ID EPHA7_HUMAN Reviewed; 998 AA. AC Q15375; A0AUX7; B2R8W1; B7ZLJ9; B7ZLK0; Q59G40; Q5VTU0; Q8N368; Q9H124; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 3. DT 24-JAN-2024, entry version 228. DE RecName: Full=Ephrin type-A receptor 7; DE EC=2.7.10.1; DE AltName: Full=EPH homology kinase 3; DE Short=EHK-3; DE AltName: Full=EPH-like kinase 11; DE Short=EK11; DE Short=hEK11; DE Flags: Precursor; GN Name=EPHA7; Synonyms=EHK3, HEK11; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=7898931; RA Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M., Basu R., RA Welcher A.A.; RT "cDNA cloning and tissue distribution of five human EPH-like receptor RT protein-tyrosine kinases."; RL Oncogene 10:897-905(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND RP VARIANT VAL-138. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NOMENCLATURE. RX PubMed=9267020; DOI=10.1016/s0092-8674(00)80500-0; RG Eph nomenclature committee; RT "Unified nomenclature for Eph family receptors and their ligands, the RT ephrins."; RL Cell 90:403-404(1997). RN [8] RP FUNCTION IN MAP2K1; MAP2K2; MAPK1 AND MAPK3 PHOSPHORYLATION. RX PubMed=17726105; DOI=10.1073/pnas.0703211104; RA Nakanishi H., Nakamura T., Canaani E., Croce C.M.; RT "ALL1 fusion proteins induce deregulation of EphA7 and ERK phosphorylation RT in human acute leukemias."; RL Proc. Natl. Acad. Sci. U.S.A. 104:14442-14447(2007). RN [9] RP ALTERNATIVE SPLICING (ISOFORM 5). RX PubMed=20126984; RA Tsuboi M., Mori H., Bunai T., Kageyama S., Suzuki M., Okudela K., RA Takamochi K., Ogawa H., Niwa H., Shinmura K., Sugimura H.; RT "Secreted form of EphA7 in lung cancer."; RL Int. J. Oncol. 36:635-640(2010). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 32-204. RA Walker J.R., Yermekbayeva L., Seitova A., Kania J., Bountra C., Weigelt J., RA Arrowsmith C.H., Edwards A.M., Bochkarev A., Dhe-Paganon S.; RT "Ephrin A7 ligand binding domain."; RL Submitted (JUN-2010) to the PDB data bank. RN [11] RP VARIANT [LARGE SCALE ANALYSIS] TRP-371. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [12] RP VARIANTS [LARGE SCALE ANALYSIS] VAL-138; LYS-170; ARG-232; SER-278 AND RP SER-903. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). 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. CC {ECO:0000269|PubMed:17726105}. 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 domain) CC (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q15375; P07333: CSF1R; NbExp=2; IntAct=EBI-1383428, EBI-2835440; CC Q15375; P29317: EPHA2; NbExp=6; IntAct=EBI-1383428, EBI-702104; CC Q15375; P29320: EPHA3; NbExp=2; IntAct=EBI-1383428, EBI-1641575; CC Q15375; P29323: EPHB2; NbExp=2; IntAct=EBI-1383428, EBI-1059294; CC Q15375; P54760: EPHB4; NbExp=3; IntAct=EBI-1383428, EBI-702121; CC Q15375; Q16288: NTRK3; NbExp=2; IntAct=EBI-1383428, EBI-3936704; CC Q15375; P52793: Efna1; Xeno; NbExp=2; IntAct=EBI-1383428, EBI-5241529; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=EPHA7-FL; CC IsoId=Q15375-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15375-2; Sequence=VSP_014382; CC Name=3; CC IsoId=Q15375-3; Sequence=VSP_014380, VSP_014381; CC Name=4; CC IsoId=Q15375-4; Sequence=VSP_041945; CC Name=5; Synonyms=EPHA7-S; CC IsoId=Q15375-5; Sequence=VSP_041943, VSP_041944; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- PTM: Phosphorylated. {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice CC site. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Expressed in lung cancer cells, lacks the CC kinase domain and is most probably secreted. {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 -!- SEQUENCE CAUTION: CC Sequence=BAD92506.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40466/EPHA7"; 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; L36642; AAA74243.1; -; mRNA. DR EMBL; AK313529; BAG36308.1; -; mRNA. DR EMBL; AB209269; BAD92506.1; ALT_INIT; mRNA. DR EMBL; AL121966; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL354857; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL591036; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW48518.1; -; Genomic_DNA. DR EMBL; BC027940; AAH27940.1; -; mRNA. DR EMBL; BC126125; AAI26126.1; -; mRNA. DR EMBL; BC126151; AAI26152.1; -; mRNA. DR EMBL; BC143857; AAI43858.1; -; mRNA. DR EMBL; BC143858; AAI43859.1; -; mRNA. DR CCDS; CCDS5031.1; -. [Q15375-1] DR CCDS; CCDS75494.1; -. [Q15375-3] DR CCDS; CCDS93973.1; -. [Q15375-4] DR PIR; I58351; I58351. DR RefSeq; NP_001275558.1; NM_001288629.1. [Q15375-2] DR RefSeq; NP_001275559.1; NM_001288630.1. [Q15375-3] DR RefSeq; NP_004431.1; NM_004440.3. [Q15375-1] DR RefSeq; XP_005248726.1; XM_005248669.2. DR PDB; 2REI; X-ray; 1.60 A; A=590-899. DR PDB; 3DKO; X-ray; 2.00 A; A=590-899. DR PDB; 3H8M; X-ray; 2.10 A; A/B=919-990. DR PDB; 3NRU; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=32-204. DR PDB; 7EEC; X-ray; 3.10 A; A=599-899. DR PDB; 7EED; X-ray; 3.05 A; A=599-899. DR PDB; 7EEF; X-ray; 2.60 A; A=599-899. DR PDBsum; 2REI; -. DR PDBsum; 3DKO; -. DR PDBsum; 3H8M; -. DR PDBsum; 3NRU; -. DR PDBsum; 7EEC; -. DR PDBsum; 7EED; -. DR PDBsum; 7EEF; -. DR AlphaFoldDB; Q15375; -. DR SMR; Q15375; -. DR BioGRID; 108359; 295. DR IntAct; Q15375; 173. DR MINT; Q15375; -. DR STRING; 9606.ENSP00000358309; -. DR BindingDB; Q15375; -. DR ChEMBL; CHEMBL4602; -. DR DrugBank; DB07970; 5-[(2-methyl-5-{[3-(trifluoromethyl)phenyl]carbamoyl}phenyl)amino]pyridine-3-carboxamide. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q15375; -. DR GuidetoPHARMACOLOGY; 1827; -. DR GlyCosmos; Q15375; 4 sites, 1 glycan. DR GlyGen; Q15375; 5 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q15375; -. DR PhosphoSitePlus; Q15375; -. DR SwissPalm; Q15375; -. DR BioMuta; EPHA7; -. DR DMDM; 146345416; -. DR CPTAC; CPTAC-1783; -. DR CPTAC; CPTAC-2787; -. DR CPTAC; CPTAC-2830; -. DR EPD; Q15375; -. DR jPOST; Q15375; -. DR MassIVE; Q15375; -. DR MaxQB; Q15375; -. DR PaxDb; 9606-ENSP00000358309; -. DR PeptideAtlas; Q15375; -. DR ProteomicsDB; 60549; -. [Q15375-1] DR ProteomicsDB; 60550; -. [Q15375-2] DR ProteomicsDB; 60551; -. [Q15375-3] DR ProteomicsDB; 60552; -. [Q15375-4] DR ProteomicsDB; 60553; -. [Q15375-5] DR Pumba; Q15375; -. DR Antibodypedia; 642; 615 antibodies from 37 providers. DR DNASU; 2045; -. DR Ensembl; ENST00000369297.1; ENSP00000358303.1; ENSG00000135333.15. [Q15375-3] DR Ensembl; ENST00000369303.9; ENSP00000358309.4; ENSG00000135333.15. [Q15375-1] DR Ensembl; ENST00000680224.1; ENSP00000506130.1; ENSG00000135333.15. [Q15375-4] DR GeneID; 2045; -. DR KEGG; hsa:2045; -. DR MANE-Select; ENST00000369303.9; ENSP00000358309.4; NM_004440.4; NP_004431.1. DR UCSC; uc003poe.5; human. [Q15375-1] DR AGR; HGNC:3390; -. DR CTD; 2045; -. DR DisGeNET; 2045; -. DR GeneCards; EPHA7; -. DR HGNC; HGNC:3390; EPHA7. DR HPA; ENSG00000135333; Group enriched (intestine, parathyroid gland). DR MIM; 602190; gene. DR neXtProt; NX_Q15375; -. DR OpenTargets; ENSG00000135333; -. DR PharmGKB; PA27822; -. DR VEuPathDB; HostDB:ENSG00000135333; -. DR eggNOG; KOG0196; Eukaryota. DR GeneTree; ENSGT00940000160189; -. DR HOGENOM; CLU_000288_141_0_1; -. DR InParanoid; Q15375; -. DR OMA; ETDYNTG; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; Q15375; -. DR TreeFam; TF315608; -. DR BRENDA; 2.7.10.1; 2681. DR PathwayCommons; Q15375; -. DR Reactome; R-HSA-2682334; EPH-Ephrin signaling. DR Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse. DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells. DR SignaLink; Q15375; -. DR SIGNOR; Q15375; -. DR BioGRID-ORCS; 2045; 14 hits in 1184 CRISPR screens. DR ChiTaRS; EPHA7; human. DR EvolutionaryTrace; Q15375; -. DR GeneWiki; EPHA7; -. DR GenomeRNAi; 2045; -. DR Pharos; Q15375; Tchem. DR PRO; PR:Q15375; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q15375; Protein. DR Bgee; ENSG00000135333; Expressed in cortical plate and 131 other cell types or tissues. DR GO; GO:0030425; C:dendrite; IBA:GO_Central. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008046; F:axon guidance receptor activity; ISS:UniProtKB. DR GO; GO:0045499; F:chemorepellent activity; ISS:UniProtKB. DR GO; GO:0005004; F:GPI-linked ephrin receptor activity; ISS:UniProtKB. DR GO; GO:0019838; F:growth factor binding; IEA:Ensembl. DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0048755; P:branching morphogenesis of a nerve; ISS:UniProtKB. DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0050919; P:negative chemotaxis; ISS:UniProtKB. DR GO; GO:0048671; P:negative regulation of collateral sprouting; IEA:Ensembl. DR GO; GO:0051964; P:negative regulation of synapse assembly; IEA:Ensembl. DR GO; GO:0072178; P:nephric duct morphogenesis; IEA:Ensembl. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB. DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB. DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:UniProtKB. DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl. DR GO; GO:0031952; P:regulation of protein autophosphorylation; ISS:UniProtKB. DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl. 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 CDD; cd00185; TNFRSF; 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; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like. 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; PF07699; Ephrin_rec_like; 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; Q15375; HS. PE 1: Evidence at protein level; KW 3D-structure; 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_0000016818" 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:0000255" 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 278..279 FT /note="PC -> RK (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014380" FT VAR_SEQ 280..998 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014381" FT VAR_SEQ 442..450 FT /note="APSQVSGVM -> GMFCVYLH (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_041943" FT VAR_SEQ 451..998 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_041944" FT VAR_SEQ 540..544 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_014382" FT VAR_SEQ 600..604 FT /note="FKFPG -> C (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_041945" FT VARIANT 138 FT /note="I -> V (in dbSNP:rs2278107)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17344846" FT /id="VAR_022105" FT VARIANT 170 FT /note="E -> K (in a colorectal adenocarcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042150" FT VARIANT 232 FT /note="G -> R (in a metastatic melanoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042151" FT VARIANT 278 FT /note="P -> S (in dbSNP:rs2278106)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_022106" FT VARIANT 371 FT /note="R -> W (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs371089003)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036090" FT VARIANT 903 FT /note="P -> S (in a metastatic melanoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042152" FT STRAND 33..37 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 54..61 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 67..74 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 96..106 FT /evidence="ECO:0007829|PDB:3NRU" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 121..132 FT /evidence="ECO:0007829|PDB:3NRU" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 144..150 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 168..174 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 178..190 FT /evidence="ECO:0007829|PDB:3NRU" FT STRAND 192..202 FT /evidence="ECO:0007829|PDB:3NRU" FT HELIX 611..613 FT /evidence="ECO:0007829|PDB:2REI" FT STRAND 614..616 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 617..624 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 630..632 FT /evidence="ECO:0007829|PDB:2REI" FT STRAND 633..641 FT /evidence="ECO:0007829|PDB:2REI" FT STRAND 643..652 FT /evidence="ECO:0007829|PDB:2REI" FT STRAND 655..657 FT /evidence="ECO:0007829|PDB:3DKO" FT STRAND 660..666 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 673..686 FT /evidence="ECO:0007829|PDB:2REI" FT STRAND 697..701 FT /evidence="ECO:0007829|PDB:2REI" FT STRAND 703..705 FT /evidence="ECO:0007829|PDB:2REI" FT STRAND 708..712 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 719..725 FT /evidence="ECO:0007829|PDB:2REI" FT TURN 726..728 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 732..751 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 761..763 FT /evidence="ECO:0007829|PDB:2REI" FT STRAND 764..766 FT /evidence="ECO:0007829|PDB:2REI" FT STRAND 772..774 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 800..802 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 805..810 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 815..830 FT /evidence="ECO:0007829|PDB:2REI" FT TURN 836..839 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 842..850 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 863..872 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 877..879 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 883..895 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 897..899 FT /evidence="ECO:0007829|PDB:2REI" FT HELIX 928..934 FT /evidence="ECO:0007829|PDB:3H8M" FT HELIX 938..940 FT /evidence="ECO:0007829|PDB:3H8M" FT HELIX 941..946 FT /evidence="ECO:0007829|PDB:3H8M" FT HELIX 952..956 FT /evidence="ECO:0007829|PDB:3H8M" FT HELIX 960..965 FT /evidence="ECO:0007829|PDB:3H8M" FT HELIX 971..988 FT /evidence="ECO:0007829|PDB:3H8M" FT CONFLICT Q15375-3:278 FT /note="R -> C (in Ref. 6; AAH27940)" FT /evidence="ECO:0000305" SQ SEQUENCE 998 AA; 112097 MW; 479B9CA0D2BB06EB CRC64; MVFQTRYPSW IILCYIWLLR FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPNGWEEISG LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK GFYLAFQDVG ACIALVSVKV YYKKCWSIIE NLAIFPDTVT GSEFSSLVEV RGTCVSSAEE EAENAPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RGFYKSSSQD LQCSRCPTHS FSDKEGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVE LSWQEPEHPN GVITEYEIKY YEKDQRERTY STVKTKSTSA SINNLKPGTV YVFQIRAFTA AGYGNYSPRL DVATLEEATG 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 DCWQKERAER PKFEQIVGIL DKMIRNPNSL KTPLGTCSRP ISPLLDQNTP DFTTFCSVGE WLQAIKMERY KDNFTAAGYN SLESVARMTI EDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV //