ID E9PG71_HUMAN Unreviewed; 949 AA. AC E9PG71; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-JAN-2019, entry version 74. DE SubName: Full=Ephrin type-A receptor 4 {ECO:0000313|Ensembl:ENSP00000386276}; GN Name=EPHA4 {ECO:0000313|Ensembl:ENSP00000386276}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000386276, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000386276, ECO:0000313|Proteomes:UP000005640} 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [2] {ECO:0000213|PubMed:19369195} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [3] {ECO:0000313|Ensembl:ENSP00000386276} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L- CC tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, CC Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; CC EC=2.7.10.1; Evidence={ECO:0000256|SAAS:SAAS01124082}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. {ECO:0000256|SAAS:SAAS00941529}. 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; AC010899; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC079834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005246431.1; XM_005246374.2. DR UniGene; Hs.371218; -. DR ProteinModelPortal; E9PG71; -. DR jPOST; E9PG71; -. DR MaxQB; E9PG71; -. DR PeptideAtlas; E9PG71; -. DR PRIDE; E9PG71; -. DR Ensembl; ENST00000409854; ENSP00000386276; ENSG00000116106. DR GeneID; 2043; -. DR UCSC; uc002vmr.3; human. DR CTD; 2043; -. DR EuPathDB; HostDB:ENSG00000116106.11; -. DR HGNC; HGNC:3388; EPHA4. DR OpenTargets; ENSG00000116106; -. DR eggNOG; KOG0196; Eukaryota. DR eggNOG; COG0515; LUCA. DR GeneTree; ENSGT00940000156948; -. DR OrthoDB; 933071at2759; -. DR ChiTaRS; EPHA4; human. DR GenomeRNAi; 2043; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000116106; Expressed in 211 organ(s), highest expression level in forebrain. DR ExpressionAtlas; E9PG71; baseline and differential. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro. DR CDD; cd10482; EphR_LBD_A4; 1. DR CDD; cd00063; FN3; 2. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 2.60.40.10; -; 2. DR InterPro; IPR027936; Eph_TM. DR InterPro; IPR034270; EphA4_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; 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; PF00041; fn3; 2. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF07647; SAM_2; 1. DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00615; EPH_lbd; 1. DR SMART; SM01411; Ephrin_rec_like; 1. DR SMART; SM00060; FN3; 2. DR SMART; SM00220; S_TKc; 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 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 ATP-binding {ECO:0000256|PIRSR:PIRSR000666-2, KW ECO:0000256|SAAS:SAAS00708816}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Kinase {ECO:0000256|SAAS:SAAS00582553}; KW Membrane {ECO:0000256|SAAS:SAAS00602683, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000666-2, KW ECO:0000256|SAAS:SAAS00708816}; KW Proteomics identification {ECO:0000213|MaxQB:E9PG71, KW ECO:0000213|PeptideAtlas:E9PG71}; KW Receptor {ECO:0000256|SAAS:SAAS00600436}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Repeat {ECO:0000256|SAAS:SAAS01054641}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|SAAS:SAAS00582553}; KW Transmembrane {ECO:0000256|SAAS:SAAS00602683, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00602683, KW ECO:0000256|SAM:Phobius}; KW Tyrosine-protein kinase {ECO:0000256|SAAS:SAAS00582553}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 949 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003245020. FT TRANSMEM 548 570 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 30 209 Eph LBD. {ECO:0000259|PROSITE:PS51550}. FT DOMAIN 328 439 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 440 537 Fibronectin type-III. FT {ECO:0000259|PROSITE:PS50853}. FT DOMAIN 621 882 Protein kinase. FT {ECO:0000259|PROSITE:PS50011}. FT DOMAIN 911 949 SAM. {ECO:0000259|PROSITE:PS50105}. FT NP_BIND 627 635 ATP. {ECO:0000256|PIRSR:PIRSR000666-2}. FT ACT_SITE 746 746 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000666-1}. FT BINDING 653 653 ATP. {ECO:0000256|PIRSR:PIRSR000666-2}. SQ SEQUENCE 949 AA; 105716 MW; CED817F8F5ABF861 CRC64; MAGIFYFALF SCLFGICDAV TGSRVYPANE VTLLDSRSVQ GELGWIASPL EGGWEEVSIM DEKNTPIRTY QVCNVMEPSQ NNWLRTDWIT REGAQRVYIE IKFTLRDCNS LPGVMGTCKE TFNLYYYESD NDKERFIREN QFVKIDTIAA DESFTQVDIG DRIMKLNTEI RDVGPLSKKG FYLAFQDVGA CIALVSVRVF YKKCPLTVRN LAQFPDTITG ADTSSLVEVR GSCVNNSEEK DVPKMYCGAD GEWLVPIGNC LCNAGHEERS GECQACKIGY YKALSTDATC AKCPPHSYSV WEGATSCTCD RGFFRADNDA ASMPCTRPPS APLNLISNVN ETSVNLEWSS PQNTGGRQDI SYNVVCKKCG AGDPSKCRPC GSGVHYTPQQ NGLKTTKVSI TDLLAHTNYT FEIWAVNGVS KYNPNPDQSV SVTVTTNQAA PSSIALVQAK EVTRYSVALA WLEPDRPNGV ILEYEVKYYE KDQNERSYRI VRTAARNTDI KGLNPLTSYV FHVRARTAAG YGDFSEPLEV TTNTVPSRII GDGANSTVLL VSVSGSVVLV VILIAAFVIS RRRSKYSKAK QEADEEKHLN QGVRTYVDPF TYEDPNQAVR EFAKEIDASC IKIEKVIGVG EFGEVCSGRL KVPGKREICV AIKTLKAGYT DKQRRDFLSE ASIMGQFDHP NIIHLEGVVT KCKPVMIITE YMENGSLDAF LRKNDGRFTV IQLVGMLRGI GSGMKYLSDM SYVHRDLAAR NILVNSNLVC KVSDFGMSRV LEDDPEAAYT TRGGKIPIRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSY GERPYWDMSN QDVIKAIEEG YRLPPPMDCP IALHQLMLDC WQKERSDRPK FGQIVNMLDK LIRNPNSLKR TGTESSRPNT ALLDPSSPEF SAVVSVGDWL QAIKMDRYKD NFTAAGYTTL EAVVHVNQE //