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Q15768

- EFNB3_HUMAN

UniProt

Q15768 - EFNB3_HUMAN

Protein

Ephrin-B3

Gene

EFNB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors 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. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons By similarity.By similarity

    GO - Molecular functioni

    1. ephrin receptor binding Source: MGI
    2. transmembrane-ephrin receptor activity Source: ProtInc

    GO - Biological processi

    1. adult walking behavior Source: Ensembl
    2. axon choice point recognition Source: Ensembl
    3. axon guidance Source: RefGenome
    4. cell-cell signaling Source: ProtInc
    5. ephrin receptor signaling pathway Source: MGI
    6. nervous system development Source: ProtInc
    7. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Host-virus interaction, Neurogenesis

    Enzyme and pathway databases

    SignaLinkiQ15768.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin-B3
    Alternative name(s):
    EPH-related receptor transmembrane ligand ELK-L3
    EPH-related receptor tyrosine kinase ligand 8
    Short name:
    LERK-8
    Gene namesi
    Name:EFNB3
    Synonyms:EPLG8, LERK8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:3228. EFNB3.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc
    2. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi124 – 1252LW → YM: Complete loss of Nipah protein G binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA27663.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Chaini28 – 340313Ephrin-B3PRO_0000008395Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi62 ↔ 104PROSITE-ProRule annotation
    Disulfide bondi92 ↔ 156PROSITE-ProRule annotation
    Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ15768.
    PRIDEiQ15768.

    PTM databases

    PhosphoSiteiQ15768.

    Miscellaneous databases

    PMAP-CutDBQ15768.

    Expressioni

    Tissue specificityi

    Highly expressed in brain; expressed in embryonic floor plate, roof plate and hindbrain segments.

    Gene expression databases

    BgeeiQ15768.
    CleanExiHS_EFNB3.
    GenevestigatoriQ15768.

    Organism-specific databases

    HPAiHPA001623.

    Interactioni

    Subunit structurei

    Interacts with GRIP1 and GRIP2. Binds to Nipah virus G protein.2 Publications

    Protein-protein interaction databases

    BioGridi108269. 7 interactions.
    DIPiDIP-59196N.
    IntActiQ15768. 4 interactions.
    STRINGi9606.ENSP00000226091.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BKFX-ray4.65C/D27-169[»]
    ProteinModelPortaliQ15768.
    SMRiQ15768. Positions 29-169.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 226199ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini248 – 34093CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei227 – 24721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 167140Ephrin RBDPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi338 – 3403PDZ-bindingSequence Analysis

    Sequence similaritiesi

    Belongs to the ephrin family.PROSITE-ProRule annotation
    Contains 1 ephrin RBD (ephrin receptor-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG268537.
    HOGENOMiHOG000220931.
    HOVERGENiHBG051448.
    InParanoidiQ15768.
    KOiK05463.
    OMAiPGKENMP.
    OrthoDBiEOG7288S5.
    PhylomeDBiQ15768.

    Family and domain databases

    Gene3Di2.60.40.420. 1 hit.
    InterProiIPR008972. Cupredoxin.
    IPR001799. Ephrin.
    IPR019765. Ephrin_CS.
    [Graphical view]
    PANTHERiPTHR11304. PTHR11304. 1 hit.
    PfamiPF00812. Ephrin. 1 hit.
    [Graphical view]
    PRINTSiPR01347. EPHRIN.
    ProDomiPD002533. Ephrin. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF49503. SSF49503. 1 hit.
    PROSITEiPS01299. EPHRIN_RBD_1. 1 hit.
    PS51551. EPHRIN_RBD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q15768-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPPHSGPGG VRVGALLLLG VLGLVSGLSL EPVYWNSANK RFQAEGGYVL    50
    YPQIGDRLDL LCPRARPPGP HSSPNYEFYK LYLVGGAQGR RCEAPPAPNL 100
    LLTCDRPDLD LRFTIKFQEY SPNLWGHEFR SHHDYYIIAT SDGTREGLES 150
    LQGGVCLTRG MKVLLRVGQS PRGGAVPRKP VSEMPMERDR GAAHSLEPGK 200
    ENLPGDPTSN ATSRGAEGPL PPPSMPAVAG AAGGLALLLL GVAGAGGAMC 250
    WRRRRAKPSE SRHPGPGSFG RGGSLGLGGG GGMGPREAEP GELGIALRGG 300
    GAADPPFCPH YEKVSGDYGH PVYIVQDGPP QSPPNIYYKV 340
    Length:340
    Mass (Da):35,835
    Last modified:November 1, 1996 - v1
    Checksum:iEDFF2A23C2FDE79F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti166 – 1661R → Q.
    VAR_002356

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U57001 mRNA. Translation: AAB05170.1.
    U66406 mRNA. Translation: AAC51203.1.
    U62775 mRNA. Translation: AAC50707.1.
    AK314841 mRNA. Translation: BAG37359.1.
    CH471108 Genomic DNA. Translation: EAW90133.1.
    CH471108 Genomic DNA. Translation: EAW90135.1.
    BC022499 mRNA. Translation: AAH22499.1.
    BC042944 mRNA. Translation: AAH42944.1.
    CCDSiCCDS11120.1.
    RefSeqiNP_001397.1. NM_001406.3.
    UniGeneiHs.26988.

    Genome annotation databases

    EnsembliENST00000226091; ENSP00000226091; ENSG00000108947.
    GeneIDi1949.
    KEGGihsa:1949.
    UCSCiuc002gis.3. human.

    Polymorphism databases

    DMDMi2494367.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U57001 mRNA. Translation: AAB05170.1 .
    U66406 mRNA. Translation: AAC51203.1 .
    U62775 mRNA. Translation: AAC50707.1 .
    AK314841 mRNA. Translation: BAG37359.1 .
    CH471108 Genomic DNA. Translation: EAW90133.1 .
    CH471108 Genomic DNA. Translation: EAW90135.1 .
    BC022499 mRNA. Translation: AAH22499.1 .
    BC042944 mRNA. Translation: AAH42944.1 .
    CCDSi CCDS11120.1.
    RefSeqi NP_001397.1. NM_001406.3.
    UniGenei Hs.26988.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BKF X-ray 4.65 C/D 27-169 [» ]
    ProteinModelPortali Q15768.
    SMRi Q15768. Positions 29-169.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108269. 7 interactions.
    DIPi DIP-59196N.
    IntActi Q15768. 4 interactions.
    STRINGi 9606.ENSP00000226091.

    PTM databases

    PhosphoSitei Q15768.

    Polymorphism databases

    DMDMi 2494367.

    Proteomic databases

    PaxDbi Q15768.
    PRIDEi Q15768.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000226091 ; ENSP00000226091 ; ENSG00000108947 .
    GeneIDi 1949.
    KEGGi hsa:1949.
    UCSCi uc002gis.3. human.

    Organism-specific databases

    CTDi 1949.
    GeneCardsi GC17P007608.
    HGNCi HGNC:3228. EFNB3.
    HPAi HPA001623.
    MIMi 602297. gene.
    neXtProti NX_Q15768.
    PharmGKBi PA27663.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268537.
    HOGENOMi HOG000220931.
    HOVERGENi HBG051448.
    InParanoidi Q15768.
    KOi K05463.
    OMAi PGKENMP.
    OrthoDBi EOG7288S5.
    PhylomeDBi Q15768.

    Enzyme and pathway databases

    SignaLinki Q15768.

    Miscellaneous databases

    ChiTaRSi EFNB3. human.
    GeneWikii EFNB3.
    GenomeRNAii 1949.
    NextBioi 7899.
    PMAP-CutDB Q15768.
    PROi Q15768.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15768.
    CleanExi HS_EFNB3.
    Genevestigatori Q15768.

    Family and domain databases

    Gene3Di 2.60.40.420. 1 hit.
    InterProi IPR008972. Cupredoxin.
    IPR001799. Ephrin.
    IPR019765. Ephrin_CS.
    [Graphical view ]
    PANTHERi PTHR11304. PTHR11304. 1 hit.
    Pfami PF00812. Ephrin. 1 hit.
    [Graphical view ]
    PRINTSi PR01347. EPHRIN.
    ProDomi PD002533. Ephrin. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF49503. SSF49503. 1 hit.
    PROSITEi PS01299. EPHRIN_RBD_1. 1 hit.
    PS51551. EPHRIN_RBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cerretti D.P.
      Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "cDNA cloning, chromosomal localization, and expression pattern of EPLG8, a new member of the EPLG gene family encoding ligands of EPH-related protein-tyrosine kinase receptors."
      Tang X.X., Pleasure D.E., Ikegaki N.
      Genomics 41:17-24(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Elk-L3, a novel transmembrane ligand for the Eph family of receptor tyrosine kinases, expressed in embryonic floor plate, roof plate and hindbrain segments."
      Gale N.W., Flenniken A., Compton D.C., Jenkins N.A., Copeland N.G., Gilbert D.J., Davis S., Wilkinson D.G., Yancopoulos G.D.
      Oncogene 13:1343-1352(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain cortex.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    7. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-42.
    8. "EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains."
      Brueckner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H., Klein R.
      Neuron 22:511-524(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRIP1 AND GRIP2.
      Tissue: Fetal brain.
    9. "Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virus."
      Negrete O.A., Wolf M.C., Aguilar H.C., Enterlein S., Wang W., Muehlberger E., Su S.V., Bertolotti-Ciarlet A., Flick R., Lee B.
      PLoS Pathog. 2:78-86(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NIPAH VIRUS PROTEIN G, MUTAGENESIS OF 124-LEU-TRP-125.

    Entry informationi

    Entry nameiEFNB3_HUMAN
    AccessioniPrimary (citable) accession number: Q15768
    Secondary accession number(s): B2RBW2
    , D3DTQ6, O00680, Q8TBH7, Q92875
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3