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Protein

Ephrin-A1

Gene

Efna1

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. 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.3 Publications

GO - Molecular functioni

GO - Biological processi

  • activation of MAPK activity Source: MGI
  • angiogenesis Source: UniProtKB-KW
  • aortic valve morphogenesis Source: BHF-UCL
  • axon guidance Source: GO_Central
  • cell migration Source: MGI
  • endocardial cushion to mesenchymal transition involved in heart valve formation Source: BHF-UCL
  • ephrin receptor signaling pathway Source: UniProtKB
  • MAPK cascade Source: MGI
  • mitral valve morphogenesis Source: BHF-UCL
  • negative regulation of dendritic spine morphogenesis Source: UniProtKB
  • negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
  • negative regulation of thymocyte apoptotic process Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • neuron differentiation Source: MGI
  • notochord formation Source: MGI
  • positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • regulation of angiogenesis Source: UniProtKB
  • regulation of axonogenesis Source: MGI
  • regulation of blood vessel endothelial cell migration Source: UniProtKB
  • regulation of cell adhesion mediated by integrin Source: MGI
  • regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  • substrate adhesion-dependent cell spreading Source: MGI
Complete GO annotation...

Keywords - Biological processi

Angiogenesis

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-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:
Gene namesi
Name:Efna1
Synonyms:Epgl1, Epl1, Lerk1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:103236. Efna1.

Subcellular locationi

  • Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity
Ephrin-A1, secreted form :
  • Secreted By similarity

GO - Cellular componenti

  • anchored component of plasma membrane Source: UniProtKB
  • extracellular exosome Source: MGI
  • intracellular Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000000835518 – 182Ephrin-A1Add BLAST165
ChainiPRO_000038963118 – ?Ephrin-A1, secreted form
PropeptideiPRO_0000008356183 – 205Removed in mature formSequence analysisAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi26N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi51 ↔ 92PROSITE-ProRule annotation
Disulfide bondi80 ↔ 140PROSITE-ProRule annotation
Lipidationi182GPI-anchor amidated serineSequence analysis1

Post-translational modificationi

Undergoes proteolysis by a metalloprotease to give rise to a soluble monomeric form.By similarity
N-Glycosylation is required for binding to EPHA2 receptor and inducing its internalization.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP52793.
PaxDbiP52793.
PRIDEiP52793.

PTM databases

iPTMnetiP52793.
PhosphoSitePlusiP52793.

Expressioni

Gene expression databases

BgeeiENSMUSG00000027954.
CleanExiMM_EFNA1.
ExpressionAtlasiP52793. baseline and differential.
GenevisibleiP52793. MM.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
EPHA7Q153752EBI-5241529,EBI-1383428From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199389. 3 interactors.
IntActiP52793. 1 interactor.
STRINGi10090.ENSMUSP00000029566.

Structurei

3D structure databases

ProteinModelPortaliP52793.
SMRiP52793.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 161Ephrin RBDPROSITE-ProRule annotationAdd BLAST144

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.
InParanoidiP52793.
KOiK05462.
OMAiEQYQLCQ.
OrthoDBiEOG091G0K52.
PhylomeDBiP52793.

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.

P52793-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFLWAPLLG LCCSLAAADR HIVFWNSSNP KFREEDYTVH VQLNDYLDII
60 70 80 90 100
CPHYEDDSVA DAAMERYTLY MVEHQEYVAC QPQSKDQVRW NCNRPSAKHG
110 120 130 140 150
PEKLSEKFQR FTPFILGKEF KEGHSYYYIS KPIYHQESQC LKLKVTVNGK
160 170 180 190 200
ITHNPQAHVN PQEKRLQADD PEVQVLHSIG YSAAPRLFPL VWAVLLLPLL

LLQSQ
Length:205
Mass (Da):23,802
Last modified:October 1, 1996 - v1
Checksum:i5A8F3A6E2091E868
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74H → Y in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti79A → T in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti81Q → E in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti91N → K in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti94R → Q in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti112T → S in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti115I → T in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti138S → T in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti154N → S in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti156Q → H in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti159V → A in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti181Y → H in BAA07344 (PubMed:7675446).Curated1
Sequence conflicti204S → T in BAA07344 (PubMed:7675446).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38146 mRNA. Translation: BAA07344.1.
U26188 mRNA. Translation: AAA67563.1.
U90662 mRNA. Translation: AAB50237.1.
BC002046 mRNA. Translation: AAH02046.1.
CCDSiCCDS17501.1.
RefSeqiNP_034237.3. NM_010107.4.
UniGeneiMm.15675.

Genome annotation databases

EnsembliENSMUST00000029566; ENSMUSP00000029566; ENSMUSG00000027954.
GeneIDi13636.
KEGGimmu:13636.
UCSCiuc008pyo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38146 mRNA. Translation: BAA07344.1.
U26188 mRNA. Translation: AAA67563.1.
U90662 mRNA. Translation: AAB50237.1.
BC002046 mRNA. Translation: AAH02046.1.
CCDSiCCDS17501.1.
RefSeqiNP_034237.3. NM_010107.4.
UniGeneiMm.15675.

3D structure databases

ProteinModelPortaliP52793.
SMRiP52793.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199389. 3 interactors.
IntActiP52793. 1 interactor.
STRINGi10090.ENSMUSP00000029566.

PTM databases

iPTMnetiP52793.
PhosphoSitePlusiP52793.

Proteomic databases

MaxQBiP52793.
PaxDbiP52793.
PRIDEiP52793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029566; ENSMUSP00000029566; ENSMUSG00000027954.
GeneIDi13636.
KEGGimmu:13636.
UCSCiuc008pyo.2. mouse.

Organism-specific databases

CTDi1942.
MGIiMGI:103236. Efna1.

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52793.
KOiK05462.
OMAiEQYQLCQ.
OrthoDBiEOG091G0K52.
PhylomeDBiP52793.

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

PROiP52793.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027954.
CleanExiMM_EFNA1.
ExpressionAtlasiP52793. baseline and differential.
GenevisibleiP52793. 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 nameiEFNA1_MOUSE
AccessioniPrimary (citable) accession number: P52793
Secondary accession number(s): P97331
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 131 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.