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Protein

Ephrin-B3

Gene

Efnb3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cell surface transmembrane 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. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons.1 Publication

GO - Molecular functioni

GO - Biological processi

  • adult walking behavior Source: MGI
  • axon choice point recognition Source: MGI
  • axon guidance Source: MGI
  • ephrin receptor signaling pathway Source: MGI
  • negative regulation of axonogenesis Source: ARUK-UCL
  • T cell costimulation Source: MGI

Keywordsi

Molecular functionDevelopmental protein
Biological processDifferentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiR-MMU-2682334 EPH-Ephrin signaling
R-MMU-3928662 EPHB-mediated forward signaling
R-MMU-3928664 Ephrin signaling
R-MMU-3928665 EPH-ephrin mediated repulsion of cells

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-B3
Gene namesi
Name:Efnb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:109196 Efnb3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 227ExtracellularSequence analysisAdd BLAST200
Transmembranei228 – 248HelicalSequence analysisAdd BLAST21
Topological domaini249 – 340CytoplasmicSequence analysisAdd BLAST92

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000000839628 – 340Ephrin-B3Add BLAST313

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi62 ↔ 104PROSITE-ProRule annotation
Disulfide bondi92 ↔ 156PROSITE-ProRule annotation
Glycosylationi210N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei271Omega-N-methylarginineCombined sources1
Modified residuei274PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiO35393
PeptideAtlasiO35393
PRIDEiO35393

PTM databases

iPTMnetiO35393
PhosphoSitePlusiO35393

Expressioni

Tissue specificityi

Expressed on lateral floor plate cells, specifically on commissural axon segments that have passed through the floor plate. Expressed in cells of the retinal ganglion cell layer during retinal axon guidance to the optic disk (PubMed:9484836, PubMed:10704386). Expressed in myogenic progenitor cells (PubMed:27446912).3 Publications

Developmental stagei

Expressed in the floor plate throughout the period of commissural axon pathfinding (PubMed:9484836, PubMed:10704386). In myogenic progenitor cells, highly expressed during early development (E11.5) and progressively repressed as developments proceeds (PubMed:27446912).3 Publications

Gene expression databases

BgeeiENSMUSG00000003934
CleanExiMM_EFNB3
ExpressionAtlasiO35393 baseline and differential
GenevisibleiO35393 MM

Interactioni

Subunit structurei

Interacts with GRIP1 and GRIP2.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
GQ4VCP55EBI-8668154,EBI-15716439From Nipah virus.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199396, 1 interactor
DIPiDIP-44833N
IntActiO35393, 6 interactors
MINTiO35393
STRINGi10090.ENSMUSP00000004036

Structurei

Secondary structure

1340
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 46Combined sources3
Beta strandi57 – 62Combined sources6
Beta strandi80 – 84Combined sources5
Helixi87 – 90Combined sources4
Beta strandi99 – 103Combined sources5
Beta strandi107 – 109Combined sources3
Beta strandi111 – 119Combined sources9
Beta strandi134 – 139Combined sources6
Turni145 – 149Combined sources5
Helixi155 – 158Combined sources4
Beta strandi162 – 166Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3D12X-ray3.00B/E29-169[»]
ProteinModelPortaliO35393
SMRiO35393
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35393

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 167Ephrin RBDPROSITE-ProRule annotationAdd BLAST140

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi338 – 340PDZ-bindingSequence analysis3

Sequence similaritiesi

Belongs to the ephrin family.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3858 Eukaryota
ENOG4111FMJ LUCA
GeneTreeiENSGT00390000005839
HOGENOMiHOG000220931
HOVERGENiHBG051448
InParanoidiO35393
KOiK05463
OMAiSSPSYEF
OrthoDBiEOG091G0BPC
PhylomeDBiO35393

Family and domain databases

CDDicd10426 Ephrin-B_Ectodomain, 1 hit
Gene3Di2.60.40.420, 1 hit
InterProiView protein in InterPro
IPR008972 Cupredoxin
IPR031328 Ephrin
IPR034255 Ephrin-B_Ecto
IPR019765 Ephrin_CS
IPR001799 Ephrin_RBD
PANTHERiPTHR11304 PTHR11304, 1 hit
PfamiView protein in Pfam
PF00812 Ephrin, 1 hit
PRINTSiPR01347 EPHRIN
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002533 Ephrin, 1 hit
SUPFAMiSSF49503 SSF49503, 1 hit
PROSITEiView protein in PROSITE
PS01299 EPHRIN_RBD_1, 1 hit
PS51551 EPHRIN_RBD_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35393-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAPHFGPGG VQVGALLLLG FAGLVSGLSL EPVYWNSANK RFQAEGGYVL
60 70 80 90 100
YPQIGDRLDL LCPRARPPGP HSSPSYEFYK LYLVEGAQGR RCEAPPAPNL
110 120 130 140 150
LLTCDRPDLD LRFTIKFQEY SPNLWGHEFR SHHDYYIIAT SDGTREGLES
160 170 180 190 200
LQGGVCLTRG MKVLLRVGQS PRGGAVPRKP VSEMPMERDR GAAHSAEPGR
210 220 230 240 250
DTIPGDPSSN ATSRGAEGPL PPPSMPAVAG AAGGMALLLL GVAGAGGAMC
260 270 280 290 300
WRRRRAKPSE SRHPGPGSFG RGGSLGLGGG GGMGPREAEP GELGIALRGG
310 320 330 340
GTADPPFCPH YEKVSGDYGH PVYIVQDGPP QSPPNIYYKV
Length:340
Mass (Da):35,885
Last modified:January 1, 1998 - v1
Checksum:i52F3D58FD209A6B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025288 mRNA Translation: AAC53537.1
BC052001 mRNA Translation: AAH52001.1
BC058617 mRNA Translation: AAH58617.1
CCDSiCCDS24896.1
RefSeqiNP_031937.1, NM_007911.5
UniGeneiMm.249637

Genome annotation databases

EnsembliENSMUST00000004036; ENSMUSP00000004036; ENSMUSG00000003934
GeneIDi13643
KEGGimmu:13643
UCSCiuc007jqi.2 mouse

Similar proteinsi

Entry informationi

Entry nameiEFNB3_MOUSE
AccessioniPrimary (citable) accession number: O35393
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: April 25, 2018
This is version 142 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health