ID Q6NTV5_XENLA Unreviewed; 978 AA.
AC Q6NTV5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 2.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=epha2.S {ECO:0000313|Xenbase:XB-GENE-17336518};
GN Synonyms=G50 {ECO:0000313|RefSeq:NP_001129645.1}, LOC100191024
GN {ECO:0000313|RefSeq:NP_001129645.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH68849.2};
RN [1] {ECO:0000313|RefSeq:NP_001129645.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=7655077;
RA Brandli A.W., Kirschner M.W.;
RT "Molecular cloning of tyrosine kinases in the early Xenopus embryo:
RT identification of Eck-related genes expressed in cranial neural crest cells
RT of the second (hyoid) arch.";
RL Dev. Dyn. 203:119-140(1995).
RN [2] {ECO:0000313|RefSeq:NP_001129645.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [3] {ECO:0000313|EMBL:AAH68849.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH68849.2};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001129645.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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; BC068849; AAH68849.2; -; mRNA.
DR RefSeq; NP_001129645.1; NM_001136173.1.
DR DNASU; 100191024; -.
DR GeneID; 100191024; -.
DR KEGG; xla:100191024; -.
DR CTD; 100191024; -.
DR Xenbase; XB-GENE-17336518; epha2.S.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 100191024; Expressed in intestine and 19 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd10480; EphR_LBD_A2; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd09543; SAM_EPH-A2; 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; 1.20.5.510; Single helix bin; 1.
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; IPR034263; EphA2_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; IPR002049; LE_dom.
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:SF12; EPHRIN TYPE-A RECEPTOR 3; 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; 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; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW Kinase {ECO:0000313|RefSeq:NP_001129645.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:NP_001129645.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001129645.1};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..978
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001129645.1"
FT /id="PRO_5033207503"
FT TRANSMEM 538..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..205
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 326..434
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 435..531
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 616..877
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 906..970
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 741
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 622..630
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 69..187
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 104..114
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 978 AA; 109367 MW; 936C6D37AC261046 CRC64;
MIMRAERIVP LLSLLLSNLF TALHTKEVVL LDFEKTQGEL GWLTHPYGKG WDLLQNVMNG
SLIYIYSVCS VQEGEQDNWL RTNWIYRSEA QRIFVELKFT VRDCNSFPGG SGTCKETFNL
YYMESDIDYG TNFQKRQFRK IDTVAPDDIT VPSDFTSRNV KVNVEVRSVG PLSRKGFYLA
FQDIGACVAL LSVRIYYKKC PSVVQGMAQF PETVAGADSQ SLAKVSGKCM NNAVSVNGED
PTMHCNTDGE WLVPIGHCLC QPGYEKVGDT CQACQPGFFK SETSNGPCLP CPDHTEPTSP
AATFCPCNDG FFRSTSDLSS APCTGFPSAP RDLTAVDLGS KVTLRWLPPS NSGGRSDITY
TVTCEKCVPE ASECTPCDSN SIRYSENPRE LKGTTLTIME LEPHLNYSFT VEARNGVSGS
GSSRSYATLR ISLNQTEPPK VTFINLDNQA TNSLSLSWSV PPRQQTRVWK YEVTYSKKHD
ANSYSVQRCE GNTVTLLKLA PGTTYVVRVQ TLTQEGVGVY SRDYEFHTLP GEETSNNAAA
IGGAIAGAIL IFIFVAIIIF MHRSRRNPNI RQSEEDIYFS KPEQLKPLKT YVDPHTYEDP
NKAVLKFTTE ISANSITRQK VIGAGEFGEV YKGILKLPGK KEAPVAVKTL KAGYTEKQRV
DFLSEASIMG QFCHHNIIRL EGVVSKNKTM MIVTEHMENG ALDKFLKDND GEFSPIQLVG
MLRGIAAGMK YLSEMNYVHR DLAARNILVN SQLVCKVSDF GLSRVLEDDP EATYTTSGGK
IPIRWTAPEA ISYRKFTSAS DVWSYGIVMW EVMSYGERPY WEMSNQEVMK AINEGFRLPA
PMDCPSAIYQ LMMQCWQQER NRRPKFPDIV SILDKLIRAP DSLKTLADFD PRISIRLPST
SGSEGMPFRT ISEWLDSIKM QQYTECFIAS PYNSMDKIIL MNQEDIKHLG IRQTGHQKRI
AFSILGLKEH ASTMGIPI
//