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P97605

- EFNA5_RAT

UniProt

P97605 - EFNA5_RAT

Protein

Ephrin-A5

Gene

Efna5

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Cell surface GPI-bound 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. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion By similarity.By similarity

    GO - Molecular functioni

    1. ephrin receptor binding Source: UniProtKB

    GO - Biological processi

    1. axonal fasciculation Source: RGD
    2. axon guidance Source: RefGenome
    3. brain development Source: RGD
    4. central nervous system development Source: RGD
    5. ephrin receptor signaling pathway Source: UniProtKB
    6. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
    7. regulation of actin cytoskeleton organization Source: UniProtKB
    8. regulation of cell-cell adhesion Source: UniProtKB
    9. regulation of focal adhesion assembly Source: UniProtKB
    10. regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
    11. regulation of microtubule cytoskeleton organization Source: UniProtKB
    12. regulation of Rac GTPase activity Source: UniProtKB
    13. regulation of Rho GTPase activity Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin-A5
    Alternative name(s):
    AL-1
    EPH-related receptor tyrosine kinase ligand 7
    Short name:
    LERK-7
    Gene namesi
    Name:Efna5
    Synonyms:Eplg7, Lerk7
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620391. Efna5.

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity. Membranecaveola By similarity; Lipid-anchorGPI-anchor By similarity
    Note: Compartmentalized in discrete caveolae-like membrane microdomains.By similarity

    GO - Cellular componenti

    1. anchored component of external side of plasma membrane Source: UniProtKB
    2. anchored component of plasma membrane Source: RefGenome
    3. caveola Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 203183Ephrin-A5PRO_0000008381Add
    BLAST
    Propeptidei204 – 22825Removed in mature formSequence AnalysisPRO_0000008382Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi62 ↔ 102PROSITE-ProRule annotation
    Disulfide bondi90 ↔ 151PROSITE-ProRule annotation
    Lipidationi203 – 2031GPI-anchor amidated asparagineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PRIDEiP97605.

    Expressioni

    Tissue specificityi

    Expressed in brain, heart, placenta and lung.

    Gene expression databases

    GenevestigatoriP97605.

    Interactioni

    Subunit structurei

    Binds to the receptor tyrosine kinases EPHA2, EPHA3, EPHB1 and EPHB2. Interacts with EPHA8; activates EPHA8. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000039406.

    Structurei

    3D structure databases

    ProteinModelPortaliP97605.
    SMRiP97605. Positions 28-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 162134Ephrin RBDPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG241965.
    HOGENOMiHOG000234373.
    HOVERGENiHBG051447.
    InParanoidiP97605.
    KOiK05462.
    PhylomeDBiP97605.

    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.

    P97605-1 [UniParc]FASTAAdd to Basket

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    MLHVEMLTLL FLVLWMCVFS QDPGSKVVAD RYAVYWNSSN PRFQRGDYHI    50
    DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW 100
    ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS 150
    CLKLKVFVRP TNSCMKTIGV RDRVFDVNDK VENSLEPADD TVHESAEPSR 200
    GENAAQTPRI PSRLLAILLF LLAMLLTL 228
    Length:228
    Mass (Da):26,358
    Last modified:December 15, 1998 - v2
    Checksum:i855985532D580022
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69279 mRNA. Translation: AAC05801.1.
    RefSeqiNP_446355.1. NM_053903.1.
    UniGeneiRn.10714.

    Genome annotation databases

    GeneIDi116683.
    KEGGirno:116683.
    UCSCiRGD:620391. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69279 mRNA. Translation: AAC05801.1 .
    RefSeqi NP_446355.1. NM_053903.1.
    UniGenei Rn.10714.

    3D structure databases

    ProteinModelPortali P97605.
    SMRi P97605. Positions 28-165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000039406.

    Proteomic databases

    PRIDEi P97605.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 116683.
    KEGGi rno:116683.
    UCSCi RGD:620391. rat.

    Organism-specific databases

    CTDi 1946.
    RGDi 620391. Efna5.

    Phylogenomic databases

    eggNOGi NOG241965.
    HOGENOMi HOG000234373.
    HOVERGENi HBG051447.
    InParanoidi P97605.
    KOi K05462.
    PhylomeDBi P97605.

    Miscellaneous databases

    NextBioi 619532.
    PROi P97605.

    Gene expression databases

    Genevestigatori P97605.

    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. "Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor involved in axon bundle formation."
      Winslow J.W., Moran P., Valverde J., Shih A., Yuan J.Q., Wong S.C., Tsai S.P., Goddard A., Henzel W.J., Hefti F., Beck K.D., Caras I.W.
      Neuron 14:973-981(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: Sprague-Dawley.
    2. "rLERK7, rat ligand for Eph-related receptor tyrosine kinase."
      Li Y.Y., McTiernan C.F., Feldman A.M.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.

    Entry informationi

    Entry nameiEFNA5_RAT
    AccessioniPrimary (citable) accession number: P97605
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3