LOCUS       NP_034269                977 aa            linear   ROD 10-DEC-2024
DEFINITION  ephrin type-A receptor 2 precursor [Mus musculus].
ACCESSION   NP_034269 XP_987548
VERSION     NP_034269.2
DBSOURCE    REFSEQ: accession NM_010139.3
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 977)
  AUTHORS   Horner,J.L., Vu,M.P., Clark,J.T., Innis,I.J. and Cheng,C.
  TITLE     Canonical ligand-dependent and non-canonical ligand-independent
            EphA2 signaling in the eye lens of wild-type, knockout, and aging
            mice
  JOURNAL   Aging (Albany NY) 16 (20), 13039-13075 (2024)
   PUBMED   39466050
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Liu,X., Li,Y., Chen,C., Dong,J., Zhou,J., Tong,D., Wang,L., Gao,X.
            and Kang,X.
  TITLE     Exosomal EphA2 promotes tumor metastasis of triple-negative breast
            cancer by damaging endothelial barrier
  JOURNAL   Clin Exp Metastasis 40 (1), 105-116 (2023)
   PUBMED   36380015
  REMARK    GeneRIF: Exosomal EphA2 promotes tumor metastasis of
            triple-negative breast cancer by damaging endothelial barrier.
REFERENCE   4  (residues 1 to 977)
  AUTHORS   Xu,Z., Ye,Y., Huang,G., Li,Y., Guo,X., Li,L., Wu,Y., Xu,W., Nian,S.
            and Yuan,Q.
  TITLE     EphA2 recognizes Dermatophagoidespteronyssinus to mediate airway
            inflammation in asthma
  JOURNAL   Int Immunopharmacol 111, 109106 (2022)
   PUBMED   35969898
  REMARK    GeneRIF: EphA2 recognizes Dermatophagoidespteronyssinus to mediate
            airway inflammation in asthma.
REFERENCE   5  (residues 1 to 977)
  AUTHORS   Chanda,K., Jana,N.R. and Mukhopadhyay,D.
  TITLE     Long non-coding RNA MALAT1 protects against Abeta1-42 induced
            toxicity by regulating the expression of receptor tyrosine kinase
            EPHA2 via quenching miR-200a/26a/26b in Alzheimer's disease
  JOURNAL   Life Sci 302, 120652 (2022)
   PUBMED   35598655
  REMARK    GeneRIF: Long non-coding RNA MALAT1 protects against Abeta1-42
            induced toxicity by regulating the expression of receptor tyrosine
            kinase EPHA2 via quenching miR-200a/26a/26b in Alzheimer's disease.
REFERENCE   6  (residues 1 to 977)
  AUTHORS   Pandey,A., Duan,H. and Dixit,V.M.
  TITLE     Characterization of a novel Src-like adapter protein that
            associates with the Eck receptor tyrosine kinase
  JOURNAL   J Biol Chem 270 (33), 19201-19204 (1995)
   PUBMED   7543898
REFERENCE   7  (residues 1 to 977)
  AUTHORS   Mark,M.R., Scadden,D.T., Wang,Z., Gu,Q., Goddard,A. and
            Godowski,P.J.
  TITLE     rse, a novel receptor-type tyrosine kinase with homology to
            Axl/Ufo, is expressed at high levels in the brain
  JOURNAL   J Biol Chem 269 (14), 10720-10728 (1994)
   PUBMED   7511603
REFERENCE   8  (residues 1 to 977)
  AUTHORS   Nieto,M.A., Gilardi-Hebenstreit,P., Charnay,P. and Wilkinson,D.G.
  TITLE     A receptor protein tyrosine kinase implicated in the segmental
            patterning of the hindbrain and mesoderm
  JOURNAL   Development 116 (4), 1137-1150 (1992)
   PUBMED   1295734
REFERENCE   9  (residues 1 to 977)
  AUTHORS   Gilardi-Hebenstreit,P., Nieto,M.A., Frain,M., Mattei,M.G.,
            Chestier,A., Wilkinson,D.G. and Charnay,P.
  TITLE     An Eph-related receptor protein tyrosine kinase gene segmentally
            expressed in the developing mouse hindbrain
  JOURNAL   Oncogene 7 (12), 2499-2506 (1992)
   PUBMED   1281307
  REMARK    Erratum:[Oncogene. 1993 Apr;8(4):1103.. PMID: 8455939]
REFERENCE   10 (residues 1 to 977)
  AUTHORS   Lindberg,R.A. and Hunter,T.
  TITLE     cDNA cloning and characterization of eck, an epithelial cell
            receptor protein-tyrosine kinase in the eph/elk family of protein
            kinases
  JOURNAL   Mol Cell Biol 10 (12), 6316-6324 (1990)
   PUBMED   2174105
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CJ088701.1, AK144202.1 and AW457468.1.
            
            On or before May 4, 2006 this sequence version replaced
            XP_987548.1, NP_034269.1.
            
            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 :: AK137704.1, AK144202.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 73.67 cM"
     Protein         1..977
                     /product="ephrin type-A receptor 2 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 2; epithelial cell kinase;
                     tyrosine-protein kinase receptor ECK; tyrosine-protein
                     kinase receptor MPK-5; tyrosine-protein kinase receptor
                     SEK-2"
                     /calculated_mol_wt=106364
     Region          1..205
                     /region_name="Mediates interaction with CLDN4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03145.3)"
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
                     /calculated_mol_wt=2507
     mat_peptide     26..977
                     /product="Ephrin type-A receptor 2. /id=PRO_0000016801"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03145.3)"
                     /calculated_mol_wt=106364
     Region          27..200
                     /region_name="EphR_LBD_A2"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 2;
                     cd10480"
                     /db_xref="CDD:198448"
     Site            order(52,54..58,60,62,64..65,67..69,72,100,102,107,150,
                     154..155,158..160,187..189,191)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198448"
     Site            128..132
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198448"
     Site            order(330,405,418)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          331..425
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            408
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            order(419..420,422..423)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            436
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Region          439..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"
     Site            539..559
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03145.3)"
     Region          <570..611
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29317; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29317; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            589
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18387945,
                     ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Region          607..907
                     /region_name="Mediates interaction with ARHGEF16.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03145.3)"
     Region          608..876
                     /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(620..623,626,628,645,647,677,693..696,740,744..745,
                     747,757..758)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P29317; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P29317; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18387945; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            773
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18387945,
                     ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            870
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29317; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Region          887..977
                     /region_name="Negatively regulates interaction with
                     ARHGEF16. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03145.3)"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29317; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29317; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29317; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Region          903..972
                     /region_name="SAM_EPH-A2"
                     /note="SAM domain of EPH-A2 family of tyrosine kinase
                     receptors; cd09543"
                     /db_xref="CDD:188942"
     Site            order(918,942,957..958,961)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188942"
     Site            order(922,955)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188942"
     Site            922
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Site            931
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P29317; propagated from
                     UniProtKB/Swiss-Prot (Q03145.3)"
     Region          975..977
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03145.3)"
     CDS             1..977
                     /gene="Epha2"
                     /gene_synonym="Eck; Myk2; Sek-2; Sek2"
                     /coded_by="NM_010139.3:133..3066"
                     /db_xref="CCDS:CCDS18869.1"
                     /db_xref="GeneID:13836"
                     /db_xref="MGI:MGI:95278"
ORIGIN      
        1 melravgfcl allwgcalaa aaaqgkevvl ldfaamkgel gwlthpygkg wdlmqnimdd
       61 mpiymysvcn vvsgdqdnwl rtnwvyreea erifielkft vrdcnsfpgg asscketfnl
      121 yyaesdvdyg tnfqkrqftk idtiapdeit vssdfearnv klnveermvg pltrkgfyla
      181 fqdigacval lsvrvyykkc pemlqslarf petiavavsd tqplatvagt cvdhavvpyg
      241 gegplmhctv dgewlvpigq clcqegyekv edacracspg ffkseasesp clecpehtlp
      301 stegatscqc eegyfraped plsmsctrpp sapnyltaig mgakvelrwt apkdtggrqd
      361 ivysvtceqc wpesgecgpc easvrysepp haltrtsvtv sdlephmnyt favearngvs
      421 glvtsrsfrt asvsinqtep pkvrledrst tslsvtwsip vsqqsrvwky evtyrkkgda
      481 nsynvrrteg fsvtlddlap dttylvqvqa ltqegqgags kvhefqtlst egsanmavig
      541 gvavgvvlll vlagvglfih rrrrnlrarq ssedvrfsks eqlkplktyv dphtyedpnq
      601 avlkftteih pscvarqkvi gagefgevyk gtlkassgkk eipvaiktlk agytekqrvd
      661 flseasimgq fshhniirle gvvskykpmm iiteymenga ldkflrekdg efsvlqlvgm
      721 lrgiasgmky lanmnyvhrd laarnilvns nlvckvsdfg lsrvleddpe atyttsggki
      781 pirwtapeai syrkftsasd vwsygivmwe vmtygerpyw elsnhevmka indgfrlptp
      841 mdcpsaiyql mmqcwqqers rrpkfadivs ildklirapd slktladfdp rvsirlpsts
      901 gsegvpfrtv sewlesikmq qytehfmvag ytaiekvvqm snedikrigv rlpghqkria
      961 ysllglkdqv ntvgipi
//
