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P52803

- EFNA5_HUMAN

UniProt

P52803 - EFNA5_HUMAN

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Protein

Ephrin-A5

Gene

EFNA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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. plasma membrane Source: UniProtKB
Complete GO annotation...

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

BgeeiP52803.
CleanExiHS_EFNA5.
ExpressionAtlasiP52803. baseline and differential.
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 – 355Combined sources
Helixi41 – 433Combined sources
Beta strandi44 – 463Combined sources
Beta strandi49 – 524Combined sources
Beta strandi57 – 615Combined sources
Helixi71 – 733Combined sources
Beta strandi76 – 827Combined sources
Helixi84 – 896Combined sources
Turni93 – 953Combined sources
Beta strandi96 – 1027Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi113 – 1175Combined sources
Beta strandi135 – 14410Combined sources
Beta strandi153 – 1586Combined sources
Helixi161 – 1644Combined sources

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.
GeneTreeiENSGT00390000015107.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLHVEMLTLV FLVLWMCVFS QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI
60 70 80 90 100
DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW
110 120 130 140 150
ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS
160 170 180 190 200
CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR
210 220
GENAAQTPRI PSRLLAILLF LLAMLLTL
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.
GeneTreei ENSGT00390000015107.
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

Bgeei P52803.
CleanExi HS_EFNA5.
ExpressionAtlasi P52803. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 120 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