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Ephrin type-A receptor 3 (EC 2.7.10.1) (EPH-like kinase 4) (EK4) (hEK4) (HEK) (Human embryo kinase) (Tyrosine-protein kinase TYRO4) (Tyrosine-protein kinase receptor ETK1) (Eph-like tyrosine kinase 1)

 EPHA3_HUMAN             Reviewed;         983 AA.
P29320; Q9H2V3; Q9H2V4;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
22-NOV-2017, entry version 193.
RecName: Full=Ephrin type-A receptor 3;
EC=2.7.10.1;
AltName: Full=EPH-like kinase 4;
Short=EK4;
Short=hEK4;
AltName: Full=HEK;
Short=Human embryo kinase;
AltName: Full=Tyrosine-protein kinase TYRO4;
AltName: Full=Tyrosine-protein kinase receptor ETK1;
Short=Eph-like tyrosine kinase 1;
Flags: Precursor;
Name=EPHA3; Synonyms=ETK, ETK1, HEK, TYRO4;
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), AND VARIANT ARG-924.
PubMed=1311845; DOI=10.1073/pnas.89.5.1611;
Wicks I.P., Wilkinson D., Salvaris E., Boyd A.W.;
"Molecular cloning of HEK, the gene encoding a receptor tyrosine
kinase expressed by human lymphoid tumor cell lines.";
Proc. Natl. Acad. Sci. U.S.A. 89:1611-1615(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Melanoma;
PubMed=10987298;
Chiari R., Hames G., Stroobant V., Texier C., Maillere B., Boon T.,
Coulie P.G.;
"Identification of a tumor-specific shared antigen derived from an Eph
receptor and presented to CD4 T cells on HLA class II molecules.";
Cancer Res. 60:4855-4863(2000).
[3]
PROTEIN SEQUENCE OF 21-29 AND 840-860, AND CHARACTERIZATION.
PubMed=1737782;
Boyd A.W., Ward L.D., Wicks I.P., Simpson R.J., Salvaris E., Wilks A.,
Welch K., Loudovaris M., Rockman S., Busmanis I.;
"Isolation and characterization of a novel receptor-type protein
tyrosine kinase (hek) from a human pre-B cell line.";
J. Biol. Chem. 267:3262-3267(1992).
[4]
NOMENCLATURE.
PubMed=9267020;
Eph nomenclature committee;
"Unified nomenclature for Eph family receptors and their ligands, the
ephrins.";
Cell 90:403-404(1997).
[5]
FUNCTION IN CELL-CELL ADHESION, EFNA5-BINDING, SUBCELLULAR LOCATION
(ISOFORM 1), INTERACTION WITH CRK, AND PHOSPHORYLATION AT TYR-596;
TYR-602 AND TYR-779.
PubMed=11870224;
Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M.,
Down M., Boyd A.W., Alewood P.F., Lackmann M.;
"Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-
expressing 293T and melanoma cells by CrkII and Rho-mediated
signalling.";
J. Cell Sci. 115:1059-1072(2002).
[6]
INVOLVEMENT IN CRC.
PubMed=12738854; DOI=10.1126/science.1082596;
Bardelli A., Parsons D.W., Silliman N., Ptak J., Szabo S., Saha S.,
Markowitz S., Willson J.K., Parmigiani G., Kinzler K.W.,
Vogelstein B., Velculescu V.E.;
"Mutational analysis of the tyrosine kinome in colorectal cancers.";
Science 300:949-949(2003).
[7]
EPHRIN LIGAND-BINDING, OLIGOMERIZATION, MUTAGENESIS OF VAL-133 AND
PHE-152, AND INTERACTION WITH CRK.
PubMed=14660665; DOI=10.1074/jbc.M309326200;
Smith F.M., Vearing C., Lackmann M., Treutlein H., Himanen J.,
Chen K., Saul A., Nikolov D., Boyd A.W.;
"Dissecting the EphA3/Ephrin-A5 interactions using a novel functional
mutagenesis screen.";
J. Biol. Chem. 279:9522-9531(2004).
[8]
IDENTIFICATION IN A COMPLEX WITH ADAM10 AND EFNA5.
PubMed=16239146; DOI=10.1016/j.cell.2005.08.014;
Janes P.W., Saha N., Barton W.A., Kolev M.V., Wimmer-Kleikamp S.H.,
Nievergall E., Blobel C.P., Himanen J.P., Lackmann M., Nikolov D.B.;
"Adam meets Eph: an ADAM substrate recognition module acts as a
molecular switch for ephrin cleavage in trans.";
Cell 123:291-304(2005).
[9]
EFNA5 LIGAND-BINDING.
PubMed=15901737; DOI=10.1074/jbc.M504972200;
Day B., To C., Himanen J.P., Smith F.M., Nikolov D.B., Boyd A.W.,
Lackmann M.;
"Three distinct molecular surfaces in ephrin-A5 are essential for a
functional interaction with EphA3.";
J. Biol. Chem. 280:26526-26532(2005).
[10]
INTERACTION WITH PTPN1, PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN1,
AND SUBCELLULAR LOCATION (ISOFORM 2).
PubMed=21135139; DOI=10.1083/jcb.201005035;
Nievergall E., Janes P.W., Stegmayer C., Vail M.E., Haj F.G.,
Teng S.W., Neel B.G., Bastiaens P.I., Lackmann M.;
"PTP1B regulates Eph receptor function and trafficking.";
J. Cell Biol. 191:1189-1203(2010).
[11]
X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) OF 577-947 IN COMPLEX WITH ATP
ANALOG, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT
TYR-596; TYR-602 AND TYR-701, AND MUTAGENESIS OF TYR-596; TYR-602;
TYR-742 AND SER-768.
PubMed=18547520; DOI=10.1016/j.str.2008.03.008;
Davis T.L., Walker J.R., Loppnau P., Butler-Cole C.,
Allali-Hassani A., Dhe-Paganon S.;
"Autoregulation by the juxtamembrane region of the human ephrin
receptor tyrosine kinase A3 (EphA3).";
Structure 16:873-884(2008).
[12]
VARIANTS [LARGE SCALE ANALYSIS] LYS-37; SER-85; LEU-621 AND ASN-806.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[13]
VARIANTS LYS-660 AND MET-933.
PubMed=16941478; DOI=10.1002/humu.9452;
Wood L.D., Calhoun E.S., Silliman N., Ptak J., Szabo S., Powell S.M.,
Riggins G.J., Wang T.L., Yan H., Gazdar A., Kern S.E., Pennacchio L.,
Kinzler K.W., Vogelstein B., Velculescu V.E.;
"Somatic mutations of GUCY2F, EPHA3, and NTRK3 in human cancers.";
Hum. Mutat. 27:1060-1061(2006).
[14]
VARIANTS [LARGE SCALE ANALYSIS] TYR-229; PHE-449; LEU-518; VAL-564;
SER-568; PRO-590; GLU-766; GLY-777; HIS-914 AND ARG-924.
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).
[15]
VARIANT ASN-207.
PubMed=20838624; DOI=10.1371/journal.pone.0012653;
Corbo V., Ritelli R., Barbi S., Funel N., Campani D., Bardelli A.,
Scarpa A.;
"Mutational profiling of kinases in human tumours of pancreatic origin
identifies candidate cancer genes in ductal and ampulla of vater
carcinomas.";
PLoS ONE 5:E12653-E12653(2010).
-!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
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 for ephrin-A ligands it binds
preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell
adhesion, cytoskeletal organization and cell migration. Plays a
role in cardiac cells migration and differentiation and regulates
the formation of the atrioventricular canal and septum during
development probably through activation by EFNA1. Involved in the
retinotectal mapping of neurons. May also control the segregation
but not the guidance of motor and sensory axons during
neuromuscular circuit development. {ECO:0000269|PubMed:11870224}.
-!- 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. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating
EFNA5 extracellular domain shedding by ADAM10 which regulates the
EFNA5-EPHA3 complex internalization and function. Interacts with
NCK1 (via SH2 domain); mediates EFNA5-EPHA3 signaling (By
similarity). Interacts (phosphorylated) with PTPN1;
dephosphorylates EPHA3 and may regulate its trafficking and
function. Interacts (phosphorylated) with CRK; mediates EFNA5-
EPHA3 signaling through RHOA GTPase activation. {ECO:0000250,
ECO:0000269|PubMed:11870224, ECO:0000269|PubMed:14660665,
ECO:0000269|PubMed:16239146, ECO:0000269|PubMed:18547520,
ECO:0000269|PubMed:21135139}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:11870224}; Single-pass type I membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted
{ECO:0000269|PubMed:21135139}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P29320-1; Sequence=Displayed;
Name=2;
IsoId=P29320-2; Sequence=VSP_002995, VSP_002996;
-!- TISSUE SPECIFICITY: Widely expressed. Highest level in placenta.
-!- PTM: Autophosphorylates upon activation by EFNA5. Phosphorylation
on Tyr-602 mediates interaction with NCK1. Dephosphorylated by
PTPN1. {ECO:0000269|PubMed:11870224, ECO:0000269|PubMed:18547520,
ECO:0000269|PubMed:21135139}.
-!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
characterized by malignant lesions arising from the inner wall of
the large intestine (the colon) and the rectum. Genetic
alterations are often associated with progression from
premalignant lesion (adenoma) to invasive adenocarcinoma. Risk
factors for cancer of the colon and rectum include colon polyps,
long-standing ulcerative colitis, and genetic family history.
{ECO:0000269|PubMed:12738854}. Note=The gene represented in this
entry may be involved in disease pathogenesis.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/EPHA3ID40463ch3p11.html";
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EMBL; M83941; AAA58633.1; -; mRNA.
EMBL; AF213459; AAG43576.1; -; mRNA.
EMBL; AF213460; AAG43577.1; -; mRNA.
CCDS; CCDS2922.1; -. [P29320-1]
CCDS; CCDS46875.1; -. [P29320-2]
PIR; A38224; A38224.
RefSeq; NP_005224.2; NM_005233.5. [P29320-1]
RefSeq; NP_872585.1; NM_182644.2. [P29320-2]
UniGene; Hs.123642; -.
PDB; 2GSF; X-ray; 1.77 A; A=577-947.
PDB; 2QO2; X-ray; 1.60 A; A=577-947.
PDB; 2QO7; X-ray; 1.60 A; A=577-947.
PDB; 2QO9; X-ray; 1.55 A; A=577-947.
PDB; 2QOB; X-ray; 1.65 A; A=609-947.
PDB; 2QOC; X-ray; 1.25 A; A=609-947.
PDB; 2QOD; X-ray; 1.15 A; A=577-947.
PDB; 2QOF; X-ray; 1.20 A; A=577-947.
PDB; 2QOI; X-ray; 1.25 A; A=577-947.
PDB; 2QOK; X-ray; 1.20 A; A=577-947.
PDB; 2QOL; X-ray; 1.07 A; A=577-947.
PDB; 2QON; X-ray; 1.79 A; A=577-947.
PDB; 2QOO; X-ray; 1.25 A; A=577-947.
PDB; 2QOQ; X-ray; 1.60 A; A=577-947.
PDB; 3DZQ; X-ray; 1.75 A; A=609-947.
PDB; 3FXX; X-ray; 1.70 A; A=577-947.
PDB; 3FY2; X-ray; 1.80 A; A=577-947.
PDB; 4G2F; X-ray; 1.70 A; A=609-947.
PDB; 4GK2; X-ray; 2.20 A; A=609-947.
PDB; 4GK3; X-ray; 1.90 A; A=609-947.
PDB; 4GK4; X-ray; 2.10 A; A=609-947.
PDB; 4L0P; X-ray; 2.26 A; A=29-201.
PDB; 4P4C; X-ray; 1.60 A; A=609-947.
PDB; 4P5Q; X-ray; 1.35 A; A=606-947.
PDB; 4P5Z; X-ray; 2.00 A; A=606-947.
PDB; 4TWN; X-ray; 1.71 A; A=609-947.
PDB; 4TWO; X-ray; 2.05 A; A=609-947.
PDBsum; 2GSF; -.
PDBsum; 2QO2; -.
PDBsum; 2QO7; -.
PDBsum; 2QO9; -.
PDBsum; 2QOB; -.
PDBsum; 2QOC; -.
PDBsum; 2QOD; -.
PDBsum; 2QOF; -.
PDBsum; 2QOI; -.
PDBsum; 2QOK; -.
PDBsum; 2QOL; -.
PDBsum; 2QON; -.
PDBsum; 2QOO; -.
PDBsum; 2QOQ; -.
PDBsum; 3DZQ; -.
PDBsum; 3FXX; -.
PDBsum; 3FY2; -.
PDBsum; 4G2F; -.
PDBsum; 4GK2; -.
PDBsum; 4GK3; -.
PDBsum; 4GK4; -.
PDBsum; 4L0P; -.
PDBsum; 4P4C; -.
PDBsum; 4P5Q; -.
PDBsum; 4P5Z; -.
PDBsum; 4TWN; -.
PDBsum; 4TWO; -.
ProteinModelPortal; P29320; -.
SMR; P29320; -.
BioGrid; 108356; 28.
DIP; DIP-40307N; -.
IntAct; P29320; 9.
MINT; MINT-7145005; -.
STRING; 9606.ENSP00000337451; -.
BindingDB; P29320; -.
ChEMBL; CHEMBL4954; -.
GuidetoPHARMACOLOGY; 1823; -.
iPTMnet; P29320; -.
PhosphoSitePlus; P29320; -.
BioMuta; EPHA3; -.
DMDM; 116241351; -.
MaxQB; P29320; -.
PaxDb; P29320; -.
PeptideAtlas; P29320; -.
PRIDE; P29320; -.
DNASU; 2042; -.
Ensembl; ENST00000336596; ENSP00000337451; ENSG00000044524. [P29320-1]
Ensembl; ENST00000452448; ENSP00000399926; ENSG00000044524. [P29320-2]
GeneID; 2042; -.
KEGG; hsa:2042; -.
UCSC; uc003dqx.2; human. [P29320-1]
CTD; 2042; -.
DisGeNET; 2042; -.
EuPathDB; HostDB:ENSG00000044524.10; -.
GeneCards; EPHA3; -.
HGNC; HGNC:3387; EPHA3.
HPA; CAB010462; -.
MIM; 114500; phenotype.
MIM; 179611; gene.
neXtProt; NX_P29320; -.
OpenTargets; ENSG00000044524; -.
PharmGKB; PA27819; -.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; P29320; -.
KO; K05104; -.
OMA; SSCDTIA; -.
OrthoDB; EOG091G00W0; -.
PhylomeDB; P29320; -.
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; P29320; -.
SIGNOR; P29320; -.
EvolutionaryTrace; P29320; -.
GeneWiki; EPH_receptor_A3; -.
GenomeRNAi; 2042; -.
PRO; PR:P29320; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000044524; -.
CleanEx; HS_EPHA3; -.
ExpressionAtlas; P29320; baseline and differential.
Genevisible; P29320; HS.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005004; F:GPI-linked ephrin receptor activity; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0097156; P:fasciculation of motor neuron axon; ISS:UniProtKB.
GO; GO:0097155; P:fasciculation of sensory neuron axon; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0051893; P:regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IDA:UniProtKB.
CDD; cd10481; EphR_LBD_A3; 1.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034266; EphA3_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; PF07699; Ephrin_rec_like; 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; 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;
3D-structure; Alternative splicing; ATP-binding; Cell adhesion;
Cell membrane; Complete proteome; Direct protein sequencing;
Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 20 {ECO:0000269|PubMed:1737782}.
CHAIN 21 983 Ephrin type-A receptor 3.
/FTId=PRO_0000016802.
TOPO_DOM 21 541 Extracellular. {ECO:0000255}.
TRANSMEM 542 565 Helical. {ECO:0000255}.
TOPO_DOM 566 983 Cytoplasmic. {ECO:0000255}.
DOMAIN 29 207 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 325 435 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 436 531 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 628 633 ATP.
NP_BIND 700 706 ATP.
NP_BIND 750 751 ATP.
MOTIF 981 983 PDZ-binding. {ECO:0000255}.
COMPBIAS 189 322 Cys-rich.
ACT_SITE 746 746 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 653 653 ATP.
MOD_RES 596 596 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11870224,
ECO:0000269|PubMed:18547520}.
MOD_RES 602 602 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11870224,
ECO:0000269|PubMed:18547520}.
MOD_RES 701 701 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:18547520}.
MOD_RES 779 779 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11870224}.
MOD_RES 937 937 Phosphotyrosine.
{ECO:0000250|UniProtKB:P29319}.
CARBOHYD 232 232 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 391 391 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 404 404 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 493 493 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 532 539 SFSISGES -> CMYYFNAV (in isoform 2).
{ECO:0000303|PubMed:10987298}.
/FTId=VSP_002995.
VAR_SEQ 540 983 Missing (in isoform 2).
{ECO:0000303|PubMed:10987298}.
/FTId=VSP_002996.
VARIANT 37 37 T -> K (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036086.
VARIANT 85 85 N -> S (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036087.
VARIANT 207 207 K -> N (in a pancreatic ductal
adenocarcinoma sample; somatic mutation;
dbSNP:rs200567888).
{ECO:0000269|PubMed:20838624}.
/FTId=VAR_068853.
VARIANT 229 229 S -> Y (in a lung large cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042126.
VARIANT 449 449 S -> F (in a lung neuroendocrine
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042127.
VARIANT 518 518 G -> L (in a lung squamous cell carcinoma
sample; somatic mutation; requires 2
nucleotide substitutions).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042128.
VARIANT 564 564 I -> V (in dbSNP:rs55712516).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042129.
VARIANT 568 568 C -> S (in dbSNP:rs56077781).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042130.
VARIANT 590 590 L -> P (in dbSNP:rs56081642).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042131.
VARIANT 621 621 I -> L (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036088.
VARIANT 660 660 T -> K (in a lung carcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:16941478}.
/FTId=VAR_065831.
VARIANT 766 766 G -> E (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042132.
VARIANT 777 777 A -> G (in dbSNP:rs34437982).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042133.
VARIANT 806 806 D -> N (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036089.
VARIANT 914 914 R -> H (in dbSNP:rs17801309).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_027919.
VARIANT 924 924 W -> R (in dbSNP:rs35124509).
{ECO:0000269|PubMed:1311845,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_042134.
VARIANT 933 933 T -> M (in a lung carcinoma sample;
somatic mutation; dbSNP:rs372594677).
{ECO:0000269|PubMed:16941478}.
/FTId=VAR_065832.
MUTAGEN 133 133 V->E: Loss of EFNA5-binding ability and
function. {ECO:0000269|PubMed:14660665}.
MUTAGEN 152 152 F->L: Loss of EFNA5-binding ability and
function. {ECO:0000269|PubMed:14660665}.
MUTAGEN 596 596 Y->F: 10-fold suppression of kinase
activity; when associated with F-602.
Full kinase activity; when associated
with F-602 and F-742. Full kinase
activity; when associated with F-602 and
A-768. {ECO:0000269|PubMed:18547520}.
MUTAGEN 602 602 Y->F: 10-fold suppression of kinase
activity; when associated with F-596.
Full kinase activity; when associated
with F-596 and F-742. Full kinase
activity; when associated with F-596 and
A-768. {ECO:0000269|PubMed:18547520}.
MUTAGEN 742 742 Y->F: Full kinase activity; when
associated with F-596 and F-602.
{ECO:0000269|PubMed:18547520}.
MUTAGEN 768 768 S->A: Full kinase activity; when
associated with F-596 and F-602.
{ECO:0000269|PubMed:18547520}.
CONFLICT 911 911 T -> S (in Ref. 1; AAA58633).
{ECO:0000305}.
STRAND 29 34 {ECO:0000244|PDB:4L0P}.
TURN 38 41 {ECO:0000244|PDB:4L0P}.
STRAND 45 48 {ECO:0000244|PDB:4L0P}.
STRAND 51 58 {ECO:0000244|PDB:4L0P}.
STRAND 64 71 {ECO:0000244|PDB:4L0P}.
STRAND 75 77 {ECO:0000244|PDB:4L0P}.
STRAND 80 83 {ECO:0000244|PDB:4L0P}.
STRAND 96 104 {ECO:0000244|PDB:4L0P}.
HELIX 106 108 {ECO:0000244|PDB:4L0P}.
STRAND 117 128 {ECO:0000244|PDB:4L0P}.
STRAND 130 132 {ECO:0000244|PDB:4L0P}.
HELIX 137 139 {ECO:0000244|PDB:4L0P}.
STRAND 141 147 {ECO:0000244|PDB:4L0P}.
HELIX 154 159 {ECO:0000244|PDB:4L0P}.
STRAND 165 170 {ECO:0000244|PDB:4L0P}.
STRAND 176 200 {ECO:0000244|PDB:4L0P}.
TURN 610 612 {ECO:0000244|PDB:2QOL}.
HELIX 618 620 {ECO:0000244|PDB:2QOL}.
STRAND 621 629 {ECO:0000244|PDB:2QOL}.
STRAND 631 641 {ECO:0000244|PDB:2QOL}.
STRAND 647 654 {ECO:0000244|PDB:2QOL}.
HELIX 661 674 {ECO:0000244|PDB:2QOL}.
STRAND 685 689 {ECO:0000244|PDB:2QOL}.
STRAND 691 694 {ECO:0000244|PDB:2QOL}.
STRAND 696 700 {ECO:0000244|PDB:2QOL}.
HELIX 707 712 {ECO:0000244|PDB:2QOL}.
TURN 713 716 {ECO:0000244|PDB:2QOL}.
HELIX 720 739 {ECO:0000244|PDB:2QOL}.
HELIX 749 751 {ECO:0000244|PDB:2QOL}.
STRAND 752 754 {ECO:0000244|PDB:2QOL}.
STRAND 760 762 {ECO:0000244|PDB:2QOL}.
HELIX 765 768 {ECO:0000244|PDB:4TWN}.
HELIX 788 790 {ECO:0000244|PDB:2QOD}.
HELIX 793 798 {ECO:0000244|PDB:2QOL}.
HELIX 803 818 {ECO:0000244|PDB:2QOL}.
TURN 819 821 {ECO:0000244|PDB:2QO9}.
TURN 824 827 {ECO:0000244|PDB:2QOL}.
HELIX 830 838 {ECO:0000244|PDB:2QOL}.
HELIX 851 860 {ECO:0000244|PDB:2QOL}.
HELIX 865 867 {ECO:0000244|PDB:2QOL}.
HELIX 871 883 {ECO:0000244|PDB:2QOL}.
HELIX 885 889 {ECO:0000244|PDB:2QOL}.
STRAND 890 892 {ECO:0000244|PDB:4G2F}.
STRAND 898 903 {ECO:0000244|PDB:2QOC}.
SEQUENCE 983 AA; 110131 MW; BE04DBF958245424 CRC64;
MDCQLSILLL LSCSVLDSFG ELIPQPSNEV NLLDSKTIQG ELGWISYPSH GWEEISGVDE
HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK FTLRDCNSIP LVLGTCKETF
NLYYMESDDD HGVKFREHQF TKIDTIAADE SFTQMDLGDR ILKLNTEIRE VGPVNKKGFY
LAFQDVGACV ALVSVRVYFK KCPFTVKNLA MFPDTVPMDS QSLVEVRGSC VNNSKEEDPP
RMYCSTEGEW LVPIGKCSCN AGYEERGFMC QACRPGFYKA LDGNMKCAKC PPHSSTQEDG
SMNCRCENNY FRADKDPPSM ACTRPPSSPR NVISNINETS VILDWSWPLD TGGRKDVTFN
IICKKCGWNI KQCEPCSPNV RFLPRQFGLT NTTVTVTDLL AHTNYTFEID AVNGVSELSS
PPRQFAAVSI TTNQAAPSPV LTIKKDRTSR NSISLSWQEP EHPNGIILDY EVKYYEKQEQ
ETSYTILRAR GTNVTISSLK PDTIYVFQIR ARTAAGYGTN SRKFEFETSP DSFSISGESS
QVVMIAISAA VAIILLTVVI YVLIGRFCGY KSKHGADEKR LHFGNGHLKL PGLRTYVDPH
TYEDPTQAVH EFAKELDATN ISIDKVVGAG EFGEVCSGRL KLPSKKEISV AIKTLKVGYT
EKQRRDFLGE ASIMGQFDHP NIIRLEGVVT KSKPVMIVTE YMENGSLDSF LRKHDAQFTV
IQLVGMLRGI ASGMKYLSDM GYVHRDLAAR NILINSNLVC KVSDFGLSRV LEDDPEAAYT
TRGGKIPIRW TSPEAIAYRK FTSASDVWSY GIVLWEVMSY GERPYWEMSN QDVIKAVDEG
YRLPPPMDCP AALYQLMLDC WQKDRNNRPK FEQIVSILDK LIRNPGSLKI ITSAAARPSN
LLLDQSNVDI TTFRTTGDWL NGVWTAHCKE IFTGVEYSSC DTIAKISTDD MKKVGVTVVG
PQKKIISSIK ALETQSKNGP VPV


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