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   24-JAN-2024, entry version 210.
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}.
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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.
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   GlyCosmos; Q61772; 2 sites, No reported glycans.
DR   GlyGen; Q61772; 2 sites.
DR   iPTMnet; Q61772; -.
DR   PhosphoSitePlus; Q61772; -.
DR   MaxQB; Q61772; -.
DR   PaxDb; 10090-ENSMUSP00000029964; -.
DR   PeptideAtlas; 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; 615 antibodies from 37 providers.
DR   DNASU; 13841; -.
DR   Ensembl; ENSMUST00000029964.12; ENSMUSP00000029964.6; ENSMUSG00000028289.13. [Q61772-1]
DR   Ensembl; ENSMUST00000080934.11; ENSMUSP00000079735.5; ENSMUSG00000028289.13. [Q61772-4]
DR   Ensembl; ENSMUST00000108194.9; ENSMUSP00000103829.3; ENSMUSG00000028289.13. [Q61772-5]
DR   GeneID; 13841; -.
DR   KEGG; mmu:13841; -.
DR   UCSC; uc008sen.3; mouse. [Q61772-1]
DR   AGR; MGI:95276; -.
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   OrthoDB; 1614410at2759; -.
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 79 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 304 other cell types or tissues.
DR   ExpressionAtlas; Q61772; baseline and differential.
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:0031594; C:neuromuscular junction; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; ISO:MGI.
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: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:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
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: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   CDD; cd10485; EphR_LBD_A7; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05066; PTKc_EphR_A; 1.
DR   CDD; cd09548; SAM_EPH-A7; 1.
DR   Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
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   PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR   PANTHER; PTHR46877:SF9; EPHRIN TYPE-A RECEPTOR 7; 1.
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; PR00014; FNTYPEIII.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM01411; Ephrin_rec_like; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 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.
DR   Genevisible; Q61772; MM.
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
//