LOCUS       NP_031965               1004 aa            linear   ROD 14-JUN-2024
DEFINITION  ephrin type-A receptor 8 isoform 1 precursor [Mus musculus].
ACCESSION   NP_031965
VERSION     NP_031965.2
DBSOURCE    REFSEQ: accession NM_007939.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Shibata,M., Pattabiraman,K., Lorente-Galdos,B., Andrijevic,D.,
            Kim,S.K., Kaur,N., Muchnik,S.K., Xing,X., Santpere,G., Sousa,A.M.M.
            and Sestan,N.
  TITLE     Regulation of prefrontal patterning and connectivity by retinoic
            acid
  JOURNAL   Nature 598 (7881), 483-488 (2021)
   PUBMED   34599305
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Weiss,A.C., Bohnenpoll,T., Kurz,J., Blank,P., Airik,R.,
            Ludtke,T.H., Kleppa,M.J., Deuper,L., Kaiser,M., Mamo,T.M.,
            Costa,R., von Hahn,T., Trowe,M.O. and Kispert,A.
  TITLE     Delayed onset of smooth muscle cell differentiation leads to
            hydroureter formation in mice with conditional loss of the zinc
            finger transcription factor gene Gata2 in the ureteric mesenchyme
  JOURNAL   J Pathol 248 (4), 452-463 (2019)
   PUBMED   30916783
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Buenaventura,D.F., Corseri,A. and Emerson,M.M.
  TITLE     Identification of Genes With Enriched Expression in Early
            Developing Mouse Cone Photoreceptors
  JOURNAL   Invest Ophthalmol Vis Sci 60 (8), 2787-2799 (2019)
   PUBMED   31260032
REFERENCE   4  (residues 1 to 1004)
  AUTHORS   Bibollet-Bahena,O., Okafuji,T., Hokamp,K., Tear,G. and
            Mitchell,K.J.
  TITLE     A dual-strategy expression screen for candidate connectivity labels
            in the developing thalamus
  JOURNAL   PLoS One 12 (5), e0177977 (2017)
   PUBMED   28558017
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1004)
  AUTHORS   Teng,T., Gaillard,A., Muzerelle,A. and Gaspar,P.
  TITLE     EphrinA5 Signaling Is Required for the Distinctive Targeting of
            Raphe Serotonin Neurons in the Forebrain
  JOURNAL   eNeuro 4 (1) (2017)
   PUBMED   28197551
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1004)
  AUTHORS   Choi,S. and Park,S.
  TITLE     Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates
            Fyn binding to the Tyr-615 site by enhancing tyrosine kinase
            activity
  JOURNAL   Oncogene 18 (39), 5413-5422 (1999)
   PUBMED   10498895
REFERENCE   7  (residues 1 to 1004)
  AUTHORS   Rogers,J.H., Ciossek,T., Menzel,P. and Pasquale,E.B.
  TITLE     Eph receptors and ephrins demarcate cerebellar lobules before and
            during their formation
  JOURNAL   Mech Dev 87 (1-2), 119-128 (1999)
   PUBMED   10495276
REFERENCE   8  (residues 1 to 1004)
  AUTHORS   Frisen,J. and Barbacid,M.
  TITLE     Genetic analysis of the role of Eph receptors in the development of
            the mammalian nervous system
  JOURNAL   Cell Tissue Res 290 (2), 209-215 (1997)
   PUBMED   9321682
  REMARK    Review article
REFERENCE   9  (residues 1 to 1004)
  AUTHORS   Park,S., Frisen,J. and Barbacid,M.
  TITLE     Aberrant axonal projections in mice lacking EphA8 (Eek) tyrosine
            protein kinase receptors
  JOURNAL   EMBO J 16 (11), 3106-3114 (1997)
   PUBMED   9214628
REFERENCE   10 (residues 1 to 1004)
  AUTHORS   Park,S. and Sanchez,M.P.
  TITLE     The Eek receptor, a member of the Eph family of tyrosine protein
            kinases, can be activated by three different Eph family ligands
  JOURNAL   Oncogene 14 (5), 533-542 (1997)
   PUBMED   9053851
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL627214.15.
            
            On Jul 31, 2007 this sequence version replaced NP_031965.1.
            
            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 :: U72207.1, SRR17784649.97055.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [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..1004
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 69.05 cM"
     Protein         1..1004
                     /product="ephrin type-A receptor 8 isoform 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="EPH- and ELK-related kinase; tyrosine-protein
                     kinase receptor EEK; Ephrin type-A receptor 8 precursor
                     (Tyrosine-protein kinase receptor EEK) (EPH-and
                     ELK-related kinase)"
                     /calculated_mol_wt=108168
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2556
     mat_peptide     27..1004
                     /product="Ephrin type-A receptor 8. /id=PRO_0000016823"
                     /note="propagated from UniProtKB/Swiss-Prot (O09127.2)"
                     /calculated_mol_wt=108168
     Region          30..202
                     /region_name="EphR_LBD_A8"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 8;
                     cd10486"
                     /db_xref="CDD:198454"
     Site            order(54,56..60,67..68,70,72,103,105,110..111,153,
                     157..158,161..163,190..192,194)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198454"
     Region          <325..>518
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            339
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O09127.2)"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O09127.2)"
     Site            431
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O09127.2)"
     Region          439..530
                     /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(439,503,518)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(519..520,522..523)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            542..562
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O09127.2)"
     Region          <561..631
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          563..569
                     /region_name="Mediates interaction with ANKS1A and ANKS1B.
                     /evidence=ECO:0000269|PubMed:17875921"
                     /note="propagated from UniProtKB/Swiss-Prot (O09127.2)"
     Region          588..643
                     /region_name="Mediates interaction with PIK3CG and
                     required for endocytosis.
                     /evidence=ECO:0000269|PubMed:11416136"
                     /note="propagated from UniProtKB/Swiss-Prot (O09127.2)"
     Site            615
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:10498895; propagated from
                     UniProtKB/Swiss-Prot (O09127.2)"
     Region          629..895
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(640..643,646,648,664,666,696,712..715,759,763..764,
                     766,776..777)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            838
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:10498895; propagated from
                     UniProtKB/Swiss-Prot (O09127.2)"
     Region          932..994
                     /region_name="SAM_EPH-A8"
                     /note="SAM domain of EPH-A8 subfamily of tyrosine kinase
                     receptors; cd09550"
                     /db_xref="CDD:188949"
     Site            order(946,979)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188949"
     Region          1002..1004
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O09127.2)"
     CDS             1..1004
                     /gene="Epha8"
                     /gene_synonym="Eek; Hek3; mKIAA1459"
                     /coded_by="NM_007939.3:95..3109"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS18813.1"
                     /db_xref="GeneID:13842"
                     /db_xref="MGI:MGI:109378"
ORIGIN      
        1 mapararlsp alwvvtaaaa atcvsagrge vnlldtstih gdwgwltypa hgwdsinevd
       61 esfrpihtyq vcnvmspnqn nwlrtnwvpr dgarrvyaei kftlrdcnsi pgvlgtcket
      121 fnlhylesdr dlgastqesq flkidtiaad esftgadlgv rrlklntevr gvgplskrgf
      181 ylafqdigac lailslriyy kkcpamvrnl aafseavtga dssslvevrg qcvrhseerd
      241 tpkmycsaeg ewlvpigkcv csagyeerrd acmacelgfy ksapgdqlca rcpphshsat
      301 paaqtcrcdl syyraaldpp saactrppsa pvnlissvng tsvtlewapp ldpggrsdit
      361 ynavcrrcpw alshceacgs gtrfvpqqts laqasllvan llahmnysfw ieavngvsnl
      421 speprsaavv nittnqaaps qvvvirqera gqtsvsllwq epeqpngiil eyeikyyekd
      481 kemqsystlk avttratvsg lkpgtryvfq vrartsagcg rfsqamevet gkprprydtr
      541 tivwicltli tglvvlllll ickkrhcgys kafqdsdeek mhyqngqapp pvflplnhpp
      601 gkfpetqfsa ephtyeepgr agrsftreie asrihiekii gsgesgevcy grlqvpgqrd
      661 vpvaikalka gyterqrqdf lseaaimgqf dhpniirleg vvtrgrlami vteymengsl
      721 daflrthdgq ftivqlvgml rgvgagmryl sdlgyihrdl aarnvlvdgr lvckvsdfgl
      781 sraleddpea ayttaggkip irwtapeaia frtfssasdv wsfgvvmwev laygerpywn
      841 mtnqdvissv eegyrlpapm gcpralhqlm ldcwhkdraq rprfahvvsv ldalvhspes
      901 lratatvsrc pppafarscf dlraggsgng dltvgdwlds irmgryrdhf aaggysslgm
      961 vlrmnaqdvr algitlmghq kkilgsiqtm raqlsstqgp rrhl
//
