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Protein

Ephrin-A5

Gene

EFNA5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • chemorepellent activity Source: Ensembl
  • ephrin receptor binding Source: UniProtKB
  • neurotrophin TRKA receptor binding Source: BHF-UCL
  • neurotrophin TRKB receptor binding Source: BHF-UCL
  • neurotrophin TRKC receptor binding Source: BHF-UCL
  • transmembrane receptor protein tyrosine kinase activator activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

BioCyciZFISH:G66-33432-MONOMER.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP52803.
SIGNORiP52803.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3225. EFNA5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi1946.
OpenTargetsiENSG00000184349.
PharmGKBiPA27660.

Polymorphism and mutation databases

BioMutaiEFNA5.
DMDMi1706678.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000000837721 – 203Ephrin-A5Add BLAST183
PropeptideiPRO_0000008378204 – 228Removed in mature formSequence analysisAdd BLAST25

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi37N-linked (GlcNAc...)1 Publication1
Disulfide bondi62 ↔ 1021 Publication
Disulfide bondi90 ↔ 1511 Publication
Lipidationi203GPI-anchor amidated asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

EPDiP52803.
MaxQBiP52803.
PaxDbiP52803.
PeptideAtlasiP52803.
PRIDEiP52803.

PTM databases

iPTMnetiP52803.
PhosphoSitePlusiP52803.

Expressioni

Gene expression databases

BgeeiENSG00000184349.
CleanExiHS_EFNA5.
ExpressionAtlasiP52803. baseline and differential.
GenevisibleiP52803. HS.

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

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • neurotrophin TRKA receptor binding Source: BHF-UCL
  • neurotrophin TRKB receptor binding Source: BHF-UCL
  • neurotrophin TRKC receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108266. 10 interactors.
DIPiDIP-48296N.
IntActiP52803. 4 interactors.
MINTiMINT-7241704.
STRINGi9606.ENSP00000328777.

Structurei

Secondary structure

1228
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 35Combined sources5
Helixi41 – 43Combined sources3
Beta strandi44 – 46Combined sources3
Beta strandi49 – 52Combined sources4
Beta strandi57 – 61Combined sources5
Helixi71 – 73Combined sources3
Beta strandi76 – 82Combined sources7
Helixi84 – 89Combined sources6
Turni93 – 95Combined sources3
Beta strandi96 – 102Combined sources7
Beta strandi108 – 111Combined sources4
Beta strandi113 – 117Combined sources5
Beta strandi135 – 144Combined sources10
Beta strandi153 – 158Combined sources6
Helixi161 – 164Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52803.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 162Ephrin RBDPROSITE-ProRule annotationAdd BLAST134

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

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52803.
KOiK05462.
OMAiTERYILY.
OrthoDBiEOG091G0IJF.
PhylomeDBiP52803.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR031328. Ephrin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[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

        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)DescriptionActionsGraphical viewLength
Natural variantiVAR_01203555N → K.Corresponds to variant rs469062dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108266. 10 interactors.
DIPiDIP-48296N.
IntActiP52803. 4 interactors.
MINTiMINT-7241704.
STRINGi9606.ENSP00000328777.

PTM databases

iPTMnetiP52803.
PhosphoSitePlusiP52803.

Polymorphism and mutation databases

BioMutaiEFNA5.
DMDMi1706678.

Proteomic databases

EPDiP52803.
MaxQBiP52803.
PaxDbiP52803.
PeptideAtlasiP52803.
PRIDEiP52803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1946.
DisGeNETi1946.
GeneCardsiEFNA5.
HGNCiHGNC:3225. EFNA5.
HPAiCAB013282.
MIMi601535. gene.
neXtProtiNX_P52803.
OpenTargetsiENSG00000184349.
PharmGKBiPA27660.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52803.
KOiK05462.
OMAiTERYILY.
OrthoDBiEOG091G0IJF.
PhylomeDBiP52803.

Enzyme and pathway databases

BioCyciZFISH:G66-33432-MONOMER.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP52803.
SIGNORiP52803.

Miscellaneous databases

ChiTaRSiEFNA5. human.
EvolutionaryTraceiP52803.
GeneWikiiEFNA5.
Ephrin-A5.
GenomeRNAii1946.
PROiP52803.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000184349.
CleanExiHS_EFNA5.
ExpressionAtlasiP52803. baseline and differential.
GenevisibleiP52803. HS.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR031328. Ephrin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.