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-A4

Gene

Efna4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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. May play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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-A4
Alternative name(s):
EPH-related receptor tyrosine kinase ligand 4
Short name:
LERK-4
Gene namesi
Name:Efna4
Synonyms:Epl4, Eplg4, Lerk4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:106643. Efna4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000000837526 – 175Ephrin-A4Add BLAST150
PropeptideiPRO_0000008376176 – 206Removed in mature formSequence analysisAdd BLAST31

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi33N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi58 ↔ 99PROSITE-ProRule annotation
Disulfide bondi86 ↔ 147PROSITE-ProRule annotation
Glycosylationi98N-linked (GlcNAc...)Sequence analysis1
Lipidationi175GPI-anchor amidated serineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiO08542.
PRIDEiO08542.

PTM databases

PhosphoSitePlusiO08542.

Expressioni

Gene expression databases

BgeeiENSMUSG00000028040.
CleanExiMM_EFNA4.
ExpressionAtlasiO08542. baseline and differential.
GenevisibleiO08542. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiO08542. 2 interactors.
MINTiMINT-7013357.
STRINGi10090.ENSMUSP00000029674.

Structurei

3D structure databases

ProteinModelPortaliO08542.
SMRiO08542.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 158Ephrin RBDPROSITE-ProRule annotationAdd BLAST133

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi41 – 43Cell attachment siteSequence analysis3

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.
InParanoidiO08542.
KOiK05462.
OMAiCCKESKS.
OrthoDBiEOG091G0K52.
PhylomeDBiO08542.

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.

O08542-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLPLLRTV LWAALLGSRL PGCSSLRHPI YWNSSNPRLL RGDAVVELGF
60 70 80 90 100
NDYLDIFCPH YESPGPPEGP ETFALYMVDW SGYEACTAEG ANAFQRWNCS
110 120 130 140 150
MPFAPFSPVR FSEKIQRYTP FPLGFEFLPG ETYYYISVPT PESPGRCLRL
160 170 180 190 200
QVSVCCKESG SSHESAHPVG SPGESGTSGW RGGHAPSPLC LLLLLLLPIL

RLLRVL
Length:206
Mass (Da):22,861
Last modified:July 15, 1999 - v2
Checksum:i43501971DD1C6EA5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 4MRLL → MLLRLGLIYPPTRPPAPPGP LV (PubMed:8903354).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90663 mRNA. Translation: AAB50238.1.
U92890, U92889 Genomic DNA. Translation: AAC39962.1.
CCDSiCCDS38489.1.
RefSeqiNP_031936.2. NM_007910.2.
UniGeneiMm.16332.

Genome annotation databases

EnsembliENSMUST00000029674; ENSMUSP00000029674; ENSMUSG00000028040.
GeneIDi13639.
KEGGimmu:13639.
UCSCiuc008pys.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90663 mRNA. Translation: AAB50238.1.
U92890, U92889 Genomic DNA. Translation: AAC39962.1.
CCDSiCCDS38489.1.
RefSeqiNP_031936.2. NM_007910.2.
UniGeneiMm.16332.

3D structure databases

ProteinModelPortaliO08542.
SMRiO08542.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08542. 2 interactors.
MINTiMINT-7013357.
STRINGi10090.ENSMUSP00000029674.

PTM databases

PhosphoSitePlusiO08542.

Proteomic databases

PaxDbiO08542.
PRIDEiO08542.

Protocols and materials databases

DNASUi13639.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029674; ENSMUSP00000029674; ENSMUSG00000028040.
GeneIDi13639.
KEGGimmu:13639.
UCSCiuc008pys.1. mouse.

Organism-specific databases

CTDi1945.
MGIiMGI:106643. Efna4.

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiO08542.
KOiK05462.
OMAiCCKESKS.
OrthoDBiEOG091G0K52.
PhylomeDBiO08542.

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

PROiO08542.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028040.
CleanExiMM_EFNA4.
ExpressionAtlasiO08542. baseline and differential.
GenevisibleiO08542. 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 nameiEFNA4_MOUSE
AccessioniPrimary (citable) accession number: O08542
Secondary accession number(s): O55218
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: November 2, 2016
This is version 123 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. 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.