK-1;
Flags: Precursor;
Name=Epha4; Synonyms=Sek, Sek1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
STRAIN=C57BL/6J; TISSUE=Embryonic brain;
PubMed=1281307;
Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G.,
Chestier A., Wilkinson D.G., Charnay P.;
"An Eph-related receptor protein tyrosine kinase gene segmentally
expressed in the developing mouse hindbrain.";
Oncogene 7:2499-2506(1992).
[2]
ERRATUM.
PubMed=8455939;
Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G.,
Chestier A., Wilkinson D.G., Charnay P.;
Oncogene 8:1103-1103(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION AT TYR-596 AND TYR-602, AND INTERACTION WITH FYN.
PubMed=8622893;
Ellis C., Kasmi F., Ganju P., Walls E., Panayotou G., Reith A.D.;
"A juxtamembrane autophosphorylation site in the Eph family receptor
tyrosine kinase, Sek, mediates high affinity interaction with
p59fyn.";
Oncogene 12:1727-1736(1996).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION IN AXON GUIDANCE.
PubMed=9789074; DOI=10.1073/pnas.95.22.13248;
Dottori M., Hartley L., Galea M., Paxinos G., Polizzotto M.,
Kilpatrick T., Bartlett P.F., Murphy M., Koentgen F., Boyd A.W.;
"EphA4 (Sek1) receptor tyrosine kinase is required for the development
of the corticospinal tract.";
Proc. Natl. Acad. Sci. U.S.A. 95:13248-13253(1998).
[8]
INTERACTION WITH NGEF, AND MUTAGENESIS OF VAL-635.
PubMed=11336673; DOI=10.1016/S0092-8674(01)00314-2;
Shamah S.M., Lin M.Z., Goldberg J.L., Estrach S., Sahin M., Hu L.,
Bazalakova M., Neve R.L., Corfas G., Debant A., Greenberg M.E.;
"EphA receptors regulate growth cone dynamics through the novel
guanine nucleotide exchange factor ephexin.";
Cell 105:233-244(2001).
[9]
DEVELOPMENTAL STAGE.
PubMed=14516691; DOI=10.1016/S0925-4773(03)00122-9;
Greferath U., Canty A.J., Messenger J., Murphy M.;
"Developmental expression of EphA4-tyrosine kinase receptor in the
mouse brain and spinal cord.";
Mech. Dev. 119:S231-S238(2002).
[10]
DISRUPTION PHENOTYPE, AND FUNCTION IN AXONAL REGENERATION.
PubMed=15537875; DOI=10.1523/JNEUROSCI.2981-04.2004;
Goldshmit Y., Galea M.P., Wise G., Bartlett P.F., Turnley A.M.;
"Axonal regeneration and lack of astrocytic gliosis in EphA4-deficient
mice.";
J. Neurosci. 24:10064-10073(2004).
[11]
FUNCTION IN ANGIOGENESIS.
PubMed=16802330; DOI=10.1002/cne.21029;
Goldshmit Y., Galea M.P., Bartlett P.F., Turnley A.M.;
"EphA4 regulates central nervous system vascular formation.";
J. Comp. Neurol. 497:864-875(2006).
[12]
DISRUPTION PHENOTYPE, AND FUNCTION IN THYMUS DEVELOPMENT.
PubMed=16818734; DOI=10.4049/jimmunol.177.2.804;
Munoz J.J., Alfaro D., Garcia-Ceca J., Alonso-C L.M., Jimenez E.,
Zapata A.;
"Thymic alterations in EphA4-deficient mice.";
J. Immunol. 177:804-813(2006).
[13]
FUNCTION IN RAC1 REGULATION, FUNCTION IN AXON GUIDANCE, AND
INTERACTION WITH CHN1.
PubMed=17719550; DOI=10.1016/j.cell.2007.07.022;
Iwasato T., Katoh H., Nishimaru H., Ishikawa Y., Inoue H., Saito Y.M.,
Ando R., Iwama M., Takahashi R., Negishi M., Itohara S.;
"Rac-GAP alpha-chimerin regulates motor-circuit formation as a key
mediator of EphrinB3/EphA4 forward signaling.";
Cell 130:742-753(2007).
[14]
FUNCTION IN NEURON MORPHOLOGY, AND INTERACTION WITH SIPA1L1.
PubMed=18094260; DOI=10.1523/JNEUROSCI.2746-07.2007;
Richter M., Murai K.K., Bourgin C., Pak D.T., Pasquale E.B.;
"The EphA4 receptor regulates neuronal morphology through SPAR-
mediated inactivation of Rap GTPases.";
J. Neurosci. 27:14205-14215(2007).
[15]
FUNCTION IN DENDRITIC SPINE MORPHOGENESIS, TOPOLOGY, SUBCELLULAR
LOCATION, AND INTERACTION WITH NGEF.
PubMed=17143272; DOI=10.1038/nn1811;
Fu W.Y., Chen Y., Sahin M., Zhao X.S., Shi L., Bikoff J.B., Lai K.O.,
Yung W.H., Fu A.K., Greenberg M.E., Ip N.Y.;
"Cdk5 regulates EphA4-mediated dendritic spine retraction through an
ephexin1-dependent mechanism.";
Nat. Neurosci. 10:67-76(2007).
[16]
FUNCTION IN AXON GUIDANCE, INTERACTION WITH CHN1, AND MUTAGENESIS OF
VAL-635.
PubMed=17785183; DOI=10.1016/j.neuron.2007.07.036;
Beg A.A., Sommer J.E., Martin J.H., Scheiffele P.;
"alpha2-Chimaerin is an essential EphA4 effector in the assembly of
neuronal locomotor circuits.";
Neuron 55:768-778(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-602, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[18]
FUNCTION IN MOTOR AND SENSORY AXONS SEGREGATION.
PubMed=18403711; DOI=10.1126/science.1153758;
Gallarda B.W., Bonanomi D., Mueller D., Brown A., Alaynick W.A.,
Andrews S.E., Lemke G., Pfaff S.L., Marquardt T.;
"Segregation of axial motor and sensory pathways via heterotypic
trans-axonal signaling.";
Science 320:233-236(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Heart;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[20]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=27446912; DOI=10.3389/fcell.2016.00058;
Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J.,
de Reynies A., Aurade F., Chang T.H., Zammit P.S., Relaix F.;
"Gene expression profiling of muscle stem cells identifies novel
regulators of postnatal myogenesis.";
Front. Cell Dev. Biol. 4:58-58(2016).
-!- FUNCTION: Receptor tyrosine kinase which binds membrane-bound
ephrin 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. Highly
promiscuous, it has the unique property among Eph receptors to
bind and to be physiologically activated by both GPI-anchored
ephrin-A and transmembrane ephrin-B ligands including EFNA1 and
EFNB3. Upon activation by ephrin ligands, modulates cell
morphology and integrin-dependent cell adhesion through regulation
of the Rac, Rap and Rho GTPases activity. Plays an important role
in the development of the nervous system controlling different
steps of axonal guidance including the establishment of the
corticospinal projections. May also control the segregation of
motor and sensory axons during neuromuscular circuit development.
In addition to its role in axonal guidance plays a role in
synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at
'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and
dendritic spine morphogenesis. In the nervous system, plays also a
role in repair after injury preventing axonal regeneration and in
angiogenesis playing a role in central nervous system vascular
formation. Additionally, its promiscuity makes it available to
participate in a variety of cell-cell signaling regulating for
instance the development of the thymic epithelium.
{ECO:0000269|PubMed:15537875, ECO:0000269|PubMed:16802330,
ECO:0000269|PubMed:16818734, ECO:0000269|PubMed:17143272,
ECO:0000269|PubMed:17719550, ECO:0000269|PubMed:17785183,
ECO:0000269|PubMed:18094260, ECO:0000269|PubMed:18403711,
ECO:0000269|PubMed:9789074}.
-!- 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 (phosphorylated at position Tyr-602) with
FYN. Interacts (via PDZ motif) with SIPA1L1 (via PDZ domain);
controls neuronal morphology through regulation of the RAP1 (RAP1A
or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases. Interacts with
CDK5, CDK5R1 and NGEF; upon activation by EFNA1 induces NGEF
phosphorylation by the kinase CDK5. Interacts with CHN1; effector
of EPHA4 in axon guidance linking EPHA4 activation to RAC1
regulation. {ECO:0000269|PubMed:11336673,
ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:17719550,
ECO:0000269|PubMed:17785183, ECO:0000269|PubMed:18094260,
ECO:0000269|PubMed:8622893}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1539152, EBI-1539152;
Q91V57-1:Chn1; NbExp=2; IntAct=EBI-1539152, EBI-1539203;
P52800:Efnb2; NbExp=2; IntAct=EBI-1539152, EBI-1032676;
Q03145:Epha2; NbExp=3; IntAct=EBI-1539152, EBI-529701;
P54763:Ephb2; NbExp=3; IntAct=EBI-1539152, EBI-537711;
Q921Q7:Rin1; NbExp=2; IntAct=EBI-1539152, EBI-15724937;
O95292:VAPB (xeno); NbExp=2; IntAct=EBI-1539152, EBI-1188298;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17143272};
Single-pass type I membrane protein {ECO:0000269|PubMed:17143272}.
Cell projection, axon {ECO:0000269|PubMed:17143272}. Cell
projection, dendrite {ECO:0000269|PubMed:17143272}. Cell junction,
synapse, postsynaptic cell membrane, postsynaptic density
{ECO:0000250}. Early endosome {ECO:0000269|PubMed:17143272}.
Note=Clustered upon activation and targeted to early endosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q03137-1; Sequence=Displayed;
Name=Short;
IsoId=Q03137-2; Sequence=VSP_002998;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highest expression in the adult brain and
retina and also detectable in kidney, lung, skeletal muscle and
thymus. Not detected in heart and liver. Expressed in myogenic
progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:27446912}.
-!- DEVELOPMENTAL STAGE: Found in both the 10-day embryonic brain and
body tissues. In the embryonic brain, expressed in the developing
cortex of the telencephalon and major cortical tracts. Also
expressed in the hippocampus, fornix and striatal cells and
tracts. In the diencephalon, strongly expressed in thalamus,
hypothalamus and thalamo-cortical projection. Also expressed in
red nuclei of the mesencephalon and in the cerebellum. In the
spinal cord, persistent expression occurs in the dorsal funiculus
and ventral gray matter. In myogenic progenitor cells, highly
expressed at E11.5 and ceases its expression at the late fetal
stage (E17.5) (PubMed:27446912). {ECO:0000269|PubMed:14516691,
ECO:0000269|PubMed:27446912}.
-!- DOMAIN: The protein kinase domain mediates interaction with NGEF.
-!- DISRUPTION PHENOTYPE: Mice are viable and fertile but display a
loss of coordination of limb movement associated with disruptions
of cortico-spinal tract. They also display altered development of
the thymic epithelium which leads to a defective T-cells
development. {ECO:0000269|PubMed:15537875,
ECO:0000269|PubMed:16818734, ECO:0000269|PubMed:9789074}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; X65138; CAA46268.1; -; mRNA.
EMBL; X57241; CAA40517.1; -; mRNA.
EMBL; S57168; AAB25836.1; -; mRNA.
EMBL; AK147698; BAE28081.1; -; mRNA.
EMBL; CH466548; EDL00429.1; -; Genomic_DNA.
EMBL; BC052164; AAH52164.1; -; mRNA.
CCDS; CCDS35627.1; -. [Q03137-1]
PIR; S78059; S78059.
RefSeq; NP_031962.2; NM_007936.3. [Q03137-1]
UniGene; Mm.400747; -.
PDB; 1B0X; X-ray; 2.00 A; A=890-981.
PDB; 2HEL; X-ray; 2.35 A; A=591-896.
PDB; 2I8J; Model; -; @=594-888.
PDB; 2XYU; X-ray; 2.12 A; A=612-896.
PDB; 2Y6M; X-ray; 1.70 A; A=606-896.
PDB; 2Y6O; X-ray; 1.54 A; A=606-896.
PDBsum; 1B0X; -.
PDBsum; 2HEL; -.
PDBsum; 2I8J; -.
PDBsum; 2XYU; -.
PDBsum; 2Y6M; -.
PDBsum; 2Y6O; -.
ProteinModelPortal; Q03137; -.
SMR; Q03137; -.
BioGrid; 199471; 4.
DIP; DIP-1019N; -.
IntAct; Q03137; 10.
MINT; Q03137; -.
STRING; 10090.ENSMUSP00000027451; -.
BindingDB; Q03137; -.
ChEMBL; CHEMBL1293259; -.
GuidetoPHARMACOLOGY; 1824; -.
iPTMnet; Q03137; -.
PhosphoSitePlus; Q03137; -.
MaxQB; Q03137; -.
PaxDb; Q03137; -.
PeptideAtlas; Q03137; -.
PRIDE; Q03137; -.
Ensembl; ENSMUST00000027451; ENSMUSP00000027451; ENSMUSG00000026235. [Q03137-1]
Ensembl; ENSMUST00000188797; ENSMUSP00000140954; ENSMUSG00000026235. [Q03137-1]
Ensembl; ENSMUST00000188952; ENSMUSP00000139640; ENSMUSG00000026235. [Q03137-1]
GeneID; 13838; -.
KEGG; mmu:13838; -.
UCSC; uc007bpz.1; mouse. [Q03137-1]
CTD; 2043; -.
MGI; MGI:98277; Epha4.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; Q03137; -.
KO; K05105; -.
OMA; NGECQAC; -.
OrthoDB; EOG091G00W0; -.
TreeFam; TF315608; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-2682334; EPH-Ephrin signaling.
Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
EvolutionaryTrace; Q03137; -.
PRO; PR:Q03137; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026235; -.
CleanEx; MM_EPHA4; -.
ExpressionAtlas; Q03137; baseline and differential.
Genevisible; Q03137; MM.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0043679; C:axon terminus; ISO:MGI.
GO; GO:0044295; C:axonal growth cone; ISO:MGI.
GO; GO:0044297; C:cell body; ISO:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0042995; C:cell projection; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0043198; C:dendritic shaft; ISO:MGI.
GO; GO:0043197; C:dendritic spine; ISO:MGI.
GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0030175; C:filopodium; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
GO; GO:0043204; C:perikaryon; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0014069; C:postsynaptic density; ISO:MGI.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0097161; F:DH domain binding; ISS:UniProtKB.
GO; GO:0046875; F:ephrin receptor binding; ISO:MGI.
GO; GO:0005004; F:GPI-linked ephrin receptor activity; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; ISO:MGI.
GO; GO:0042731; F:PH domain binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
GO; GO:0005005; F:transmembrane-ephrin receptor activity; IDA:UniProtKB.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
GO; GO:0021957; P:corticospinal tract morphogenesis; IMP:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISO:MGI.
GO; GO:0097156; P:fasciculation of motor neuron axon; IMP:UniProtKB.
GO; GO:0097155; P:fasciculation of sensory neuron axon; IMP:UniProtKB.
GO; GO:0008347; P:glial cell migration; ISO:MGI.
GO; GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB.
GO; GO:0048681; P:negative regulation of axon regeneration; IMP:UniProtKB.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:ARUK-UCL.
GO; GO:1903051; P:negative regulation of proteolysis involved in cellular protein catabolic process; ISO:MGI.
GO; GO:0072178; P:nephric duct morphogenesis; IGI:MGI.
GO; GO:0106030; P:neuron projection fasciculation; IDA:ARUK-UCL.
GO; GO:0097485; P:neuron projection guidance; IDA:ARUK-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:MGI.
GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISO:MGI.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IGI:ARUK-UCL.
GO; GO:2001108; P:positive regulation of Rho guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0048710; P:regulation of astrocyte differentiation; IMP:UniProtKB.
GO; GO:0050770; P:regulation of axonogenesis; IMP:UniProtKB.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
GO; GO:1905244; P:regulation of modification of synaptic structure; IGI:ARUK-UCL.
CDD; cd10482; EphR_LBD_A4; 1.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034270; EphA4_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; 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; PF07647; SAM_2; 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; SM00220; S_TKc; 1.
SMART; SM00454; SAM; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 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;
3D-structure; Alternative splicing; ATP-binding; Cell adhesion;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Developmental protein; Endosome; Glycoprotein; Kinase; Membrane;
Neurogenesis; Nucleotide-binding; Phosphoprotein;
Postsynaptic cell membrane; Receptor; Reference proteome; Repeat;
Signal; Synapse; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 986 Ephrin type-A receptor 4.
/FTId=PRO_0000016808.
TOPO_DOM 20 547 Extracellular. {ECO:0000255}.
TRANSMEM 548 569 Helical. {ECO:0000255}.
TOPO_DOM 570 986 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 209 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 328 439 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 440 537 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 621 882 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 911 975 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 627 635 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 984 986 PDZ-binding. {ECO:0000255}.
COMPBIAS 191 325 Cys-rich.
ACT_SITE 746 746 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 653 653 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 596 596 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:8622893}.
MOD_RES 602 602 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:18034455,
ECO:0000269|PubMed:8622893}.
MOD_RES 779 779 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 928 928 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 783 832 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_002998.
MUTAGEN 635 635 V->M: Kinase dead; loss of
autophosphorylation and loss of CHN1
phosphorylation. No effect on interaction
with NGEF. {ECO:0000269|PubMed:11336673,
ECO:0000269|PubMed:17785183}.
CONFLICT 145 145 I -> T (in Ref. 1; CAA46268/AAB25836).
{ECO:0000305}.
HELIX 618 620 {ECO:0000244|PDB:2Y6O}.
STRAND 621 629 {ECO:0000244|PDB:2Y6O}.
STRAND 631 640 {ECO:0000244|PDB:2Y6O}.
STRAND 648 655 {ECO:0000244|PDB:2Y6O}.
HELIX 661 674 {ECO:0000244|PDB:2Y6O}.
STRAND 685 689 {ECO:0000244|PDB:2Y6O}.
STRAND 691 694 {ECO:0000244|PDB:2Y6O}.
STRAND 696 700 {ECO:0000244|PDB:2Y6O}.
HELIX 707 712 {ECO:0000244|PDB:2Y6O}.
TURN 713 716 {ECO:0000244|PDB:2Y6O}.
HELIX 720 739 {ECO:0000244|PDB:2Y6O}.
HELIX 749 751 {ECO:0000244|PDB:2Y6O}.
STRAND 752 754 {ECO:0000244|PDB:2Y6O}.
STRAND 760 762 {ECO:0000244|PDB:2Y6O}.
HELIX 788 790 {ECO:0000244|PDB:2Y6O}.
HELIX 793 798 {ECO:0000244|PDB:2Y6O}.
HELIX 803 818 {ECO:0000244|PDB:2Y6O}.
TURN 824 827 {ECO:0000244|PDB:2Y6O}.
HELIX 830 838 {ECO:0000244|PDB:2Y6O}.
HELIX 851 860 {ECO:0000244|PDB:2Y6O}.
HELIX 865 867 {ECO:0000244|PDB:2Y6O}.
HELIX 871 883 {ECO:0000244|PDB:2Y6O}.
HELIX 885 888 {ECO:0000244|PDB:2Y6O}.
HELIX 916 922 {ECO:0000244|PDB:1B0X}.
HELIX 926 928 {ECO:0000244|PDB:1B0X}.
HELIX 929 934 {ECO:0000244|PDB:1B0X}.
HELIX 940 943 {ECO:0000244|PDB:1B0X}.
HELIX 948 954 {ECO:0000244|PDB:1B0X}.
HELIX 959 977 {ECO:0000244|PDB:1B0X}.
HELIX 978 980 {ECO:0000244|PDB:1B0X}.
SEQUENCE 986 AA; 109814 MW; 89BEB2C7CDB54A55 CRC64;
MAGIFYFILF SFLFGICDAV TGSRVYPANE VTLLDSRSVQ GELGWIASPL EGGWEEVSIM
DEKNTPIRTY QVCNVMEASQ NNWLRTDWIT REGAQRVYIE IKFTLRDCNS LPGVMGTCKE
TFNLYYYESD NDKERFIRES QFGKIDTIAA DESFTQVDIG DRIMKLNTEI RDVGPLSKKG
FYLAFQDVGA CIALVSVRVF YKKCPLTVRN LAQFPDTITG ADTSSLVEVR GSCVNNSEEK
DVPKMYCGAD GEWLVPIGNC LCNAGHEEQN GECQACKIGY YKALSTDASC AKCPPHSYSV
WEGATSCTCD RGFFRADNDA ASMPCTRPPS APLNLISNVN ETSVNLEWSS PQNTGGRQDI
SYNVVCKKCG AGDPSKCRPC GSGVHYTPQQ NGLKTTRVSI TDLLAHTNYT FEIWAVNGVS
KYNPSPDQSV SVTVTTNQAA PSSIALVQAK EVTRYSVALA WLEPDRPNGV ILEYEVKYYE
KDQNERSYRI VRTAARNTDI KGLNPLTSYV FHVRARTAAG YGDFSEPLEV TTNTVPSRII
GDGANSTVLL VSVSGSVVLV VILIAAFVIS RRRSKYSKAK QEADEEKHLN QGVRTYVDPF
TYEDPNQAVR EFAKEIDASC IKIEKVIGVG EFGEVCSGRL KVPGKREICV AIKTLKAGYT
DKQRRDFLSE ASIMGQFDHP NIIHLEGVVT KCKPVMIITE YMENGSLDAF LRKNDGRFTV
IQLVGMLRGI GSGMKYLSDM SYVHRDLAAR NILVNSNLVC KVSDFGMSRV LEDDPEAAYT
TRGGKIPIRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSY GERPYWDMSN QDVIKAIEEG
YRLPPPMDCP IALHQLMLDC WQKERSDRPK FGQIVNMLDK LIRNPNSLKR TGSESSRPNT
ALLDPSSPEF SAVVSVGDWL QAIKMDRYKD NFTAAGYTTL EAVVHMSQDD LARIGITAIT
HQNKILSSVQ AMRTQMQQMH GRMVPV


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