LOCUS       NP_113752                984 aa            linear   ROD 01-APR-2024
DEFINITION  ephrin type-A receptor 3 precursor [Rattus norvegicus].
ACCESSION   NP_113752 XP_346415
VERSION     NP_113752.2
DBSOURCE    REFSEQ: accession NM_031564.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Li,M., Yang,C., Liu,X., Yuan,L., Zhang,F., Wang,M., Miao,D., Gu,X.,
            Jiang,S., Cui,B., Tong,J. and Yu,Z.
  TITLE     EphA3 promotes malignant transformation of colorectal epithelial
            cells by upregulating oncogenic pathways
  JOURNAL   Cancer Lett 383 (2), 195-203 (2016)
   PUBMED   27721017
  REMARK    GeneRIF: EphA3 promotes malignant transformation of colorectal
            epithelial cells by upregulating oncogenic signaling pathways.
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Buensuceso,A.V. and Deroo,B.J.
  TITLE     The ephrin signaling pathway regulates morphology and adhesion of
            mouse granulosa cells in vitro
  JOURNAL   Biol Reprod 88 (1), 25 (2013)
   PUBMED   23242526
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Brennaman,L.H., Zhang,X., Guan,H., Triplett,J.W., Brown,A.,
            Demyanenko,G.P., Manis,P.B., Landmesser,L. and Maness,P.F.
  TITLE     Polysialylated NCAM and ephrinA/EphA regulate synaptic development
            of GABAergic interneurons in prefrontal cortex
  JOURNAL   Cereb Cortex 23 (1), 162-177 (2013)
   PUBMED   22275477
REFERENCE   4  (residues 1 to 984)
  AUTHORS   Wang,L., Klein,R., Zheng,B. and Marquardt,T.
  TITLE     Anatomical coupling of sensory and motor nerve trajectory via axon
            tracking
  JOURNAL   Neuron 71 (2), 263-277 (2011)
   PUBMED   21791286
REFERENCE   5  (residues 1 to 984)
  AUTHORS   Nievergall,E., Janes,P.W., Stegmayer,C., Vail,M.E., Haj,F.G.,
            Teng,S.W., Neel,B.G., Bastiaens,P.I. and Lackmann,M.
  TITLE     PTP1B regulates Eph receptor function and trafficking
  JOURNAL   J Cell Biol 191 (6), 1189-1203 (2010)
   PUBMED   21135139
REFERENCE   6  (residues 1 to 984)
  AUTHORS   Cheng,N., Brantley,D., Fang,W.B., Liu,H., Fanslow,W.,
            Cerretti,D.P., Bussell,K.N., Reith,A., Jackson,D. and Chen,J.
  TITLE     Inhibition of VEGF-dependent multistage carcinogenesis by soluble
            EphA receptors
  JOURNAL   Neoplasia 5 (5), 445-456 (2003)
   PUBMED   14670182
REFERENCE   7  (residues 1 to 984)
  AUTHORS   Yang,J., Kim,O., Wu,J. and Qiu,Y.
  TITLE     Interaction between tyrosine kinase Etk and a RUN domain- and FYVE
            domain-containing protein RUFY1. A possible role of ETK in
            regulation of vesicle trafficking
  JOURNAL   J Biol Chem 277 (33), 30219-30226 (2002)
   PUBMED   11877430
REFERENCE   8  (residues 1 to 984)
  AUTHORS   Munoz,J.J., Alonso-C,L.M., Sacedon,R., Crompton,T., Vicente,A.,
            Jimenez,E., Varas,A. and Zapata,A.G.
  TITLE     Expression and function of the Eph A receptors and their ligands
            ephrins A in the rat thymus
  JOURNAL   J Immunol 169 (1), 177-184 (2002)
   PUBMED   12077243
REFERENCE   9  (residues 1 to 984)
  AUTHORS   Lawrenson,I.D., Wimmer-Kleikamp,S.H., Lock,P., Schoenwaelder,S.M.,
            Down,M., Boyd,A.W., Alewood,P.F. and Lackmann,M.
  TITLE     Ephrin-A5 induces rounding, blebbing and de-adhesion of
            EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated
            signalling
  JOURNAL   J Cell Sci 115 (Pt 5), 1059-1072 (2002)
   PUBMED   11870224
REFERENCE   10 (residues 1 to 984)
  AUTHORS   Li,Y.Y., McTiernan,C.F. and Feldman,A.M.
  TITLE     IL-1 beta alters the expression of the receptor tyrosine kinase
            gene r-EphA3 in neonatal rat cardiomyocytes
  JOURNAL   Am J Physiol 274 (1), H331-H341 (1998)
   PUBMED   9458884
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Nov 26, 2020 this sequence version replaced NP_113752.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U69278.1, SRR26643298.65815.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11p12"
     Protein         1..984
                     /product="ephrin type-A receptor 3 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 3; tyrosine-protein kinase
                     TYRO4; tyrosine-protein kinase receptor REK4; EK4; rEK4;
                     EPH-like kinase 4"
                     /calculated_mol_wt=108030
     sig_peptide     1..20
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
                     /calculated_mol_wt=2180
     mat_peptide     21..984
                     /product="Ephrin type-A receptor 3. /id=PRO_0000016804"
                     /note="propagated from UniProtKB/Swiss-Prot (O08680.1)"
                     /calculated_mol_wt=108030
     Region          29..201
                     /region_name="EphR_LBD_A3"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 3;
                     cd10481"
                     /db_xref="CDD:198449"
     Site            order(53,55..59,66..67,69,71,102,104,109..110,152,
                     156..157,160..162,189..191,193)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198449"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
     Region          <323..>516
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
     Site            391
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
     Site            404
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
     Region          437..528
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(437,501,516)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            493
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
     Site            order(517..518,520..521)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            542..565
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08680.1)"
     Region          <566..619
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P29320; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P29320; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
     Region          617..883
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(628,630..632,636,652,654,700..701,703,747,751..752,
                     754,765,784..788,797,831)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(628..632,636,652,654,700..703,706..707,751..752,754,
                     765)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P29320; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
     Site            order(747,751,784..788,797,831)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            764..790
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P29320; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
     Region          913..975
                     /region_name="SAM_EPH-A3"
                     /note="SAM domain of EPH-A3 subfamily of tyrosine kinase
                     receptors; cd09544"
                     /db_xref="CDD:188943"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P29319; propagated from
                     UniProtKB/Swiss-Prot (O08680.1)"
     Region          982..984
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O08680.1)"
     CDS             1..984
                     /gene="Epha3"
                     /coded_by="NM_031564.2:35..2989"
                     /db_xref="GeneID:29210"
                     /db_xref="RGD:68389"
ORIGIN      
        1 mdchlsilil lgccvlscsr elspqpsnev nlldsktiqg elgwisypsh gweeisgvde
       61 hytpirtyqv cnvmdhsqnn wlrtnwvprn saqkiyvelk ftlrdcnsip lvlgtcketf
      121 nlyymesddd hgvkflehqf tkidtiaade sftqmdlgdr ilklnteire vgpvnkkgfy
      181 lafqdvgacv alvsvrvyfk kcpftvknla mfpdtvpmds qslvevrgsc vnnskeedpp
      241 rmycstegew lvpigkctcn agyeergfic qacrpgfyka ldgvakctkc pphsstqedg
      301 smncrcenny fraekdppsm actrppsapr nvisninets vildwswpld tggrkditfn
      361 iickkcgwnv rqcepcspnv rflprqlglt nttvtvtdll ahtnytfeid aingvselss
      421 pprqfaavsi ttnqaapspv mtikkdrtsr nsislswqep ehpngiildy evkyyekqeq
      481 etsytilrar gtnvtisslk pdttyvfqir artaagygtn srkfefetsp dsfsisgens
      541 hvvmiaisaa vaiivltvvt yvlvgrfcgy hkskhssdek rlhfgnghlr lpglrtyvdp
      601 htyedptqav hefakeldat niaidkvvga gefgevcsgr lklpskkeis vaiktlkvgy
      661 tekqrrdflg easimgqfdh pniirlegvv tkskpvmivt eymengslds flrkhdaqft
      721 viqlvgmlrg iasgmkylsd mgyvhrdlaa rnilinsnlv ckvsdfglsr vleddpeaay
      781 ttrggkipir wtspeaiayr kftsasdvws ygivlwevms ygerpywems nqdvikavde
      841 gyrlpppmdc paalyqlmld cwqkdrnnrp kfeqivsild klirnpgslk iitsaaarps
      901 nllldqsnvd iatfhttgdw lngmrtahck eiftgveyss cdtiakistd dmkkvgvtvv
      961 gpqkkiissi kaletqskng pvpv
//
