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P97553 (EFNA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. 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-A1
Alternative name(s):
EPH-related receptor tyrosine kinase ligand 1
Short name=LERK-1
Immediate early response protein B61

Cleaved into the following chain:

  1. Ephrin-A1, secreted form
Gene names
Name:Efna1
Synonyms:Epgl1, Lerk1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis By similarity.

Subunit structure

Monomer. Homodimer. Forms heterodimers with EPHA2. Binds to the receptor tyrosine kinases EPHA2, EPHA3, EPHA4, EPHA5, EPHA6 and EPHA7. Also binds with low affinity to EPHA1 By similarity.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor By similarity.

Ephrin-A1, secreted form: Secreted By similarity.

Post-translational modification

Undergoes proteolysis by a metalloprotease to give rise to a soluble monomeric form By similarity.

Sequence similarities

Belongs to the ephrin family.

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

Ontologies

Keywords
   Biological processAngiogenesis
   Cellular componentCell membrane
Membrane
Secreted
   DiseaseTumor suppressor
   DomainSignal
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Non-traceable author statement PubMed 12615978. Source: RGD

aortic valve morphogenesis

Inferred from electronic annotation. Source: Ensembl

axon guidance

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell migration

Inferred from electronic annotation. Source: Ensembl

endocardial cushion to mesenchymal transition involved in heart valve formation

Inferred from electronic annotation. Source: Ensembl

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

mitral valve morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

notochord formation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

regulation of peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

substrate adhesion-dependent cell spreading

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentanchored component of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionephrin receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 182165Ephrin-A1
PRO_0000008357
Chain18 – ?Ephrin-A1, secreted formPRO_0000389633
Propeptide183 – 20523Removed in mature form Potential
PRO_0000008358

Regions

Domain18 – 151134Ephrin RBD

Amino acid modifications

Lipidation1821GPI-anchor amidated serine Potential
Glycosylation261N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 92 By similarity
Disulfide bond80 ↔ 140 By similarity

Experimental info

Sequence conflict181A → V in BAA07242. Ref.1
Sequence conflict681T → S in BAA07242. Ref.1
Sequence conflict901W → V in BAA07242. Ref.1
Sequence conflict1591A → V in BAA07242. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P97553 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: E9ED3F73AE7FC4CA

FASTA20523,763
        10         20         30         40         50         60 
MEFLWAPLLG LCCSLAAADR HIVFWNSSNP KFREEDYTVH VQLNDYLDII CPHYEDDSVA 

        70         80         90        100        110        120 
DAAMERYTLY MVEHQEYVTC EPQSKDQVRW KCNQPSAKHG PEKLSEKFQR FTPFTLGKEF 

       130        140        150        160        170        180 
KEGHSYYYIS KPIYHQETQC LKLKVTVNGK ITHSPHAHAN PQEKRLQADD PEVQVLHSIG 

       190        200 
HSAAPRLFPL VWAVLLLPLL LLQTQ 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of rat and mouse B61 gene: implications on organogenesis."
Takahashi H., Ikeda T.
Oncogene 11:879-883(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain.
[2]"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: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38056 mRNA. Translation: BAA07242.1.
BC070514 mRNA. Translation: AAH70514.1.
RefSeqNP_446051.2. NM_053599.2.
UniGeneRn.8427.

3D structure databases

ProteinModelPortalP97553.
SMRP97553. Positions 18-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000027920.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027920; ENSRNOP00000027920; ENSRNOG00000020573.
GeneID94268.
KEGGrno:94268.
UCSCRGD:620388. rat.

Organism-specific databases

CTD1942.
RGD620388. Efna1.

Phylogenomic databases

eggNOGNOG296825.
GeneTreeENSGT00390000015107.
HOGENOMHOG000234373.
HOVERGENHBG051447.
InParanoidP97553.
KOK05462.
OMAPIHHQED.
OrthoDBEOG70W3FD.
PhylomeDBP97553.

Gene expression databases

GenevestigatorP97553.

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

NextBio617895.
PROP97553.

Entry information

Entry nameEFNA1_RAT
AccessionPrimary (citable) accession number: P97553
Secondary accession number(s): Q6NS29
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 98 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