ID   EPHA5_HUMAN             Reviewed;        1037 AA.
AC   P54756; Q7Z3F2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 3.
DT   24-JAN-2024, entry version 220.
DE   RecName: Full=Ephrin type-A receptor 5;
DE            EC=2.7.10.1;
DE   AltName: Full=Brain-specific kinase;
DE   AltName: Full=EPH homology kinase 1;
DE            Short=EHK-1;
DE   AltName: Full=EPH-like kinase 7;
DE            Short=EK7;
DE            Short=hEK7;
DE   Flags: Precursor;
GN   Name=EPHA5; Synonyms=BSK, EHK1, HEK7, TYRO4;
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), SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9191074; DOI=10.1016/s0169-328x(96)00268-9;
RA   Miescher G.C., Taylor V., Olivieri G., Mindermann T., Shrock E.,
RA   Steck A.J.;
RT   "Extensive splice variation and localization of the EHK-1 receptor tyrosine
RT   kinase in adult human brain and glial tumors.";
RL   Brain Res. Mol. Brain Res. 46:17-24(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Retina;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-1037.
RC   TISSUE=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   [5]
RP   IDENTIFICATION OF EFNA5 AS LIGAND, AND PHOSPHORYLATION.
RX   PubMed=7748564; DOI=10.1016/0896-6273(95)90335-6;
RA   Winslow J.W., Moran P., Valverde J., Shih A., Yuan J.Q., Wong S.C.,
RA   Tsai S.P., Goddard A., Henzel W.J., Hefti F., Beck K.D., Caras I.W.;
RT   "Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor
RT   involved in axon bundle formation.";
RL   Neuron 14:973-981(1995).
RN   [6]
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   [7]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=10375373; DOI=10.1177/002215549904700702;
RA   Olivieri G., Miescher G.C.;
RT   "Immunohistochemical localization of EphA5 in the adult human central
RT   nervous system.";
RL   J. Histochem. Cytochem. 47:855-861(1999).
RN   [8]
RP   VARIANTS [LARGE SCALE ANALYSIS] THR-81; ALA-235; GLN-330; GLN-417; LYS-503;
RP   CYS-506; GLU-582; THR-672; THR-673; ILE-856; ARG-959 AND SER-1032.
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 most probably constitutes the cognate/functional ligand
CC       for EPHA5. Functions as an axon guidance molecule during development
CC       and may be involved in the development of the retinotectal, entorhino-
CC       hippocampal and hippocamposeptal pathways. Together with EFNA5 plays
CC       also a role in synaptic plasticity in adult brain through regulation of
CC       synaptogenesis. In addition to its function in the nervous system, the
CC       interaction of EPHA5 with EFNA5 mediates communication between
CC       pancreatic islet cells to regulate glucose-stimulated insulin secretion
CC       (By similarity). {ECO:0000250}.
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 SAM domain) with SAMD5 (via SAM domain) (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:Q60629}.
CC   -!- INTERACTION:
CC       P54756; P29317: EPHA2; NbExp=3; IntAct=EBI-1383718, EBI-702104;
CC       P54756; P54760: EPHB4; NbExp=2; IntAct=EBI-1383718, EBI-702121;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10375373};
CC       Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC       axon {ECO:0000250|UniProtKB:P54757}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:10375373, ECO:0000269|PubMed:9191074}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=P54756-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P54756-2; Sequence=VSP_002999;
CC       Name=3;
CC         IsoId=P54756-3; Sequence=VSP_039118, VSP_039119;
CC   -!- TISSUE SPECIFICITY: Almost exclusively expressed in the nervous system
CC       in cortical neurons, cerebellar Purkinje cells and pyramidal neurons
CC       within the cortex and hippocampus. Display an increasing gradient of
CC       expression from the forebrain to hindbrain and spinal cord.
CC       {ECO:0000269|PubMed:10375373, ECO:0000269|PubMed:9191074}.
CC   -!- PTM: Phosphorylated. Phosphorylation is stimulated by the ligand EFNA5.
CC       Dephosphorylation upon stimulation by glucose, inhibits EPHA5 forward
CC       signaling and results in insulin secretion (By similarity).
CC       {ECO:0000250}.
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; X95425; CAA64700.1; -; mRNA.
DR   EMBL; AC018683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC105923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC115223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX537946; CAD97914.1; -; mRNA.
DR   EMBL; L36644; AAA74245.1; -; mRNA.
DR   CCDS; CCDS3513.1; -. [P54756-1]
DR   CCDS; CCDS3514.1; -. [P54756-2]
DR   RefSeq; NP_001268694.1; NM_001281765.2.
DR   RefSeq; NP_001268695.1; NM_001281766.2.
DR   RefSeq; NP_001305690.1; NM_001318761.1. [P54756-3]
DR   RefSeq; NP_004430.4; NM_004439.7. [P54756-1]
DR   RefSeq; NP_872272.2; NM_182472.4. [P54756-2]
DR   PDB; 2R2P; X-ray; 2.40 A; A=653-939.
DR   PDB; 4ET7; X-ray; 2.60 A; A=59-235.
DR   PDBsum; 2R2P; -.
DR   PDBsum; 4ET7; -.
DR   AlphaFoldDB; P54756; -.
DR   SMR; P54756; -.
DR   BioGRID; 108358; 138.
DR   IntAct; P54756; 122.
DR   MINT; P54756; -.
DR   STRING; 9606.ENSP00000480763; -.
DR   BindingDB; P54756; -.
DR   ChEMBL; CHEMBL3987; -.
DR   DrugBank; DB01254; Dasatinib.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; P54756; -.
DR   GuidetoPHARMACOLOGY; 1825; -.
DR   GlyCosmos; P54756; 6 sites, No reported glycans.
DR   GlyGen; P54756; 7 sites.
DR   iPTMnet; P54756; -.
DR   PhosphoSitePlus; P54756; -.
DR   SwissPalm; P54756; -.
DR   BioMuta; EPHA5; -.
DR   DMDM; 259016353; -.
DR   EPD; P54756; -.
DR   jPOST; P54756; -.
DR   MassIVE; P54756; -.
DR   MaxQB; P54756; -.
DR   PaxDb; 9606-ENSP00000480763; -.
DR   PeptideAtlas; P54756; -.
DR   ProteomicsDB; 56712; -. [P54756-1]
DR   ProteomicsDB; 56713; -. [P54756-2]
DR   ProteomicsDB; 56714; -. [P54756-3]
DR   TopDownProteomics; P54756-2; -. [P54756-2]
DR   ABCD; P54756; 4 sequenced antibodies.
DR   Antibodypedia; 12603; 593 antibodies from 35 providers.
DR   DNASU; 2044; -.
DR   Ensembl; ENST00000273854.7; ENSP00000273854.3; ENSG00000145242.14. [P54756-1]
DR   Ensembl; ENST00000354839.8; ENSP00000346899.4; ENSG00000145242.14. [P54756-2]
DR   GeneID; 2044; -.
DR   KEGG; hsa:2044; -.
DR   UCSC; uc003hcy.5; human. [P54756-1]
DR   AGR; HGNC:3389; -.
DR   CTD; 2044; -.
DR   DisGeNET; 2044; -.
DR   GeneCards; EPHA5; -.
DR   HGNC; HGNC:3389; EPHA5.
DR   HPA; ENSG00000145242; Tissue enriched (brain).
DR   MIM; 600004; gene.
DR   neXtProt; NX_P54756; -.
DR   OpenTargets; ENSG00000145242; -.
DR   PharmGKB; PA27821; -.
DR   VEuPathDB; HostDB:ENSG00000145242; -.
DR   eggNOG; KOG0196; Eukaryota.
DR   GeneTree; ENSGT00940000156266; -.
DR   HOGENOM; CLU_000288_141_4_1; -.
DR   InParanoid; P54756; -.
DR   OMA; VAWTWTW; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; P54756; -.
DR   TreeFam; TF315608; -.
DR   BRENDA; 2.7.10.1; 2681.
DR   PathwayCommons; P54756; -.
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; P54756; -.
DR   SIGNOR; P54756; -.
DR   BioGRID-ORCS; 2044; 11 hits in 1193 CRISPR screens.
DR   ChiTaRS; EPHA5; human.
DR   EvolutionaryTrace; P54756; -.
DR   GeneWiki; EPH_receptor_A5; -.
DR   GenomeRNAi; 2044; -.
DR   Pharos; P54756; Tchem.
DR   PRO; PR:P54756; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P54756; Protein.
DR   Bgee; ENSG00000145242; Expressed in cortical plate and 100 other cell types or tissues.
DR   ExpressionAtlas; P54756; baseline and differential.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005003; F:ephrin receptor activity; ISS:UniProtKB.
DR   GO; GO:0005004; F:GPI-linked ephrin receptor activity; ISS:UniProtKB.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0021766; P:hippocampus development; ISS:UniProtKB.
DR   GO; GO:0048666; P:neuron development; IEP:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR   CDD; cd10483; EphR_LBD_A5; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05066; PTKc_EphR_A; 1.
DR   CDD; cd09546; SAM_EPH-A5; 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; IPR034277; EphA5_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; 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:SF13; EPHRIN TYPE-A RECEPTOR 5; 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; 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; P54756; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW   Cell projection; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1037
FT                   /note="Ephrin type-A receptor 5"
FT                   /id="PRO_0000016812"
FT   TOPO_DOM        25..573
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        574..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        595..1037
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          60..238
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT   DOMAIN          357..467
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          468..562
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          675..936
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          965..1029
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1035..1037
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        800
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         681..689
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         707
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         650
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         656
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         833
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         982
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..69
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_039118"
FT   VAR_SEQ         563
FT                   /note="F -> SV (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_039119"
FT   VAR_SEQ         597..619
FT                   /note="SCCECGCGRASSLCAVAHPSLIW -> R (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002999"
FT   VARIANT         81
FT                   /note="N -> T (in dbSNP:rs33932471)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042138"
FT   VARIANT         235
FT                   /note="S -> A (in dbSNP:rs55710198)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042139"
FT   VARIANT         330
FT                   /note="E -> Q (in dbSNP:rs56205382)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042140"
FT   VARIANT         417
FT                   /note="R -> Q (in a lung adenocarcinoma sample; somatic
FT                   mutation; dbSNP:rs199614818)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042141"
FT   VARIANT         503
FT                   /note="E -> K (in a lung large cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042142"
FT   VARIANT         506
FT                   /note="Y -> C (in dbSNP:rs56074660)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_045912"
FT   VARIANT         582
FT                   /note="G -> E (in a lung adenocarcinoma sample; somatic
FT                   mutation; dbSNP:rs1057520012)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042143"
FT   VARIANT         672
FT                   /note="A -> T (in dbSNP:rs36050417)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042144"
FT   VARIANT         673
FT                   /note="S -> T (in dbSNP:rs56359290)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042145"
FT   VARIANT         856
FT                   /note="T -> I (in a lung squamous cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042146"
FT   VARIANT         959
FT                   /note="H -> R (in dbSNP:rs56312931)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042147"
FT   VARIANT         1032
FT                   /note="N -> S (in a lung large cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042148"
FT   CONFLICT        11
FT                   /note="R -> H (in Ref. 1; CAA64700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="G -> D (in Ref. 3; CAD97914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        506
FT                   /note="Y -> H (in Ref. 1; CAA64700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        611
FT                   /note="A -> V (in Ref. 3; CAD97914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        616
FT                   /note="S -> I (in Ref. 1; CAA64700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        820
FT                   /note="G -> E (in Ref. 3; CAD97914)"
FT                   /evidence="ECO:0000305"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          76..89
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          126..135
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          148..157
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          172..178
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          196..202
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          207..219
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   STRAND          221..230
FT                   /evidence="ECO:0007829|PDB:4ET7"
FT   HELIX           663..665
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           672..674
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   STRAND          675..683
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   STRAND          685..694
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   STRAND          702..708
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           715..728
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   STRAND          739..743
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   STRAND          745..748
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   STRAND          750..754
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           761..766
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   TURN            767..770
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           774..793
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           803..805
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   STRAND          806..808
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   STRAND          814..816
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           842..844
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           847..852
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           857..873
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   TURN            878..881
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           884..893
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           905..914
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           919..921
FT                   /evidence="ECO:0007829|PDB:2R2P"
FT   HELIX           925..936
FT                   /evidence="ECO:0007829|PDB:2R2P"
SQ   SEQUENCE   1037 AA;  114803 MW;  578C2F4D950DE419 CRC64;
     MRGSGPRGAG RRRPPSGGGD TPITPASLAG CYSAPRRAPL WTCLLLCAAL RTLLASPSNE
     VNLLDSRTVM GDLGWIAFPK NGWEEIGEVD ENYAPIHTYQ VCKVMEQNQN NWLLTSWISN
     EGASRIFIEL KFTLRDCNSL PGGLGTCKET FNMYYFESDD QNGRNIKENQ YIKIDTIAAD
     ESFTELDLGD RVMKLNTEVR DVGPLSKKGF YLAFQDVGAC IALVSVRVYY KKCPSVVRHL
     AVFPDTITGA DSSQLLEVSG SCVNHSVTDE PPKMHCSAEG EWLVPIGKCM CKAGYEEKNG
     TCQVCRPGFF KASPHIQSCG KCPPHSYTHE EASTSCVCEK DYFRRESDPP TMACTRPPSA
     PRNAISNVNE TSVFLEWIPP ADTGGRKDVS YYIACKKCNS HAGVCEECGG HVRYLPRQSG
     LKNTSVMMVD LLAHTNYTFE IEAVNGVSDL SPGARQYVSV NVTTNQAAPS PVTNVKKGKI
     AKNSISLSWQ EPDRPNGIIL EYEIKYFEKD QETSYTIIKS KETTITAEGL KPASVYVFQI
     RARTAAGYGV FSRRFEFETT PVFAASSDQS QIPVIAVSVT VGVILLAVVI GVLLSGSCCE
     CGCGRASSLC AVAHPSLIWR CGYSKAKQDP EEEKMHFHNG HIKLPGVRTY IDPHTYEDPN
     QAVHEFAKEI EASCITIERV IGAGEFGEVC SGRLKLPGKR ELPVAIKTLK VGYTEKQRRD
     FLGEASIMGQ FDHPNIIHLE GVVTKSKPVM IVTEYMENGS LDTFLKKNDG QFTVIQLVGM
     LRGISAGMKY LSDMGYVHRD LAARNILINS NLVCKVSDFG LSRVLEDDPE AAYTTRGGKI
     PIRWTAPEAI AFRKFTSASD VWSYGIVMWE VVSYGERPYW EMTNQDVIKA VEEGYRLPSP
     MDCPAALYQL MLDCWQKERN SRPKFDEIVN MLDKLIRNPS SLKTLVNASC RVSNLLAEHS
     PLGSGAYRSV GEWLEAIKMG RYTEIFMENG YSSMDAVAQV TLEDLRRLGV TLVGHQKKIM
     NSLQEMKVQL VNGMVPL
//