Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ephrin-A5

Gene

Efna5

Organism
Mus musculus (Mouse)
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.4 Publications

GO - Molecular functioni

  • chemorepellent activity Source: MGI
  • ephrin receptor binding Source: UniProtKB
  • neurotrophin TRKB receptor binding Source: BHF-UCL

GO - Biological processi

  • axon guidance Source: MGI
  • cellular response to follicle-stimulating hormone stimulus Source: MGI
  • cellular response to forskolin Source: MGI
  • collateral sprouting Source: BHF-UCL
  • ephrin receptor signaling pathway Source: UniProtKB
  • negative regulation of substrate adhesion-dependent cell spreading Source: MGI
  • positive regulation of collateral sprouting Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of synapse assembly Source: BHF-UCL
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of cell-cell adhesion Source: UniProtKB
  • regulation of cell morphogenesis Source: MGI
  • regulation of focal adhesion assembly Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
  • regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • regulation of microtubule cytoskeleton organization Source: UniProtKB
  • retinal ganglion cell axon guidance Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiR-MMU-2682334. EPH-Ephrin signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.

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:Epl7, Eplg7, Lerk7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:107444. Efna5.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: MGI
  • anchored component of external side of plasma membrane Source: UniProtKB
  • anchored component of plasma membrane Source: GO_Central
  • basement membrane Source: MGI
  • caveola Source: UniProtKB-SubCell
  • cell periphery Source: MGI
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice display cataract an opacification of the lens.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000000837921 – 203Ephrin-A5Add BLAST183
PropeptideiPRO_0000008380204 – 228Removed in mature formSequence analysisAdd BLAST25

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi37N-linked (GlcNAc...)1 Publication1
Disulfide bondi62 ↔ 102PROSITE-ProRule annotation1 Publication
Disulfide bondi90 ↔ 151PROSITE-ProRule annotation1 Publication
Glycosylationi162N-linked (GlcNAc...); atypical1 Publication1
Lipidationi203GPI-anchor amidated asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiO08543.
PRIDEiO08543.

PTM databases

PhosphoSitePlusiO08543.

Expressioni

Gene expression databases

BgeeiENSMUSG00000048915.
CleanExiMM_EFNA5.
GenevisibleiO08543. MM.

Interactioni

Subunit structurei

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 similarity). Binds to EPHB2. Interacts with EPHA8; activates EPHA8.By similarity2 Publications

GO - Molecular functioni

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

Protein-protein interaction databases

IntActiO08543. 2 interactors.
STRINGi10090.ENSMUSP00000076115.

Structurei

Secondary structure

1228
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 35Combined sources6
Helixi41 – 44Combined sources4
Beta strandi49 – 52Combined sources4
Beta strandi57 – 61Combined sources5
Beta strandi67 – 69Combined sources3
Beta strandi71 – 73Combined sources3
Beta strandi77 – 82Combined sources6
Helixi84 – 88Combined sources5
Beta strandi92 – 102Combined sources11
Beta strandi108 – 111Combined sources4
Beta strandi113 – 117Combined sources5
Beta strandi134 – 144Combined sources11
Beta strandi148 – 150Combined sources3
Beta strandi153 – 158Combined sources6
Turni161 – 164Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SHWX-ray2.20A28-164[»]
1SHXX-ray2.10A/B28-164[»]
ProteinModelPortaliO08543.
SMRiO08543.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08543.

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.
InParanoidiO08543.
KOiK05462.
OMAiTERYILY.
OrthoDBiEOG091G0IJF.
PhylomeDBiO08543.

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]

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. AlignAdd to basket

Isoform Long (identifier: O08543-1) [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

        10         20         30         40         50
MLHVEMLTLL FLVLWMCVFS QDPGSKVVAD 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):26,339
Last modified:July 1, 1997 - v1
Checksum:i85439F5337420022
GO
Isoform Short (identifier: O08543-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     163-189: Missing.

Show »
Length:201
Mass (Da):23,338
Checksum:iC5F5E78FD6674316
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001449163 – 189Missing in isoform Short. 1 PublicationAdd BLAST27

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90664 mRNA. Translation: AAB50239.1.
U90665 mRNA. Translation: AAB50240.1.
BC040218 mRNA. Translation: AAH40218.1.
CCDSiCCDS28934.1. [O08543-2]
CCDS28935.1. [O08543-1]
RefSeqiNP_034239.1. NM_010109.3. [O08543-2]
NP_997537.1. NM_207654.2. [O08543-1]
UniGeneiMm.401670.
Mm.7978.

Genome annotation databases

EnsembliENSMUST00000076840; ENSMUSP00000076115; ENSMUSG00000048915. [O08543-1]
ENSMUST00000078839; ENSMUSP00000077883; ENSMUSG00000048915. [O08543-2]
GeneIDi13640.
KEGGimmu:13640.
UCSCiuc008dfg.2. mouse. [O08543-1]
uc008dfh.2. mouse. [O08543-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90664 mRNA. Translation: AAB50239.1.
U90665 mRNA. Translation: AAB50240.1.
BC040218 mRNA. Translation: AAH40218.1.
CCDSiCCDS28934.1. [O08543-2]
CCDS28935.1. [O08543-1]
RefSeqiNP_034239.1. NM_010109.3. [O08543-2]
NP_997537.1. NM_207654.2. [O08543-1]
UniGeneiMm.401670.
Mm.7978.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SHWX-ray2.20A28-164[»]
1SHXX-ray2.10A/B28-164[»]
ProteinModelPortaliO08543.
SMRiO08543.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08543. 2 interactors.
STRINGi10090.ENSMUSP00000076115.

PTM databases

PhosphoSitePlusiO08543.

Proteomic databases

PaxDbiO08543.
PRIDEiO08543.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000076840; ENSMUSP00000076115; ENSMUSG00000048915. [O08543-1]
ENSMUST00000078839; ENSMUSP00000077883; ENSMUSG00000048915. [O08543-2]
GeneIDi13640.
KEGGimmu:13640.
UCSCiuc008dfg.2. mouse. [O08543-1]
uc008dfh.2. mouse. [O08543-2]

Organism-specific databases

CTDi1946.
MGIiMGI:107444. Efna5.

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiO08543.
KOiK05462.
OMAiTERYILY.
OrthoDBiEOG091G0IJF.
PhylomeDBiO08543.

Enzyme and pathway databases

ReactomeiR-MMU-2682334. EPH-Ephrin signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

ChiTaRSiEfna5. mouse.
EvolutionaryTraceiO08543.
PROiO08543.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000048915.
CleanExiMM_EFNA5.
GenevisibleiO08543. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: O08543
Secondary accession number(s): O08544
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.