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O08680

- EPHA3_RAT

UniProt

O08680 - EPHA3_RAT

Protein

Ephrin type-A receptor 3

Gene

Epha3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development By similarity.By similarity

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei654 – 6541ATPPROSITE-ProRule annotation
    Active sitei747 – 7471Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi629 – 6346ATPPROSITE-ProRule annotation
    Nucleotide bindingi701 – 7077ATPPROSITE-ProRule annotation
    Nucleotide bindingi751 – 7522ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. GPI-linked ephrin receptor activity Source: UniProtKB

    GO - Biological processi

    1. cell migration Source: UniProtKB
    2. ephrin receptor signaling pathway Source: UniProtKB
    3. fasciculation of motor neuron axon Source: UniProtKB
    4. fasciculation of sensory neuron axon Source: UniProtKB
    5. fever generation Source: RGD
    6. regulation of actin cytoskeleton organization Source: UniProtKB
    7. regulation of epithelial to mesenchymal transition Source: UniProtKB
    8. regulation of focal adhesion assembly Source: UniProtKB
    9. regulation of microtubule cytoskeleton organization Source: UniProtKB
    10. regulation of Rho GTPase activity Source: UniProtKB
    11. response to cytokine Source: RGD
    12. response to lipopolysaccharide Source: RGD

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 5301.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-A receptor 3 (EC:2.7.10.1)
    Alternative name(s):
    EPH-like kinase 4
    Short name:
    EK4
    Short name:
    rEK4
    Tyrosine-protein kinase TYRO4
    Gene namesi
    Name:Epha3
    Synonyms:Rek4, Tyro4
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi68389. Epha3.

    Subcellular locationi

    GO - Cellular componenti

    1. early endosome Source: UniProtKB
    2. integral component of plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Chaini21 – 984964Ephrin type-A receptor 3PRO_0000016804Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis
    Modified residuei597 – 5971Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei603 – 6031Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei702 – 7021Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei780 – 7801Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei938 – 9381PhosphotyrosineBy similarity

    Post-translational modificationi

    Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-603 mediates interaction with NCK1. Dephosphorylated by PTPN1 By similarity.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiO08680.
    PRIDEiO08680.

    PTM databases

    PhosphoSiteiO08680.

    Expressioni

    Tissue specificityi

    Most abundant in the heart, brain and lung.

    Inductioni

    Down-regulated by IL1-beta in neonatal cardiac myocytes.

    Gene expression databases

    GenevestigatoriO08680.

    Interactioni

    Subunit structurei

    Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function. Interacts (phosphorylated) with PTPN1; dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts (phosphorylated) with CRK; mediates EFNA5-EPHA3 signaling through RHOA GTPase activation. Interacts with NCK1 (via SH2 domain); mediates EFNA5-EPHA3 signaling By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000043263.

    Structurei

    3D structure databases

    ProteinModelPortaliO08680.
    SMRiO08680. Positions 29-203, 614-907.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 541521ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini566 – 984419CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei542 – 56524HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 207179Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini325 – 435111Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini436 – 53297Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini622 – 883262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini912 – 97665SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi982 – 9843PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi189 – 322134Cys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
    Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    InParanoidiO08680.
    KOiK05104.
    PhylomeDBiO08680.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 2 hits.
    InterProiIPR027936. Eph_TM.
    IPR001090. Ephrin_rcpt_lig-bd_dom.
    IPR003961. Fibronectin_type3.
    IPR008979. Galactose-bd-like.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016257. Tyr_kinase_ephrin_rcpt.
    IPR001426. Tyr_kinase_rcpt_V_CS.
    [Graphical view]
    PfamiPF14575. EphA2_TM. 1 hit.
    PF01404. Ephrin_lbd. 1 hit.
    PF00041. fn3. 2 hits.
    PF07699. GCC2_GCC3. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00615. EPH_lbd. 1 hit.
    SM00060. FN3. 2 hits.
    SM00454. SAM. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS01186. EGF_2. 1 hit.
    PS51550. EPH_LBD. 1 hit.
    PS50853. FN3. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
    PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O08680-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDCHLSILIL FGCCVLSCSR ELSPQPSNEV NLLDSKTIQG ELGWISYPSH    50
    GWEEISGVDE HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK 100
    FTLRDCNSIP LVLGTCKETF NLYYMESDDD HGVKFLEHQF TKIDTIAADE 150
    SFTQMDLGDR ILKLNTEIRE VGPVNKKGFY LAFQDVGACV ALVSVRVYFK 200
    KCPFTVKNLA MFPDTVPMDS QSLVEVRGSC VNNSKEEDPP RMYCSTEGEW 250
    LVPIGKCTCN AGYEERGFIC QACRPGFYKA LDGVAKCTKC PPHSSTQEDG 300
    SMNCRCENNY FRAEKDPPSM ACTRPPSAPR NVISNINETS VILDWSWPLD 350
    TGGRKDITFN IICKKCGWNV RQCEPCSPNV RFLPRQLGLT NTTVTVTDLL 400
    AHTNYTFEID AINGVSELSS PPRQFAAVSI TTNQAAPSPV MTIKKDRTSR 450
    NSISLSWQEP EHPNGIILDY EVKYYEKQEQ ETSYTILRAR GTNVTISSLK 500
    PDTTYVFQIR ARTAAGYGTN SRKFEFENSP DSFSISGENS HVVMIAISAA 550
    VAIIVLTVVT YVLVGRFCGY HKSKHSSDEK RLHFGNGHLR LPGLRTYVDP 600
    HTYEDPTQAV HEFAKELDAT NIAIDKVVGA GEFGEVCSGR LKLPSKKEIS 650
    VAIKTLKVGY TEKQRRDFLG EASIMGQFDH PNIIRLEGVV TKSKPVMIVT 700
    EYMENGSLDS FLRKHDAQFT VIQLVGMLRG IASGMKYLSD MGYVHRDLAA 750
    RNILINSNLV CKVSDFGLSR VLEDDPEAAY TTRGGKIPVR WTSPEATAYR 800
    KFTSASDVWS YGIVLWEVMS YGERPYWEMS NQDVIKAVDE GYRLPLPMDC 850
    PAALYQLMLD CWQKDRNNRP KFEQIVSILD KLIRNPGSLK IITSAAARPS 900
    NLLLDQSNVD IATFHTTGDW LNGMRTAHCK EIFTGVEYSS CDTIAKISTD 950
    DMKKVGVTVV GPQKKIISSI KALETQSKNG PVPV 984
    Length:984
    Mass (Da):110,228
    Last modified:July 1, 1997 - v1
    Checksum:iF170C49312F7A0AB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69278 mRNA. Translation: AAC06273.1.
    PIRiPT0186.
    RefSeqiNP_113752.1. NM_031564.1.
    UniGeneiRn.10713.

    Genome annotation databases

    GeneIDi29210.
    KEGGirno:29210.
    UCSCiRGD:68389. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69278 mRNA. Translation: AAC06273.1 .
    PIRi PT0186.
    RefSeqi NP_113752.1. NM_031564.1.
    UniGenei Rn.10713.

    3D structure databases

    ProteinModelPortali O08680.
    SMRi O08680. Positions 29-203, 614-907.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000043263.

    PTM databases

    PhosphoSitei O08680.

    Proteomic databases

    PaxDbi O08680.
    PRIDEi O08680.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 29210.
    KEGGi rno:29210.
    UCSCi RGD:68389. rat.

    Organism-specific databases

    CTDi 2042.
    RGDi 68389. Epha3.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi O08680.
    KOi K05104.
    PhylomeDBi O08680.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 5301.

    Miscellaneous databases

    NextBioi 608380.
    PROi O08680.

    Gene expression databases

    Genevestigatori O08680.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 2 hits.
    InterProi IPR027936. Eph_TM.
    IPR001090. Ephrin_rcpt_lig-bd_dom.
    IPR003961. Fibronectin_type3.
    IPR008979. Galactose-bd-like.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016257. Tyr_kinase_ephrin_rcpt.
    IPR001426. Tyr_kinase_rcpt_V_CS.
    [Graphical view ]
    Pfami PF14575. EphA2_TM. 1 hit.
    PF01404. Ephrin_lbd. 1 hit.
    PF00041. fn3. 2 hits.
    PF07699. GCC2_GCC3. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00615. EPH_lbd. 1 hit.
    SM00060. FN3. 2 hits.
    SM00454. SAM. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS01186. EGF_2. 1 hit.
    PS51550. EPH_LBD. 1 hit.
    PS50853. FN3. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
    PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "IL-1 beta alters the expression of the receptor tyrosine kinase gene r-EphA3 in neonatal rat cardiomyocytes."
      Li Y.Y., McTiernan C.F., Feldman A.M.
      Am. J. Physiol. 274:H331-H341(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.

    Entry informationi

    Entry nameiEPHA3_RAT
    AccessioniPrimary (citable) accession number: O08680
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3