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Ephrin type-A receptor 4 (EC 2.7.10.1) (EPH-like kinase 8) (EK8) (cEK8)

 EPHA4_CHICK             Reviewed;         986 AA.
Q07496; Q90772;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
05-DEC-2018, entry version 168.
RecName: Full=Ephrin type-A receptor 4;
EC=2.7.10.1;
AltName: Full=EPH-like kinase 8;
Short=EK8;
Short=cEK8;
Flags: Precursor;
Name=EPHA4; Synonyms=CEK8;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spinal cord;
PubMed=8808406; DOI=10.1016/0925-4773(95)00461-0;
Ohta K., Nakamura M., Hirokawa K., Tanaka S., Iwama A., Suda T.,
Ando M., Tanaka H.;
"The receptor tyrosine kinase, Cek8, is transiently expressed on
subtypes of motoneurons in the spinal cord during development.";
Mech. Dev. 54:59-69(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 138-986.
TISSUE=Embryo;
PubMed=8510926;
Sajjadi F.G., Pasquale E.B.;
"Five novel avian Eph-related tyrosine kinases are differentially
expressed.";
Oncogene 8:1807-1813(1993).
[3]
INTERACTION WITH SIPA1L1.
PubMed=18094260; DOI=10.1523/JNEUROSCI.2746-07.2007;
Richter M., Murai K.K., Bourgin C., Pak D.T., Pasquale E.B.;
"The EphA4 receptor regulates neuronal morphology through SPAR-
mediated inactivation of Rap GTPases.";
J. Neurosci. 27:14205-14215(2007).
-!- FUNCTION: Receptor tyrosine kinase which binds membrane-bound
ephrin family ligands residing on adjacent cells, leading to
contact-dependent bidirectional signaling into neighboring cells.
The signaling pathway downstream of the receptor is referred to as
forward signaling while the signaling pathway downstream of the
ephrin ligand is referred to as reverse signaling. Highly
promiscuous, it has the unique property among Eph receptors to
bind and to be physiologically activated by both GPI-anchored
ephrin-A and transmembrane ephrin-B ligands including EFNA1 and
EFNB3. Upon activation by ephrin ligands, modulates cell
morphology and integrin-dependent cell adhesion through regulation
of the Rac, Rap and Rho GTPases activity. Plays an important role
in the development of the nervous system controlling different
steps of axonal guidance including the establishment of the
corticospinal projections (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
-!- SUBUNIT: Interacts with the src family kinase, p59-Fyn, through
the major phosphorylation site at position Tyr-602 (By
similarity). Interacts (via PDZ motif) with SIPA1L1 (via PDZ
domain); controls neuronal morphology through regulation of the
RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases.
{ECO:0000250, ECO:0000269|PubMed:18094260}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Early endosome
{ECO:0000250}. Note=Clustered upon activation and targeted to
early endosome. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed at high levels in brain, with
expression also detected in the kidney, lung, muscle and thymus.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; D38174; BAA07373.1; -; mRNA.
EMBL; Z19059; CAA79509.1; -; mRNA.
PIR; I50617; I50617.
RefSeq; NP_990112.1; NM_204781.1.
UniGene; Gga.304; -.
ProteinModelPortal; Q07496; -.
SMR; Q07496; -.
STRING; 9031.ENSGALP00000008426; -.
PaxDb; Q07496; -.
PRIDE; Q07496; -.
GeneID; 395559; -.
KEGG; gga:395559; -.
CTD; 2043; -.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; Q07496; -.
KO; K05105; -.
OMA; QIHGRMV; -.
OrthoDB; EOG091G00W0; -.
PhylomeDB; Q07496; -.
TreeFam; TF315608; -.
BRENDA; 2.7.10.1; 1306.
PRO; PR:Q07496; -.
Proteomes; UP000000539; Unplaced.
Bgee; ENSGALG00000005256; Expressed in 11 organ(s), highest expression level in testis.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0097161; F:DH domain binding; ISS:UniProtKB.
GO; GO:0005004; F:GPI-linked ephrin receptor activity; ISS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0097155; P:fasciculation of sensory neuron axon; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
GO; GO:0009968; P:negative regulation of signal transduction; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:2001108; P:positive regulation of Rho guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0035282; P:segmentation; NAS:AgBase.
GO; GO:0001756; P:somitogenesis; NAS:AgBase.
CDD; cd10482; EphR_LBD_A4; 1.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034270; EphA4_rcpt_lig-bd.
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
Pfam; PF14575; EphA2_TM; 1.
Pfam; PF01404; Ephrin_lbd; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF07647; SAM_2; 1.
PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00615; EPH_lbd; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00060; FN3; 2.
SMART; SM00220; S_TKc; 1.
SMART; SM00454; SAM; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS51550; EPH_LBD; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
ATP-binding; Cell adhesion; Cell membrane; Complete proteome;
Developmental protein; Endosome; Glycoprotein; Kinase; Membrane;
Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 986 Ephrin type-A receptor 4.
/FTId=PRO_0000016809.
TOPO_DOM 20 547 Extracellular. {ECO:0000255}.
TRANSMEM 548 569 Helical. {ECO:0000255}.
TOPO_DOM 570 986 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 209 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 328 439 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 440 537 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 621 882 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 911 975 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 627 635 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 984 986 PDZ-binding. {ECO:0000255}.
COMPBIAS 191 325 Cys-rich.
ACT_SITE 746 746 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 653 653 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 596 596 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 602 602 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 779 779 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 928 928 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 138 138 R -> G (in Ref. 2; CAA79509).
{ECO:0000305}.
CONFLICT 487 487 S -> T (in Ref. 2; CAA79509).
{ECO:0000305}.
SEQUENCE 986 AA; 109483 MW; BD88C2A5BD840A0F CRC64;
MAGVPVGALL PLLVGVCGAV TGSRVYPANE VTLLDSRSVQ GELGWIASPL EGGWEEVSIM
DEKNTPIRTY QVCNVMEPSQ NNWLRTDWIP REGAQRVYIE IKFTLRDCNS LPGVMGTCKE
TFNLYYYESN NDKERFIRES QFAKIDTIAA DESFTQVDIG DRIMKLNTEV RDVGPLSKKG
FYLAFQDVGA CIALVSVRVF YKKCPLTVRN LAQFPDTITG ADTSSLVEVR GSCVNNSEEK
DVPKMYCGAD GEWLVPIGNC LCNAGYEERN GECQACKIGY YKALSTDVAC AKCPPHSYSI
WEGSTSCTCD RGFFRAENDA ASMPCTRPPS APQNLISNVN ETSVNLEWSA PQNKGGRDDI
SYNVVCKRCG AGEPSHCRSC GSGVHFSPQQ NGLKTTKVSI TDLLAHTNYT FEVWAVNGVS
KHNPSQDQAV SVTVTTNQAA PSPIALIQAK EITRHSVALA WLEPDRPNGV ILEYEVKYYE
KDQNERSYRI VKTASRNTDI KGLNPLTSYV FHVRARTAAG YGDFSGPFEF TTNTVPSPII
GDGTNPTVLL VSVAGSVVLV 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 TGSESSRPST
ALLDPSSPEF SAVVSVSDWL QAIKMERYKD NFTAAGYTTL EAVVHMNQDD LARIGITAIT
HQNKILSSVQ AMRSQMQQMH GRMVPV


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