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Ephrin type-A receptor 4 (EC 2.7.10.1) (EPH-like kinase 8) (EK8) (hEK8) (Tyrosine-protein kinase TYRO1) (Tyrosine-protein kinase receptor SEK)

 EPHA4_HUMAN             Reviewed;         986 AA.
P54764; A8K2P1; B2R601; B7Z6Q8; Q2M380;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 186.
RecName: Full=Ephrin type-A receptor 4;
EC=2.7.10.1;
AltName: Full=EPH-like kinase 8;
Short=EK8;
Short=hEK8;
AltName: Full=Tyrosine-protein kinase TYRO1;
AltName: Full=Tyrosine-protein kinase receptor SEK;
Flags: Precursor;
Name=EPHA4; Synonyms=HEK8, SEK, TYRO1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=7898931;
Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M.,
Basu R., Welcher A.A.;
"cDNA cloning and tissue distribution of five human EPH-like receptor
protein-tyrosine kinases.";
Oncogene 10:897-905(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[5]
NOMENCLATURE.
PubMed=9267020;
Eph nomenclature committee;
"Unified nomenclature for Eph family receptors and their ligands, the
ephrins.";
Cell 90:403-404(1997).
[6]
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).
[7]
FUNCTION IN PHOSPHORYLATION OF CDK5, AND AUTOPHOSPHORYLATION.
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[9]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 29-209.
PubMed=18708347; DOI=10.1074/jbc.M804114200;
Qin H., Shi J., Noberini R., Pasquale E.B., Song J.;
"Crystal structure and NMR binding reveal that two small molecule
antagonists target the high affinity ephrin-binding channel of the
EphA4 receptor.";
J. Biol. Chem. 283:29473-29484(2008).
[10]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 30-202 IN COMPLEX WITH EFNA2
OR EFNB2, AND LIGAND-BINDING.
PubMed=19836338; DOI=10.1016/j.str.2009.07.018;
Bowden T.A., Aricescu A.R., Nettleship J.E., Siebold C.,
Rahman-Huq N., Owens R.J., Stuart D.I., Jones E.Y.;
"Structural plasticity of EPH receptor A4 facilitates cross-class
ephrin signaling.";
Structure 17:1386-1397(2009).
[11]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 29-203 IN COMPLEX WITH
EFNB2, AND MUTAGENESIS OF GLN-40 AND GLU-42.
PubMed=19875447; DOI=10.1074/jbc.M109.064824;
Qin H., Noberini R., Huan X., Shi J., Pasquale E.B., Song J.;
"Structural characterization of the EphA4-Ephrin-B2 complex reveals
new features enabling Eph-ephrin binding promiscuity.";
J. Biol. Chem. 285:644-654(2010).
[12]
VARIANTS [LARGE SCALE ANALYSIS] GLN-269; GLU-370 AND PHE-399.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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:17143272}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000270|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 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 (By similarity). 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. {ECO:0000269|PubMed:18094260,
ECO:0000269|PubMed:19836338, ECO:0000269|PubMed:19875447,
ECO:0007001}.
-!- INTERACTION:
O43921:EFNA2; NbExp=4; IntAct=EBI-5773557, EBI-8603210;
P52803:EFNA5; NbExp=2; IntAct=EBI-5773557, EBI-1753674;
P52799:EFNB2; NbExp=4; IntAct=EBI-5773557, EBI-7532268;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0007001}; Single-pass
type I membrane protein {ECO:0007001}. Cell projection, axon
{ECO:0007001}. Cell projection, dendrite {ECO:0007001}. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0007001}. Early endosome {ECO:0007001}.
Note=Clustered upon activation and targeted to early endosome.
{ECO:0007001}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P54764-1; Sequence=Displayed;
Name=2;
IsoId=P54764-2; Sequence=VSP_056016;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The protein kinase domain mediates interaction with NGEF.
{ECO:0007001}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000270|PROSITE-
ProRule:PRU00159}.
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EMBL; L36645; AAA74246.1; -; mRNA.
EMBL; AK290306; BAF82995.1; -; mRNA.
EMBL; AK300772; BAH13344.1; -; mRNA.
EMBL; AK312380; BAG35298.1; -; mRNA.
EMBL; AC010899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC105000; AAI05001.1; -; mRNA.
EMBL; BC105002; AAI05003.1; -; mRNA.
CCDS; CCDS2447.1; -. [P54764-1]
PIR; I78844; I78844.
RefSeq; NP_001291465.1; NM_001304536.1. [P54764-1]
RefSeq; NP_001291466.1; NM_001304537.1. [P54764-2]
RefSeq; NP_004429.1; NM_004438.4. [P54764-1]
UniGene; Hs.371218; -.
PDB; 2LW8; NMR; -; A=29-209.
PDB; 2WO1; X-ray; 1.85 A; A/B=30-202.
PDB; 2WO2; X-ray; 2.45 A; A=30-202.
PDB; 2WO3; X-ray; 2.35 A; A=30-202.
PDB; 3CKH; X-ray; 2.80 A; A/B=29-209.
PDB; 3GXU; X-ray; 2.50 A; A=29-203.
PDB; 4BK4; X-ray; 3.65 A; A/B=20-547.
PDB; 4BK5; X-ray; 4.00 A; A=20-547.
PDB; 4BKA; X-ray; 5.30 A; A=20-547.
PDB; 4BKF; X-ray; 4.65 A; A/B=20-547.
PDB; 4M4P; X-ray; 2.08 A; A=27-543.
PDB; 4M4R; X-ray; 3.13 A; A/C/E/G=27-543.
PDB; 4W4Z; X-ray; 2.41 A; A/B/C/D=29-204.
PDB; 4W50; X-ray; 2.42 A; A/B/C/D=29-204.
PDB; 5JR2; X-ray; 1.75 A; A/B/C/D=29-204.
PDBsum; 2LW8; -.
PDBsum; 2WO1; -.
PDBsum; 2WO2; -.
PDBsum; 2WO3; -.
PDBsum; 3CKH; -.
PDBsum; 3GXU; -.
PDBsum; 4BK4; -.
PDBsum; 4BK5; -.
PDBsum; 4BKA; -.
PDBsum; 4BKF; -.
PDBsum; 4M4P; -.
PDBsum; 4M4R; -.
PDBsum; 4W4Z; -.
PDBsum; 4W50; -.
PDBsum; 5JR2; -.
ProteinModelPortal; P54764; -.
SMR; P54764; -.
BioGrid; 108357; 49.
DIP; DIP-48294N; -.
IntAct; P54764; 8.
STRING; 9606.ENSP00000281821; -.
BindingDB; P54764; -.
ChEMBL; CHEMBL3988; -.
GuidetoPHARMACOLOGY; 1824; -.
iPTMnet; P54764; -.
PhosphoSitePlus; P54764; -.
BioMuta; EPHA4; -.
DMDM; 1711371; -.
EPD; P54764; -.
MaxQB; P54764; -.
PaxDb; P54764; -.
PeptideAtlas; P54764; -.
PRIDE; P54764; -.
TopDownProteomics; P54764-1; -. [P54764-1]
DNASU; 2043; -.
Ensembl; ENST00000281821; ENSP00000281821; ENSG00000116106. [P54764-1]
Ensembl; ENST00000409938; ENSP00000386829; ENSG00000116106. [P54764-1]
GeneID; 2043; -.
KEGG; hsa:2043; -.
UCSC; uc002vmq.4; human. [P54764-1]
CTD; 2043; -.
DisGeNET; 2043; -.
EuPathDB; HostDB:ENSG00000116106.11; -.
GeneCards; EPHA4; -.
HGNC; HGNC:3388; EPHA4.
HPA; CAB028368; -.
MalaCards; EPHA4; -.
MIM; 602188; gene.
neXtProt; NX_P54764; -.
OpenTargets; ENSG00000116106; -.
PharmGKB; PA27820; -.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; P54764; -.
KO; K05105; -.
OMA; NGECQAC; -.
OrthoDB; EOG091G00W0; -.
PhylomeDB; P54764; -.
TreeFam; TF315608; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-2682334; EPH-Ephrin signaling.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
SignaLink; P54764; -.
SIGNOR; P54764; -.
ChiTaRS; EPHA4; human.
EvolutionaryTrace; P54764; -.
GeneWiki; EPH_receptor_A4; -.
GenomeRNAi; 2043; -.
PRO; PR:P54764; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000116106; -.
CleanEx; HS_EPHA4; -.
ExpressionAtlas; P54764; baseline and differential.
Genevisible; P54764; HS.
GO; GO:0030424; C:axon; HMP:UniProtKB.
GO; GO:0043679; C:axon terminus; RCA:Ensembl.
GO; GO:0044295; C:axonal growth cone; RCA:Ensembl.
GO; GO:0030054; C:cell junction; RCA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; RCA:Ensembl.
GO; GO:0005737; C:cytoplasm; HMP:UniProtKB.
GO; GO:0030425; C:dendrite; HMP:UniProtKB.
GO; GO:0043198; C:dendritic shaft; HMP:ARUK-UCL.
GO; GO:0043197; C:dendritic spine; HMP:ARUK-UCL.
GO; GO:0031901; C:early endosome membrane; HMP:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; RCA:Ensembl.
GO; GO:0030175; C:filopodium; RCA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; RCA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; HMP:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; RCA:Ensembl.
GO; GO:0031594; C:neuromuscular junction; RCA:Ensembl.
GO; GO:0043204; C:perikaryon; RCA:Ensembl.
GO; GO:0005886; C:plasma membrane; IBA:Reactome.
GO; GO:0014069; C:postsynaptic density; RCA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; RCA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; RCA:UniProtKB-KW.
GO; GO:0097161; F:DH domain binding; HTP:UniProtKB.
GO; GO:0046875; F:ephrin receptor binding; RCA:Ensembl.
GO; GO:0005004; F:GPI-linked ephrin receptor activity; HMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; RCA:Ensembl.
GO; GO:0016301; F:kinase activity; IPI:ARUK-UCL.
GO; GO:0042731; F:PH domain binding; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; HTP:UniProtKB.
GO; GO:1990782; F:protein tyrosine kinase binding; IDA:ARUK-UCL.
GO; GO:0005005; F:transmembrane-ephrin receptor activity; HMP:UniProtKB.
GO; GO:0007628; P:adult walking behavior; RCA:Ensembl.
GO; GO:0007155; P:cell adhesion; RCA:UniProtKB-KW.
GO; GO:1904646; P:cellular response to amyloid-beta; HMP:ARUK-UCL.
GO; GO:0021957; P:corticospinal tract morphogenesis; HMP:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; IPI:ARUK-UCL.
GO; GO:0097156; P:fasciculation of motor neuron axon; HMP:UniProtKB.
GO; GO:0097155; P:fasciculation of sensory neuron axon; HMP:UniProtKB.
GO; GO:0008347; P:glial cell migration; RCA:Ensembl.
GO; GO:0008045; P:motor neuron axon guidance; HMP:UniProtKB.
GO; GO:0048681; P:negative regulation of axon regeneration; HMP:UniProtKB.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; HMP:ARUK-UCL.
GO; GO:0010977; P:negative regulation of neuron projection development; HMP:ARUK-UCL.
GO; GO:1903051; P:negative regulation of proteolysis involved in cellular protein catabolic process; IPI:ARUK-UCL.
GO; GO:0072178; P:nephric duct morphogenesis; RCA:Ensembl.
GO; GO:0106030; P:neuron projection fasciculation; HMP:ARUK-UCL.
GO; GO:0097485; P:neuron projection guidance; HMP:ARUK-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; HTP:UniProtKB.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IPI:ARUK-UCL.
GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IPI:ARUK-UCL.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; RCA:Ensembl.
GO; GO:0043507; P:positive regulation of JUN kinase activity; RCA:Ensembl.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; HMP:ARUK-UCL.
GO; GO:2001108; P:positive regulation of Rho guanyl-nucleotide exchange factor activity; HTP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; HTP:UniProtKB.
GO; GO:0050821; P:protein stabilization; IPI:ARUK-UCL.
GO; GO:0048710; P:regulation of astrocyte differentiation; HMP:UniProtKB.
GO; GO:0050770; P:regulation of axonogenesis; HMP:UniProtKB.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; HMP:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; HMP:UniProtKB.
GO; GO:1905244; P:regulation of modification of synaptic structure; HMP: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; Polymorphism;
Postsynaptic cell membrane; Receptor; Reference proteome; Repeat;
Signal; Synapse; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 19 {ECO:0000270}.
CHAIN 20 986 Ephrin type-A receptor 4.
/FTId=PRO_0000016807.
TOPO_DOM 20 547 Extracellular. {ECO:0000270}.
TRANSMEM 548 569 Helical. {ECO:0000270}.
TOPO_DOM 570 986 Cytoplasmic. {ECO:0000270}.
DOMAIN 30 209 Eph LBD. {ECO:0000270|PROSITE-
ProRule:PRU00883}.
DOMAIN 328 439 Fibronectin type-III 1.
{ECO:0000270|PROSITE-ProRule:PRU00316}.
DOMAIN 440 537 Fibronectin type-III 2.
{ECO:0000270|PROSITE-ProRule:PRU00316}.
DOMAIN 621 882 Protein kinase. {ECO:0000270|PROSITE-
ProRule:PRU00159}.
DOMAIN 911 975 SAM. {ECO:0000270|PROSITE-
ProRule:PRU00184}.
NP_BIND 627 635 ATP. {ECO:0000270|PROSITE-
ProRule:PRU00159}.
MOTIF 984 986 PDZ-binding. {ECO:0000270}.
COMPBIAS 191 325 Cys-rich.
ACT_SITE 746 746 Proton acceptor. {ECO:0000270|PROSITE-
ProRule:PRU00159, ECO:0000270|PROSITE-
ProRule:PRU10028}.
BINDING 653 653 ATP. {ECO:0000270|PROSITE-
ProRule:PRU00159}.
MOD_RES 596 596 Phosphotyrosine; by autocatalysis.
{ECO:0007001|UniProtKB:Q03137}.
MOD_RES 602 602 Phosphotyrosine; by autocatalysis.
{ECO:0007001|UniProtKB:Q03137}.
MOD_RES 779 779 Phosphotyrosine; by autocatalysis.
{ECO:0000270}.
MOD_RES 928 928 Phosphotyrosine; by autocatalysis.
{ECO:0000270}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000270}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000270}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000270}.
CARBOHYD 545 545 N-linked (GlcNAc...) asparagine.
{ECO:0000270}.
VAR_SEQ 1 53 MAGIFYFALFSCLFGICDAVTGSRVYPANEVTLLDSRSVQG
ELGWIASPLEGG -> MK (in isoform 2).
{ECO:0000319|PubMed:14702039}.
/FTId=VSP_056016.
VARIANT 269 269 R -> Q (in dbSNP:rs35084379).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042135.
VARIANT 370 370 G -> E (in a bladder carcinoma NOS
sample; somatic mutation;
dbSNP:rs756952113).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042136.
VARIANT 399 399 S -> F (in a metastatic melanoma sample;
somatic mutation; dbSNP:rs868224085).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042137.
VARIANT 953 953 R -> K (in dbSNP:rs35341687).
/FTId=VAR_049721.
MUTAGEN 40 40 Q->A: 10-fold reduced affinity for EFNB2;
when associated with A-42.
{ECO:0000269|PubMed:19875447}.
MUTAGEN 42 42 E->A: 10-fold reduced affinity for EFNB2;
when associated with A-40.
{ECO:0000269|PubMed:19875447}.
CONFLICT 71 71 Q -> P (in Ref. 2; BAF82995).
{ECO:0000320}.
CONFLICT 102 102 K -> R (in Ref. 2; BAF82995).
{ECO:0000320}.
CONFLICT 137 137 I -> V (in Ref. 2; BAG35298).
{ECO:0000320}.
CONFLICT 362 362 Y -> H (in Ref. 2; BAF82995).
{ECO:0000320}.
STRAND 30 35 {ECO:0000307|PDB:5JR2}.
HELIX 36 38 {ECO:0000307|PDB:5JR2}.
TURN 40 42 {ECO:0000307|PDB:4M4R}.
STRAND 46 60 {ECO:0000307|PDB:5JR2}.
STRAND 62 65 {ECO:0000307|PDB:2LW8}.
STRAND 66 73 {ECO:0000307|PDB:5JR2}.
STRAND 77 79 {ECO:0000307|PDB:5JR2}.
STRAND 82 85 {ECO:0000307|PDB:5JR2}.
STRAND 93 96 {ECO:0000307|PDB:2LW8}.
STRAND 97 105 {ECO:0000307|PDB:5JR2}.
HELIX 108 110 {ECO:0000307|PDB:5JR2}.
TURN 115 117 {ECO:0000307|PDB:2WO1}.
STRAND 120 130 {ECO:0000307|PDB:5JR2}.
STRAND 131 133 {ECO:0000307|PDB:2LW8}.
HELIX 139 141 {ECO:0000307|PDB:5JR2}.
STRAND 143 149 {ECO:0000307|PDB:5JR2}.
STRAND 154 158 {ECO:0000307|PDB:5JR2}.
TURN 159 162 {ECO:0000307|PDB:4M4P}.
STRAND 163 173 {ECO:0000307|PDB:5JR2}.
STRAND 178 189 {ECO:0000307|PDB:5JR2}.
STRAND 191 202 {ECO:0000307|PDB:5JR2}.
STRAND 207 209 {ECO:0000307|PDB:4M4P}.
STRAND 212 214 {ECO:0000307|PDB:4M4P}.
STRAND 226 230 {ECO:0000307|PDB:4M4P}.
STRAND 237 248 {ECO:0000307|PDB:4M4P}.
STRAND 257 262 {ECO:0000307|PDB:4M4P}.
STRAND 266 269 {ECO:0000307|PDB:4M4P}.
STRAND 272 275 {ECO:0000307|PDB:4M4P}.
STRAND 304 306 {ECO:0000307|PDB:4M4R}.
STRAND 333 340 {ECO:0000307|PDB:4M4P}.
STRAND 343 349 {ECO:0000307|PDB:4M4P}.
STRAND 361 368 {ECO:0000307|PDB:4M4P}.
TURN 373 375 {ECO:0000307|PDB:4M4R}.
STRAND 385 388 {ECO:0000307|PDB:4M4P}.
STRAND 390 393 {ECO:0000307|PDB:4M4P}.
STRAND 395 401 {ECO:0000307|PDB:4M4P}.
STRAND 405 416 {ECO:0000307|PDB:4M4P}.
STRAND 418 423 {ECO:0000307|PDB:4M4P}.
HELIX 426 428 {ECO:0000307|PDB:4M4P}.
STRAND 429 435 {ECO:0000307|PDB:4M4P}.
STRAND 447 452 {ECO:0000307|PDB:4M4P}.
STRAND 457 461 {ECO:0000307|PDB:4M4P}.
STRAND 473 483 {ECO:0000307|PDB:4M4P}.
STRAND 489 500 {ECO:0000307|PDB:4M4P}.
STRAND 508 517 {ECO:0000307|PDB:4M4P}.
STRAND 528 531 {ECO:0000307|PDB:4M4P}.
TURN 538 540 {ECO:0000307|PDB:4M4P}.
SEQUENCE 986 AA; 109860 MW; 0C39C1152EDDD46F CRC64;
MAGIFYFALF SCLFGICDAV TGSRVYPANE VTLLDSRSVQ GELGWIASPL EGGWEEVSIM
DEKNTPIRTY QVCNVMEPSQ NNWLRTDWIT REGAQRVYIE IKFTLRDCNS LPGVMGTCKE
TFNLYYYESD NDKERFIREN QFVKIDTIAA DESFTQVDIG DRIMKLNTEI RDVGPLSKKG
FYLAFQDVGA CIALVSVRVF YKKCPLTVRN LAQFPDTITG ADTSSLVEVR GSCVNNSEEK
DVPKMYCGAD GEWLVPIGNC LCNAGHEERS GECQACKIGY YKALSTDATC AKCPPHSYSV
WEGATSCTCD RGFFRADNDA ASMPCTRPPS APLNLISNVN ETSVNLEWSS PQNTGGRQDI
SYNVVCKKCG AGDPSKCRPC GSGVHYTPQQ NGLKTTKVSI TDLLAHTNYT FEIWAVNGVS
KYNPNPDQSV 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 TGTESSRPNT
ALLDPSSPEF SAVVSVGDWL QAIKMDRYKD NFTAAGYTTL EAVVHVNQED LARIGITAIT
HQNKILSSVQ AMRTQMQQMH GRMVPV


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