EPHA5_CHICK
ID EPHA5_CHICK Reviewed; 1013 AA.
AC P54755; Q07495;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ephrin type-A receptor 5;
DE EC=2.7.10.1;
DE AltName: Full=EPH-like kinase 7;
DE Short=EK7;
DE Short=cEK7;
DE Flags: Precursor;
GN Name=EPHA5; Synonyms=CEK7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Body wall;
RX PubMed=7958948; DOI=10.1016/0378-1119(94)90692-0;
RA Siever D.A., Verderame M.F.;
RT "Identification of a complete Cek7 receptor protein tyrosine kinase coding
RT sequence and cDNAs of alternatively spliced transcripts.";
RL Gene 148:219-226(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 512-1013.
RC TISSUE=Brain;
RX PubMed=8510926;
RA Sajjadi F.G., Pasquale E.B.;
RT "Five novel avian Eph-related tyrosine kinases are differentially
RT expressed.";
RL Oncogene 8:1807-1813(1993).
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 (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 {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54757};
CC Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC axon {ECO:0000250|UniProtKB:P54757}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P54756}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=3;
CC IsoId=P54755-1; Sequence=Displayed;
CC Name=1;
CC IsoId=P54755-2; Sequence=VSP_003005;
CC Name=2;
CC IsoId=P54755-3; Sequence=VSP_003004, VSP_003005;
CC -!- TISSUE SPECIFICITY: Detected in the 10-day embryonic brain, weaker
CC expression in the rest of the 10-day embryo. Undetected in adult
CC tissues.
CC -!- PTM: Phosphorylated. Phosphorylation is stimulated by the ligand EFNA5
CC (By similarity). {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; U03910; AAB60613.1; -; mRNA.
DR EMBL; U03910; AAB60614.1; -; mRNA.
DR EMBL; U03910; AAB60612.1; -; mRNA.
DR EMBL; Z19058; CAA79508.1; -; mRNA.
DR PIR; I50615; I50615.
DR AlphaFoldDB; P54755; -.
DR SMR; P54755; -.
DR STRING; 9031.ENSGALP00000037020; -.
DR PaxDb; P54755; -.
DR VEuPathDB; HostDB:geneid_395997; -.
DR eggNOG; KOG0196; Eukaryota.
DR InParanoid; P54755; -.
DR OrthoDB; 933071at2759; -.
DR PhylomeDB; P54755; -.
DR BRENDA; 2.7.10.1; 1306.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005004; F:GPI-linked ephrin receptor 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; 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:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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; 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; 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; 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell membrane; Cell projection;
KW Glycoprotein; Kinase; Membrane; Neurogenesis; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1013
FT /note="Ephrin type-A receptor 5"
FT /id="PRO_0000016815"
FT TOPO_DOM 32..549
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..1013
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..214
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 333..443
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 444..538
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 651..912
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 941..1013
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 1011..1013
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 776
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 657..665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 626
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 632
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 809
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 958
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 280..443
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003004"
FT VAR_SEQ 573..595
FT /note="SCCDHGCGWASSLRAVAYPSLIW -> R (in isoform 1 and
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003005"
FT CONFLICT 981..1013
FT /note="LRRLGVTLVGHQKKIMNSLQEMKVQLVNGMVPL -> ESPCEKWSLTLHPLF
FT PTGYQT (in Ref. 2; CAA79508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1013 AA; 112246 MW; AC36FD6AEBF38382 CRC64;
MGLRGGGGRA GGPAPGWTCL LLCAALRSLL ASPGSEVNLL DSRTVMGDLG WIAYPKNGWE
EIGEVDENYA PIHTYQVCKV MEQNQNNWLL TSWISNEGRP ASSFELKFTL RDCNSLPGGL
GTCKETFNMY YFESDDEDGR NIRENQYIKI DTIAADESFT ELDLGDRVMK LNTEVRDVGP
LTKKGFYLAF QDVGACIALV SVRVYYKKCP SVIRNLARFP DTITGADSSQ LLEVSGVCVN
HSVTDEAPKM HCSAEGEWLV PIGKCLCKAG YEEKNNTCQV CRPGFFKASP HSPSCSKCPP
HSYTLDEAST SCLCEEHYFR RESDPPTMAC TRPPSAPRSA ISNVNETSVF LEWIPPADTG
GRKDVSYYIA CKKCNSHSGL CEACGSHVRY LPQQTGLKNT SVMMVDLLAH TNYTFEIEAV
NGVSDQNPGA RQFVSVNVTT NQAAPSPVSS VKKGKITKNS ISLSWQEPDR PNGIILEYEI
KYFEKDQETS YTIIKSKETA ITADGLKPGS AYVFQIRART AAGYGGFSRR FEFETSPVLA
ASSDQSQIPI IVVSVTVGVI LLAVVIGFLL SGSCCDHGCG WASSLRAVAY PSLIWRCGYS
KAKQDPEEEK MHFHNGHIKL PGVRTYIDPH TYEDPNQAVH EFAKEIEASC ITIERVIGAG
EFGEVCSGRL KLQGKREFPV AIKTLKVGYT EKQRRDFLGE ASIMGQFDHP NIIHLEGVVT
KSKPVMIVTE YMENGSLDTF LKKNDGQFTV IQLVGMLRGI ASGMKYLSDM GYVHRDLAAR
NILINSNLVC KVSDFGLSRV LEDDPEAAYT TRGGKIPIRW TAPEAIAFRK FTSASDVWSY
GIVMWEVMSY GERPYWEMTN QDVIKAVEEG YRLPSPMDCP AALYQLMLDC WQKDRNSRPK
FDEIVSMLDK LIRNPSSLKT LVNASSRVSN LLVEHSPVGS GAYRSVGEWL EAIKMGRYTE
IFMENGYSSM DSVAQVTLED LRRLGVTLVG HQKKIMNSLQ EMKVQLVNGM VPL
