EPHA7_HUMAN
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 03-AUG-2022, entry version 220.
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; P29317: EPHA2; NbExp=3; IntAct=EBI-1383428, EBI-702104;
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="http://atlasgeneticsoncology.org/Genes/EPHA7ID40466ch6q16.html";
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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 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; 159.
DR IntAct; Q15375; 43.
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 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 EPD; Q15375; -.
DR jPOST; Q15375; -.
DR MassIVE; Q15375; -.
DR MaxQB; Q15375; -.
DR PaxDb; Q15375; -.
DR PeptideAtlas; Q15375; -.
DR PRIDE; 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 Antibodypedia; 642; 556 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 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; 1585262at2759; -.
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 1106 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 129 other tissues.
DR Genevisible; Q15375; HS.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
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:0046875; F:ephrin receptor binding; IEA:Ensembl.
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: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; 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: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:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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 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; 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 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; 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 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
