LOCUS       NP_001120791             986 aa            linear   ROD 03-APR-2024
DEFINITION  ephrin type-B receptor 2 precursor [Rattus norvegicus].
ACCESSION   NP_001120791 XP_001069612 XP_233574
VERSION     NP_001120791.2
DBSOURCE    REFSEQ: accession NM_001127319.4
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 986)
  AUTHORS   Duan,G.B., Wang,J.W., Sun,H.H., Dong,Z.Y., Zhang,Y., Wang,Z.X.,
            Chen,Y., Chen,Y., Huang,Y. and Xu,S.C.
  TITLE     Overexpression of EphB2 in the basolateral amygdala is crucial for
            inducing visceral pain sensitization in rats subjected to water
            avoidance stress
  JOURNAL   CNS Neurosci Ther 30 (2), e14611 (2024)
   PUBMED   38353051
  REMARK    GeneRIF: Overexpression of EphB2 in the basolateral amygdala is
            crucial for inducing visceral pain sensitization in rats subjected
            to water avoidance stress.
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Bodin,R., Paille,V., Oullier,T., Durand,T., Aubert,P., Le
            Berre-Scoul,C., Hulin,P., Neunlist,M. and Cisse,M.
  TITLE     The ephrin receptor EphB2 regulates the connectivity and activity
            of enteric neurons
  JOURNAL   J Biol Chem 297 (5), 101300 (2021)
   PUBMED   34648765
  REMARK    GeneRIF: The ephrin receptor EphB2 regulates the connectivity and
            activity of enteric neurons.
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wu,J., Lu,B., Yang,R., Chen,Y., Chen,X. and Li,Y.
  TITLE     EphB2 knockdown decreases the formation of astroglial-fibrotic
            scars to promote nerve regeneration after spinal cord injury in
            rats
  JOURNAL   CNS Neurosci Ther 27 (6), 714-724 (2021)
   PUBMED   33794069
  REMARK    GeneRIF: EphB2 knockdown decreases the formation of
            astroglial-fibrotic scars to promote nerve regeneration after
            spinal cord injury in rats.
REFERENCE   4  (residues 1 to 986)
  AUTHORS   Sun,C.L., Li,C.W., He,N., Tang,Y.Z., Li,X.L., Xue,F.S. and Ni,J.X.
  TITLE     Blockade of Erythropoietin-Producing Human Hepatocellular Carcinoma
            Receptor B1 in Spinal Dorsal Horn Alleviates Visceral Pain in Rats
  JOURNAL   Pain Res Manag 2021, 7582494 (2021)
   PUBMED   33880135
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 986)
  AUTHORS   Yu,T., Chu,S., Liu,X., Li,J., Chen,Q., Xu,M., Wu,H., Li,M.,
            Dong,Y., Zhu,F., Zhou,H., Hu,D. and Fan,H.
  TITLE     Extracellular vesicles derived from EphB2-overexpressing bone
            marrow mesenchymal stem cells ameliorate DSS-induced colitis by
            modulating immune balance
  JOURNAL   Stem Cell Res Ther 12 (1), 181 (2021)
   PUBMED   33722292
  REMARK    GeneRIF: Extracellular vesicles derived from EphB2-overexpressing
            bone marrow mesenchymal stem cells ameliorate DSS-induced colitis
            by modulating immune balance.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 986)
  AUTHORS   Cowan,C.A., Yokoyama,N., Bianchi,L.M., Henkemeyer,M. and
            Fritzsch,B.
  TITLE     EphB2 guides axons at the midline and is necessary for normal
            vestibular function
  JOURNAL   Neuron 26 (2), 417-430 (2000)
   PUBMED   10839360
REFERENCE   7  (residues 1 to 986)
  AUTHORS   Adams,R.H., Wilkinson,G.A., Weiss,C., Diella,F., Gale,N.W.,
            Deutsch,U., Risau,W. and Klein,R.
  TITLE     Roles of ephrinB ligands and EphB receptors in cardiovascular
            development: demarcation of arterial/venous domains, vascular
            morphogenesis, and sprouting angiogenesis
  JOURNAL   Genes Dev 13 (3), 295-306 (1999)
   PUBMED   9990854
REFERENCE   8  (residues 1 to 986)
  AUTHORS   Torres,R., Firestein,B.L., Dong,H., Staudinger,J., Olson,E.N.,
            Huganir,R.L., Bredt,D.S., Gale,N.W. and Yancopoulos,G.D.
  TITLE     PDZ proteins bind, cluster, and synaptically colocalize with Eph
            receptors and their ephrin ligands
  JOURNAL   Neuron 21 (6), 1453-1463 (1998)
   PUBMED   9883737
REFERENCE   9  (residues 1 to 986)
  AUTHORS   Orioli,D., Henkemeyer,M., Lemke,G., Klein,R. and Pawson,T.
  TITLE     Sek4 and Nuk receptors cooperate in guidance of commissural axons
            and in palate formation
  JOURNAL   EMBO J 15 (22), 6035-6049 (1996)
   PUBMED   8947026
REFERENCE   10 (residues 1 to 986)
  AUTHORS   Henkemeyer,M., Orioli,D., Henderson,J.T., Saxton,T.M., Roder,J.,
            Pawson,T. and Klein,R.
  TITLE     Nuk controls pathfinding of commissural axons in the mammalian
            central nervous system
  JOURNAL   Cell 86 (1), 35-46 (1996)
   PUBMED   8689685
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Dec 2, 2020 this sequence version replaced NP_001120791.1.
            
            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 :: SRR26360194.390913.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..986
                     /product="ephrin type-B receptor 2 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-B receptor 2; ephrin type-B receptor
                     2-like"
                     /calculated_mol_wt=107341
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2565
     Region          19..196
                     /region_name="EphR_LBD_B2"
                     /note="Ligand Binding Domain of Ephrin type-B Receptor 2;
                     cd10477"
                     /db_xref="CDD:198445"
     Site            order(28..30,32,44..47,49,53,55,57,60,93..95,99,101,147,
                     149..156,158..159,184,186,188)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198445"
     Site            order(325,400,415)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          326..421
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(416,418,420..421)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            order(436,500,515)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          437..520
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(516..517,519..520)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          <565..617
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          616..884
                     /region_name="PTKc_EphR_B"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphB Ephrin Receptors; cd05065"
                     /db_xref="CDD:173638"
     Site            order(627..631,635,651,653,699..700,702,706,746,750..751,
                     753,764,785..789,798,832)
                     /site_type="active"
                     /db_xref="CDD:173638"
     Site            order(627..629,631,635,651,653,699..700,702,706,751,753,
                     764)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173638"
     Site            order(746,750,785..789,798,832)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173638"
     Site            763..791
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173638"
     Region          910..980
                     /region_name="SAM_EPH-B2"
                     /note="SAM domain of EPH-B2 subfamily of tyrosine kinase
                     receptors; cd09552"
                     /db_xref="CDD:188951"
     Site            order(912..913,915,937,943..944,952,960..963,965..966,974,
                     978)
                     /site_type="other"
                     /note="homooligomer interface [polypeptide binding]"
                     /db_xref="CDD:188951"
     Site            order(912,915,921,942,970,973..974)
                     /site_type="other"
                     /note="putative homodimer interface (head-to-head)
                     [polypeptide binding]"
                     /db_xref="CDD:188951"
     Site            order(930,963)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188951"
     Site            order(946..951,954,972,975,978..979)
                     /site_type="other"
                     /note="homodimer interface (tail-to-tail) [polypeptide
                     binding]"
                     /db_xref="CDD:188951"
     CDS             1..986
                     /gene="Ephb2"
                     /gene_synonym="RGD1564232"
                     /coded_by="NM_001127319.4:161..3121"
                     /db_xref="GeneID:313633"
                     /db_xref="RGD:1564232"
ORIGIN      
        1 mavrrlgaal lllpllaave etlmdsttat aelgwmvhpp sgweevsgyd enmntirtyq
       61 vcnvfessqn nwlrtkfirr rgahrihvem kfsvrdcssi psvpgscket fnlyyyeadf
      121 dlatktfpnw menpwvkvdt iaadesfsqv dlggrvmkin tevrsfgpvs rngfylafqd
      181 yggcmsliav rvfyrkcprv iqngaifqet lsgaestslv aargsciana eevdvpikly
      241 cngdgewlvp igrcmckagf eavengtvcr gcpsgtfkan qgdeacthcp insrttsega
      301 tncvcrngyy radldpldmp cttipsapqa vissvnetsl mlewtpprds ggredlvyni
      361 ickscgsgrg actrcgdnvq yaprqlglte priyisdlla htqytfeiqa vngvtdqspf
      421 spqfasvnit tnqaapsavs imhqvsrtvd sitlswsqpd qpngvildye lqyyekelse
      481 ynataikspt ntvtvqglka gaiyvfqvra rtvagygrys gkmyfqtmte aeyqtsikek
      541 lplivgssaa gvvfviavvv iaivcnrrgf eradseytdk lqhytsghmt pgmkiyidpf
      601 tyedpneavr efakeidisc vkieqvigag efgevcsghl klpgkreifv aiktlksgyt
      661 ekqrrdflse asimgqfdhp nvihlegvvt kstpvmiite fmengsldsf lrqndgqftv
      721 iqlvgmlrgi aagmkyladm nyvhrdlaar nilvnsnlvc kvsdfglsrf leddtsdpty
      781 tsalggkipi rwtapeaiqy rkftsasdvw sygivmwevm sygerpywdm tnqdvinaie
      841 qdyrlpppmd cpsalhqlml dcwqkdrnhr pkfgqivntl dkmirnpnsl kamaplssgi
      901 nlplldrtip dytsfntvde wleaikmgqy kesftnagft sfdvvsqmmm edilrvgvtl
      961 aghqkkilns iqvmraqmnq iqsvev
//
