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P52803

- EFNA5_HUMAN

UniProt

P52803 - EFNA5_HUMAN

Protein

Ephrin-A5

Gene

EFNA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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.2 Publications

    GO - Molecular functioni

    1. chemorepellent activity Source: Ensembl
    2. ephrin receptor binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Enzyme and pathway databases

    SignaLinkiP52803.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:3225. EFNA5.

    Subcellular locationi

    Cell membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication. Membranecaveola 1 Publication; Lipid-anchorGPI-anchor 1 Publication
    Note: Compartmentalized in discrete caveolae-like membrane microdomains.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27660.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 203183Ephrin-A5PRO_0000008377Add
    BLAST
    Propeptidei204 – 22825Removed in mature formSequence AnalysisPRO_0000008378Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi37 – 371N-linked (GlcNAc...)1 Publication
    Disulfide bondi62 ↔ 102
    Disulfide bondi90 ↔ 151
    Lipidationi203 – 2031GPI-anchor amidated asparagineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiP52803.
    PaxDbiP52803.
    PeptideAtlasiP52803.
    PRIDEiP52803.

    Expressioni

    Gene expression databases

    ArrayExpressiP52803.
    BgeeiP52803.
    CleanExiHS_EFNA5.
    GenevestigatoriP52803.

    Organism-specific databases

    HPAiCAB013282.

    Interactioni

    Subunit structurei

    Binds to EPHB2. Interacts with EPHA8; activates EPHA8 By similarity. Binds to the receptor tyrosine kinases EPHA2, EPHA3 and EPHB1. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi108266. 6 interactions.
    DIPiDIP-48296N.
    IntActiP52803. 2 interactions.
    MINTiMINT-7241704.
    STRINGi9606.ENSP00000328777.

    Structurei

    Secondary structure

    1
    228
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 355
    Helixi41 – 433
    Beta strandi49 – 524
    Beta strandi57 – 615
    Beta strandi77 – 826
    Helixi84 – 885
    Turni93 – 953
    Beta strandi97 – 1015
    Beta strandi108 – 1114
    Beta strandi113 – 1175
    Beta strandi135 – 1428
    Beta strandi153 – 1586
    Turni161 – 1633

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2X11X-ray4.83B27-166[»]
    3MX0X-ray3.51B/D28-165[»]
    4BK5X-ray4.00C27-166[»]
    4BKAX-ray5.30C27-166[»]
    4L0PX-ray2.26B27-166[»]
    4M4RX-ray3.13B/D/F/H27-165[»]
    ProteinModelPortaliP52803.
    SMRiP52803. Positions 28-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52803.

    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.
    InParanoidiP52803.
    KOiK05462.
    OMAiTERYILY.
    OrthoDBiEOG70W3FD.
    PhylomeDBiP52803.

    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.

    P52803-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLHVEMLTLV FLVLWMCVFS QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI    50
    DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW 100
    ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS 150
    CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR 200
    GENAAQTPRI PSRLLAILLF LLAMLLTL 228
    Length:228
    Mass (Da):26,297
    Last modified:October 1, 1996 - v1
    Checksum:i6893B1CCACFF3F57
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551N → K.
    Corresponds to variant rs469062 [ dbSNP | Ensembl ].
    VAR_012035

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26403 mRNA. Translation: AAB60377.1.
    BC075054 mRNA. Translation: AAH75054.1.
    BC075055 mRNA. Translation: AAH75055.1.
    CCDSiCCDS4097.1.
    PIRiI58170.
    RefSeqiNP_001953.1. NM_001962.2.
    UniGeneiHs.288741.

    Genome annotation databases

    EnsembliENST00000333274; ENSP00000328777; ENSG00000184349.
    GeneIDi1946.
    KEGGihsa:1946.
    UCSCiuc003kol.3. human.

    Polymorphism databases

    DMDMi1706678.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26403 mRNA. Translation: AAB60377.1 .
    BC075054 mRNA. Translation: AAH75054.1 .
    BC075055 mRNA. Translation: AAH75055.1 .
    CCDSi CCDS4097.1.
    PIRi I58170.
    RefSeqi NP_001953.1. NM_001962.2.
    UniGenei Hs.288741.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2X11 X-ray 4.83 B 27-166 [» ]
    3MX0 X-ray 3.51 B/D 28-165 [» ]
    4BK5 X-ray 4.00 C 27-166 [» ]
    4BKA X-ray 5.30 C 27-166 [» ]
    4L0P X-ray 2.26 B 27-166 [» ]
    4M4R X-ray 3.13 B/D/F/H 27-165 [» ]
    ProteinModelPortali P52803.
    SMRi P52803. Positions 28-165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108266. 6 interactions.
    DIPi DIP-48296N.
    IntActi P52803. 2 interactions.
    MINTi MINT-7241704.
    STRINGi 9606.ENSP00000328777.

    Polymorphism databases

    DMDMi 1706678.

    Proteomic databases

    MaxQBi P52803.
    PaxDbi P52803.
    PeptideAtlasi P52803.
    PRIDEi P52803.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000333274 ; ENSP00000328777 ; ENSG00000184349 .
    GeneIDi 1946.
    KEGGi hsa:1946.
    UCSCi uc003kol.3. human.

    Organism-specific databases

    CTDi 1946.
    GeneCardsi GC05M106712.
    HGNCi HGNC:3225. EFNA5.
    HPAi CAB013282.
    MIMi 601535. gene.
    neXtProti NX_P52803.
    PharmGKBi PA27660.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG241965.
    HOGENOMi HOG000234373.
    HOVERGENi HBG051447.
    InParanoidi P52803.
    KOi K05462.
    OMAi TERYILY.
    OrthoDBi EOG70W3FD.
    PhylomeDBi P52803.

    Enzyme and pathway databases

    SignaLinki P52803.

    Miscellaneous databases

    EvolutionaryTracei P52803.
    GeneWikii EFNA5.
    Ephrin-A5.
    GenomeRNAii 1946.
    NextBioi 7887.
    PROi P52803.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52803.
    Bgeei P52803.
    CleanExi HS_EFNA5.
    Genevestigatori P52803.

    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].
    2. "LERK-7: a ligand of the Eph-related kinases is developmentally regulated in the brain."
      Kozlosky C.J., Vanden Bos T., Park L.S., Cerretti D.P., Carpenter M.K.
      Cytokine 9:540-549(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "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.
    4. "Compartmentalized signaling by GPI-anchored ephrin-A5 requires the Fyn tyrosine kinase to regulate cellular adhesion."
      Davy A., Gale N.W., Murray E.W., Klinghoffer R.A., Soriano P., Feuerstein C., Robbins S.M.
      Genes Dev. 13:3125-3135(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling."
      Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M., Boyd A.W., Alewood P.F., Lackmann M.
      J. Cell Sci. 115:1059-1072(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL-CELL ADHESION, EPHA3-BINDING, SUBCELLULAR LOCATION.
    6. "Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans."
      Janes P.W., Saha N., Barton W.A., Kolev M.V., Wimmer-Kleikamp S.H., Nievergall E., Blobel C.P., Himanen J.P., Lackmann M., Nikolov D.B.
      Cell 123:291-304(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH ADAM10 AND EPHA3.
    7. "Crystal structure of the human ephrin-A5 ectodomain."
      Nikolov D.B., Li C., Lackmann M., Jeffrey P., Himanen J.P.
      Protein Sci. 16:996-1000(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-189, GLYCOSYLATION AT ASN-37.

    Entry informationi

    Entry nameiEFNA5_HUMAN
    AccessioniPrimary (citable) accession number: P52803
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 119 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, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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