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P52797

- EFNA3_HUMAN

UniProt

P52797 - EFNA3_HUMAN

Protein

Ephrin-A3

Gene

EFNA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (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 By similarity.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. axon guidance Source: RefGenome
    2. cell-cell signaling Source: ProtInc
    3. ephrin receptor signaling pathway Source: UniProtKB

    Enzyme and pathway databases

    SignaLinkiP52797.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin-A3
    Alternative name(s):
    EFL-2
    EHK1 ligand
    Short name:
    EHK1-L
    EPH-related receptor tyrosine kinase ligand 3
    Short name:
    LERK-3
    Gene namesi
    Name:EFNA3
    Synonyms:EFL2, EPLG3, LERK3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3223. EFNA3.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. integral component of plasma membrane Source: ProtInc
    3. membrane Source: UniProtKB-KW
    4. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27658.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 214192Ephrin-A3PRO_0000008369Add
    BLAST
    Propeptidei215 – 23824Removed in mature formSequence AnalysisPRO_0000008370Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi63 ↔ 110PROSITE-ProRule annotation
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi99 ↔ 158PROSITE-ProRule annotation
    Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
    Lipidationi214 – 2141GPI-anchor amidated glycineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PRIDEiP52797.

    Expressioni

    Tissue specificityi

    Expressed in brain, skeletal muscle, spleen, thymus, prostate, testis, ovary, small intestine, and peripheral blood leukocytes.

    Gene expression databases

    ArrayExpressiP52797.
    BgeeiP52797.
    CleanExiHS_EFNA3.
    GenevestigatoriP52797.

    Organism-specific databases

    HPAiCAB010494.

    Interactioni

    Subunit structurei

    Interacts with EPHA8; activates EPHA8.

    Protein-protein interaction databases

    BioGridi108264. 3 interactions.
    IntActiP52797. 1 interaction.
    MINTiMINT-1378559.
    STRINGi9606.ENSP00000357393.

    Structurei

    3D structure databases

    ProteinModelPortaliP52797.
    SMRiP52797. Positions 31-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 169140Ephrin 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

    eggNOGiNOG295575.
    HOGENOMiHOG000234373.
    HOVERGENiHBG051447.
    InParanoidiP52797.
    KOiK05462.
    OMAiCEQKSGP.
    OrthoDBiEOG70W3FD.
    PhylomeDBiP52797.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P52797-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAAPLLLLL LLVPVPLLPL LAQGPGGALG NRHAVYWNSS NQHLRREGYT    50
    VQVNVNDYLD IYCPHYNSSG VGPGAGPGPG GGAEQYVLYM VSRNGYRTCN 100
    ASQGFKRWEC NRPHAPHSPI KFSEKFQRYS AFSLGYEFHA GHEYYYISTP 150
    THNLHWKCLR MKVFVCCAST SHSGEKPVPT LPQFTMGPNV KINVLEDFEG 200
    ENPQVPKLEK SISGTSPKRE HLPLAVGIAF FLMTFLAS 238
    Length:238
    Mass (Da):26,350
    Last modified:October 1, 1996 - v1
    Checksum:i8EFD6AE8FE33FDDA
    GO
    Isoform 2 (identifier: P52797-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         170-196: TSHSGEKPVPTLPQFTMGPNVKINVLE → K

    Note: No experimental confirmation available.

    Show »
    Length:212
    Mass (Da):23,575
    Checksum:i275AA7F0383A5074
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 744Missing in AAA52368. (PubMed:7973638)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti190 – 1901V → M.
    Corresponds to variant rs17723260 [ dbSNP | Ensembl ].
    VAR_048937

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei170 – 19627TSHSG…INVLE → K in isoform 2. 1 PublicationVSP_055483Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14187 mRNA. Translation: AAC50078.1.
    L37360 mRNA. Translation: AAA52368.1.
    AK316248 mRNA. Translation: BAH14619.1.
    AL691442 Genomic DNA. Translation: CAI15318.1.
    CH471121 Genomic DNA. Translation: EAW53137.1.
    BC017722 mRNA. Translation: AAH17722.1.
    BC110406 mRNA. Translation: AAI10407.1.
    CCDSiCCDS1090.1.
    PIRiI38849.
    RefSeqiNP_004943.1. NM_004952.4.
    UniGeneiHs.516656.

    Genome annotation databases

    EnsembliENST00000368408; ENSP00000357393; ENSG00000143590. [P52797-1]
    GeneIDi1944.
    KEGGihsa:1944.
    UCSCiuc001fhf.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14187 mRNA. Translation: AAC50078.1 .
    L37360 mRNA. Translation: AAA52368.1 .
    AK316248 mRNA. Translation: BAH14619.1 .
    AL691442 Genomic DNA. Translation: CAI15318.1 .
    CH471121 Genomic DNA. Translation: EAW53137.1 .
    BC017722 mRNA. Translation: AAH17722.1 .
    BC110406 mRNA. Translation: AAI10407.1 .
    CCDSi CCDS1090.1.
    PIRi I38849.
    RefSeqi NP_004943.1. NM_004952.4.
    UniGenei Hs.516656.

    3D structure databases

    ProteinModelPortali P52797.
    SMRi P52797. Positions 31-165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108264. 3 interactions.
    IntActi P52797. 1 interaction.
    MINTi MINT-1378559.
    STRINGi 9606.ENSP00000357393.

    Proteomic databases

    PRIDEi P52797.

    Protocols and materials databases

    DNASUi 1944.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368408 ; ENSP00000357393 ; ENSG00000143590 . [P52797-1 ]
    GeneIDi 1944.
    KEGGi hsa:1944.
    UCSCi uc001fhf.3. human.

    Organism-specific databases

    CTDi 1944.
    GeneCardsi GC01P155051.
    HGNCi HGNC:3223. EFNA3.
    HPAi CAB010494.
    MIMi 601381. gene.
    neXtProti NX_P52797.
    PharmGKBi PA27658.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295575.
    HOGENOMi HOG000234373.
    HOVERGENi HBG051447.
    InParanoidi P52797.
    KOi K05462.
    OMAi CEQKSGP.
    OrthoDBi EOG70W3FD.
    PhylomeDBi P52797.

    Enzyme and pathway databases

    SignaLinki P52797.

    Miscellaneous databases

    GeneWikii EFNA3.
    GenomeRNAii 1944.
    NextBioi 7875.
    PROi P52797.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52797.
    Bgeei P52797.
    CleanExi HS_EFNA3.
    Genevestigatori P52797.

    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. "Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins."
      Kozlosky C.J., Maraskovsky E., McGrew J.T., Vanden Bos T., Teepe M., Lyman S.D., Srinivasan S., Fletcher F.A., Gayle R.B. III, Cerretti D.P., Beckmann M.P.
      Oncogene 10:299-306(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity."
      Davis S., Gale N.W., Aldrich T.H., Maisonpierre P.C., Lhotak V., Pawson T., Goldfarb M., Yancopoulos G.D.
      Science 266:816-819(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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] (ISOFORM 2).
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Brain and Duodenum.

    Entry informationi

    Entry nameiEFNA3_HUMAN
    AccessioniPrimary (citable) accession number: P52797
    Secondary accession number(s): B7ZAD3
    , D3DV85, Q0VGC9, Q5SR70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 122 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3