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P97605 (EFNA5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin-A5
Alternative name(s):
AL-1
EPH-related receptor tyrosine kinase ligand 7
Short name=LERK-7
Gene names
Name:Efna5
Synonyms:Eplg7, Lerk7
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Subunit structure

Binds to the receptor tyrosine kinases EPHA2, EPHA3, EPHB1 and EPHB2. Interacts with EPHA8; activates EPHA8. 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.

Subcellular location

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

Tissue specificity

Expressed in brain, heart, placenta and lung.

Sequence similarities

Belongs to the ephrin family.

Contains 1 ephrin RBD (ephrin receptor-binding) domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from Biological aspect of Ancestor. Source: RefGenome

axonal fasciculation

Non-traceable author statement Ref.1. Source: RGD

brain development

Inferred from mutant phenotype Ref.1. Source: RGD

central nervous system development

Non-traceable author statement Ref.1. Source: RGD

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Rac GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Rho GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of microtubule cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentanchored component of external side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

anchored component of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

caveola

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionephrin receptor binding

Inferred from physical interaction PubMed 20824214. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 203183Ephrin-A5
PRO_0000008381
Propeptide204 – 22825Removed in mature form Potential
PRO_0000008382

Regions

Domain29 – 162134Ephrin RBD

Amino acid modifications

Lipidation2031GPI-anchor amidated asparagine Potential
Glycosylation371N-linked (GlcNAc...) Potential
Disulfide bond62 ↔ 102 By similarity
Disulfide bond90 ↔ 151 By similarity

Sequences

Sequence LengthMass (Da)Tools
P97605 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 855985532D580022

FASTA22826,358
        10         20         30         40         50         60 
MLHVEMLTLL FLVLWMCVFS QDPGSKVVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV 

        70         80         90        100        110        120 
FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL 

       130        140        150        160        170        180 
FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV RDRVFDVNDK 

       190        200        210        220 
VENSLEPADD TVHESAEPSR GENAAQTPRI PSRLLAILLF LLAMLLTL 

« Hide

References

[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], PARTIAL PROTEIN SEQUENCE.
Strain: Sprague-Dawley.
[2]"rLERK7, rat ligand for Eph-related receptor tyrosine kinase."
Li Y.Y., McTiernan C.F., Feldman A.M.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U69279 mRNA. Translation: AAC05801.1.
RefSeqNP_446355.1. NM_053903.1.
UniGeneRn.10714.

3D structure databases

ProteinModelPortalP97605.
SMRP97605. Positions 28-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000039406.

Proteomic databases

PRIDEP97605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID116683.
KEGGrno:116683.
UCSCRGD:620391. rat.

Organism-specific databases

CTD1946.
RGD620391. Efna5.

Phylogenomic databases

eggNOGNOG241965.
HOGENOMHOG000234373.
HOVERGENHBG051447.
InParanoidP97605.
KOK05462.
PhylomeDBP97605.

Gene expression databases

GenevestigatorP97605.

Family and domain databases

Gene3D2.60.40.420. 1 hit.
InterProIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view]
PANTHERPTHR11304. PTHR11304. 1 hit.
PfamPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSPR01347. EPHRIN.
ProDomPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF49503. SSF49503. 1 hit.
PROSITEPS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio619532.
PROP97605.

Entry information

Entry nameEFNA5_RAT
AccessionPrimary (citable) accession number: P97605
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families