EPHA7_MOUSE
ID EPHA7_MOUSE Reviewed; 998 AA.
AC Q61772; Q61505; Q61773; Q61774; Q8BSU8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Ephrin type-A receptor 7;
DE EC=2.7.10.1;
DE AltName: Full=Developmental kinase 1;
DE Short=mDK-1;
DE AltName: Full=EPH homology kinase 3;
DE Short=EHK-3;
DE AltName: Full=Embryonic brain kinase;
DE Short=EBK;
DE Flags: Precursor;
GN Name=Epha7; Synonyms=Ebk, Ehk3, Mdk1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7824284;
RA Ciossek T., Millauer B., Ullrich A.;
RT "Identification of alternatively spliced mRNAs encoding variants of MDK1, a
RT novel receptor tyrosine kinase expressed in the murine nervous system.";
RL Oncogene 10:97-108(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9368721; DOI=10.1247/csf.22.477;
RA Talukder A.H., Muramatsu T., Kaneda N.;
RT "A novel truncated variant form of Ebk/MDK1 receptor tyrosine kinase is
RT expressed in embryonic mouse brain.";
RL Cell Struct. Funct. 22:477-485(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 431-998 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8541219; DOI=10.1016/0925-4773(95)00411-s;
RA Ellis J., Liu Q., Breitman M., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA Tempest H.V., Warren S., Muir E., Schilling H., Fletcher F.A.,
RA Ziegler S.F., Rogers J.H.;
RT "Embryo brain kinase: a novel gene of the eph/elk receptor tyrosine kinase
RT family.";
RL Mech. Dev. 52:319-341(1995).
RN [7]
RP INTERACTION WITH GRIP1 AND PICK1, AND IDENTIFICATION OF PDZ-BINDING MOTIF.
RX PubMed=9883737; DOI=10.1016/s0896-6273(00)80663-7;
RA Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N.,
RA Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.;
RT "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors
RT and their ephrin ligands.";
RL Neuron 21:1453-1463(1998).
RN [8]
RP FUNCTION IN CELL ADHESION AND REPULSION (ISOFORMS 1 AND 4), EFNA5
RP LIGAND-BINDING, PHOSPHORYLATION, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11089974; DOI=10.1038/35041577;
RA Holmberg J., Clarke D.L., Frisen J.;
RT "Regulation of repulsion versus adhesion by different splice forms of an
RT Eph receptor.";
RL Nature 408:203-206(2000).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN APOPTOSIS.
RX PubMed=15902206; DOI=10.1038/nature03651;
RA Depaepe V., Suarez-Gonzalez N., Dufour A., Passante L., Gorski J.A.,
RA Jones K.R., Ledent C., Vanderhaeghen P.;
RT "Ephrin signalling controls brain size by regulating apoptosis of neural
RT progenitors.";
RL Nature 435:1244-1250(2005).
RN [10]
RP DISRUPTION PHENOTYPE, FUNCTION IN TOPOGRAPHIC MAPPING, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15996548; DOI=10.1016/j.neuron.2005.05.030;
RA Rashid T., Upton A.L., Blentic A., Ciossek T., Knoell B., Thompson I.D.,
RA Drescher U.;
RT "Opposing gradients of ephrin-As and EphA7 in the superior colliculus are
RT essential for topographic mapping in the mammalian visual system.";
RL Neuron 47:57-69(2005).
RN [11]
RP FUNCTION IN CORTICOTHALAMIC AXON GUIDANCE.
RX PubMed=16301174; DOI=10.1016/j.neuron.2005.09.021;
RA Torii M., Levitt P.;
RT "Dissociation of corticothalamic and thalamocortical axon targeting by an
RT EphA7-mediated mechanism.";
RL Neuron 48:563-575(2005).
RN [12]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT "Gene expression profiling of muscle stem cells identifies novel regulators
RT of postnatal myogenesis.";
RL Front. Cell Dev. Biol. 4:58-58(2016).
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-
CC anchored ephrin-A family ligands residing on adjacent cells, leading to
CC contact-dependent bidirectional signaling into neighboring cells. The
CC signaling pathway downstream of the receptor is referred to as forward
CC signaling while the signaling pathway downstream of the ephrin ligand
CC is referred to as reverse signaling. Among GPI-anchored ephrin-A
CC ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their
CC interaction regulates brain development modulating cell-cell adhesion
CC and repulsion. Has a repellent activity on axons and is for instance
CC involved in the guidance of corticothalamic axons and in the proper
CC topographic mapping of retinal axons to the colliculus. May also
CC regulate brain development through a caspase(CASP3)-dependent
CC proapoptotic activity. Forward signaling may result in activation of
CC components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1
CC AND MAPK3 which are phosphorylated upon activation of EPHA7. Isoform 4
CC which lacks the kinase domain may regulate isoform 1 adhesive
CC properties. {ECO:0000269|PubMed:15902206, ECO:0000269|PubMed:15996548,
CC ECO:0000269|PubMed:16301174}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer
CC is composed of an ephrin dimer and a receptor dimer. Oligomerization is
CC probably required to induce biological responses (By similarity).
CC Interacts (via PDZ-binding motif) with GRIP1 and PICK1 (via PDZ
CC domain). {ECO:0000250, ECO:0000269|PubMed:9883737}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11089974};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:11089974}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=MDK1, EPHA7-FL;
CC IsoId=Q61772-1; Sequence=Displayed;
CC Name=2; Synonyms=MDK1-1, Ebk-td1;
CC IsoId=Q61772-2; Sequence=VSP_003006;
CC Name=3; Synonyms=MDK1-2;
CC IsoId=Q61772-3; Sequence=VSP_003007;
CC Name=4; Synonyms=MDK1-T1, EPHA7-T1;
CC IsoId=Q61772-4; Sequence=VSP_003008, VSP_003009;
CC Name=5; Synonyms=MDK1-T2, EPHA7-T2;
CC IsoId=Q61772-5; Sequence=VSP_003010, VSP_003011;
CC -!- TISSUE SPECIFICITY: Widely expressed in embryo. In adult, expression
CC restricted to hippocampus, testis and spleen. Expressed in myogenic
CC progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: During visual system development, expressed in an
CC anterior to posterior decreasing gradient stretching through the entire
CC midbrain. This gradient has the reverse orientation to the one defined
CC by the expression of ephrins. Isoform 4 and isoform 5 are expressed at
CC the edges of the embryonic cranial neural fold. In myogenic progenitor
CC cells, highly expressed, at least as early as 11.5 dpc, expression
CC decreases until 4 weeks after birth (PubMed:27446912).
CC {ECO:0000269|PubMed:11089974, ECO:0000269|PubMed:15996548,
CC ECO:0000269|PubMed:27446912}.
CC -!- PTM: Phosphorylated. Isoform 4 inhibits isoform 1 phosphorylation and
CC may regulate its function in adhesion. {ECO:0000269|PubMed:11089974}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable, fertile and show no gross
CC morphological or behavioral defects. However, topographic targeting
CC errors of nasal and temporal retinal axons appear during development of
CC the retinocollicular projections in the visual system. 10 percent of
CC the embryos also display exencephalic overgrowth of forebrain tissues
CC which might be the result of reduced apoptosis.
CC {ECO:0000269|PubMed:15902206, ECO:0000269|PubMed:15996548}.
CC -!- MISCELLANEOUS: [Isoform 4]: Truncated receptor lacking the kinase
CC domain. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Truncated receptor lacking the kinase
CC domain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X79082; CAA55687.1; -; mRNA.
DR EMBL; X79083; CAA55688.1; -; mRNA.
DR EMBL; X79084; CAA55689.1; -; mRNA.
DR EMBL; AK030480; BAC26982.1; -; mRNA.
DR EMBL; BX000989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466538; EDL05518.1; -; Genomic_DNA.
DR EMBL; X81466; CAA57224.1; -; mRNA.
DR CCDS; CCDS18013.1; -. [Q61772-1]
DR CCDS; CCDS51132.1; -. [Q61772-4]
DR CCDS; CCDS71353.1; -. [Q61772-3]
DR PIR; I48612; I48612.
DR PIR; I48614; I48614.
DR PIR; JC5672; JC5672.
DR RefSeq; NP_001277363.1; NM_001290434.1.
DR RefSeq; NP_034271.3; NM_010141.4. [Q61772-1]
DR RefSeq; XP_006537669.1; XM_006537606.3. [Q61772-2]
DR RefSeq; XP_006537670.1; XM_006537607.3. [Q61772-5]
DR AlphaFoldDB; Q61772; -.
DR SMR; Q61772; -.
DR BioGRID; 199474; 2.
DR STRING; 10090.ENSMUSP00000029964; -.
DR BindingDB; Q61772; -.
DR ChEMBL; CHEMBL4739689; -.
DR GuidetoPHARMACOLOGY; 1827; -.
DR GlyGen; Q61772; 2 sites.
DR iPTMnet; Q61772; -.
DR PhosphoSitePlus; Q61772; -.
DR MaxQB; Q61772; -.
DR PaxDb; Q61772; -.
DR PeptideAtlas; Q61772; -.
DR PRIDE; Q61772; -.
DR ProteomicsDB; 275757; -. [Q61772-1]
DR ProteomicsDB; 275758; -. [Q61772-2]
DR ProteomicsDB; 275759; -. [Q61772-3]
DR ProteomicsDB; 275760; -. [Q61772-4]
DR ProteomicsDB; 275761; -. [Q61772-5]
DR Antibodypedia; 642; 556 antibodies from 37 providers.
DR DNASU; 13841; -.
DR Ensembl; ENSMUST00000029964; ENSMUSP00000029964; ENSMUSG00000028289. [Q61772-1]
DR Ensembl; ENSMUST00000080934; ENSMUSP00000079735; ENSMUSG00000028289. [Q61772-4]
DR Ensembl; ENSMUST00000108194; ENSMUSP00000103829; ENSMUSG00000028289. [Q61772-5]
DR GeneID; 13841; -.
DR KEGG; mmu:13841; -.
DR UCSC; uc008sen.3; mouse. [Q61772-1]
DR CTD; 2045; -.
DR MGI; MGI:95276; Epha7.
DR VEuPathDB; HostDB:ENSMUSG00000028289; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000160189; -.
DR HOGENOM; CLU_000288_141_3_1; -.
DR InParanoid; Q61772; -.
DR OMA; ETDYNTG; -.
DR PhylomeDB; Q61772; -.
DR TreeFam; TF315608; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-2682334; EPH-Ephrin signaling.
DR Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR BioGRID-ORCS; 13841; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Epha7; mouse.
DR PRO; PR:Q61772; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q61772; protein.
DR Bgee; ENSMUSG00000028289; Expressed in vestibular membrane of cochlear duct and 303 other tissues.
DR ExpressionAtlas; Q61772; baseline and differential.
DR Genevisible; Q61772; MM.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008046; F:axon guidance receptor activity; IMP:UniProtKB.
DR GO; GO:0045499; F:chemorepellent activity; IDA:MGI.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:MGI.
DR GO; GO:0005004; F:GPI-linked ephrin receptor activity; IDA:UniProtKB.
DR GO; GO:0019838; F:growth factor binding; IPI:ARUK-UCL.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; IMP:MGI.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; IDA:BHF-UCL.
DR GO; GO:0051964; P:negative regulation of synapse assembly; IDA:BHF-UCL.
DR GO; GO:0072178; P:nephric duct morphogenesis; IGI:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:0031952; P:regulation of protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10485; EphR_LBD_A7; 1.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034283; EphA7_rcpt_lig-bd.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; ATP-binding; Cell membrane;
KW Developmental protein; Glycoprotein; Kinase; Membrane; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..998
FT /note="Ephrin type-A receptor 7"
FT /id="PRO_0000016819"
FT TOPO_DOM 28..555
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..998
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..210
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 331..441
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 442..537
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 633..894
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 923..987
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 996..998
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 758
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 639..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 608
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 614
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 791
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 940
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 540..544
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9368721"
FT /id="VSP_003006"
FT VAR_SEQ 600..626
FT /note="FKFPGTKTYIDPETYEDPNRAVHQFAK -> SLYRERGDGMEKTQHNKKWMI
FT ASCSRL (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003010"
FT VAR_SEQ 600..610
FT /note="FKFPGTKTYID -> SLVTNEHLSVL (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003008"
FT VAR_SEQ 601..604
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003007"
FT VAR_SEQ 611..998
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003009"
FT VAR_SEQ 627..998
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003011"
FT CONFLICT 207
FT /note="S -> T (in Ref. 1; CAA55687/CAA55688/CAA55689)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="Y -> H (in Ref. 6; CAA57224)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="K -> Q (in Ref. 1; CAA55687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 998 AA; 111860 MW; FCA1E83490E746E1 CRC64;
MVVQTRFPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPSGWEEISG
LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK
ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK
GFYLAFQDVG ACIALVSVKV YYKKCWSIVE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE
EAENSPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS
FSDREGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR
NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG
VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVQ LSWQEPEHPN GVITEYEIKY
YEKDQRERTY STLKTKSTSA SINNLKPGTV YVFQIRAVTA AGYGNYSPRL DVATLEEASG
KMFEATAVSS EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF
KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG RLKLPGKRDV
AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV VTRGKPVMIV IEFMENGALD
AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA DMGYVHRDLA ARNILVNSNL VCKVSDFGLS
RVIEDDPEAV YTTTGGKIPV RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM
SNQDVIKAIE EGYRLPAPMD CPAGLHQLML DCWQKDRAER PKFEQIVGIL DKMIRNPSSL
KTPLGTCSRP LSPLLDQSTP DFTAFCSVGE WLQAIKMERY KDNFTAAGYN SLESVARMTI
DDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV
