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Protein

Ephrin-A1

Gene

Efna1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

GO - Molecular functioni

  • ephrin receptor binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Angiogenesis

Enzyme and pathway databases

ReactomeiR-RNO-2682334. EPH-Ephrin signaling.
R-RNO-3928663. EPHA-mediated growth cone collapse.
R-RNO-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, Lerk1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi620388. Efna1.

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 182165Ephrin-A1PRO_0000008357Add
BLAST
Chaini18 – ?Ephrin-A1, secreted formPRO_0000389633
Propeptidei183 – 20523Removed in mature formSequence analysisPRO_0000008358Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi26 – 261N-linked (GlcNAc...)Sequence analysis
Disulfide bondi51 ↔ 92PROSITE-ProRule annotation
Disulfide bondi80 ↔ 140PROSITE-ProRule annotation
Lipidationi182 – 1821GPI-anchor amidated serineSequence analysis

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

PaxDbiP97553.

Expressioni

Gene expression databases

BgeeiENSRNOG00000020573.
GenevisibleiP97553. RN.

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

GO - Molecular functioni

  • ephrin receptor binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027920.

Structurei

3D structure databases

ProteinModelPortaliP97553.
SMRiP97553. Positions 18-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 151134Ephrin RBDPROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiP97553.
KOiK05462.
OMAiEQYQLCQ.
OrthoDBiEOG091G0K52.
PhylomeDBiP97553.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[Graphical view]
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.

P97553-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFLWAPLLG LCCSLAAADR HIVFWNSSNP KFREEDYTVH VQLNDYLDII
60 70 80 90 100
CPHYEDDSVA DAAMERYTLY MVEHQEYVTC EPQSKDQVRW KCNQPSAKHG
110 120 130 140 150
PEKLSEKFQR FTPFTLGKEF KEGHSYYYIS KPIYHQETQC LKLKVTVNGK
160 170 180 190 200
ITHSPHAHAN PQEKRLQADD PEVQVLHSIG HSAAPRLFPL VWAVLLLPLL

LLQTQ
Length:205
Mass (Da):23,763
Last modified:August 30, 2005 - v2
Checksum:iE9ED3F73AE7FC4CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181A → V in BAA07242 (PubMed:7675446).Curated
Sequence conflicti68 – 681T → S in BAA07242 (PubMed:7675446).Curated
Sequence conflicti90 – 901W → V in BAA07242 (PubMed:7675446).Curated
Sequence conflicti159 – 1591A → V in BAA07242 (PubMed:7675446).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38056 mRNA. Translation: BAA07242.1.
BC070514 mRNA. Translation: AAH70514.1.
RefSeqiNP_446051.2. NM_053599.2.
UniGeneiRn.8427.

Genome annotation databases

EnsembliENSRNOT00000027920; ENSRNOP00000027920; ENSRNOG00000020573.
GeneIDi94268.
KEGGirno:94268.
UCSCiRGD:620388. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38056 mRNA. Translation: BAA07242.1.
BC070514 mRNA. Translation: AAH70514.1.
RefSeqiNP_446051.2. NM_053599.2.
UniGeneiRn.8427.

3D structure databases

ProteinModelPortaliP97553.
SMRiP97553. Positions 18-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027920.

Proteomic databases

PaxDbiP97553.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027920; ENSRNOP00000027920; ENSRNOG00000020573.
GeneIDi94268.
KEGGirno:94268.
UCSCiRGD:620388. rat.

Organism-specific databases

CTDi1942.
RGDi620388. Efna1.

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP97553.
KOiK05462.
OMAiEQYQLCQ.
OrthoDBiEOG091G0K52.
PhylomeDBiP97553.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP97553.

Gene expression databases

BgeeiENSRNOG00000020573.
GenevisibleiP97553. RN.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[Graphical view]
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_RAT
AccessioniPrimary (citable) accession number: P97553
Secondary accession number(s): Q6NS29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 30, 2005
Last modified: September 7, 2016
This is version 116 of the entry and version 2 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. 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.