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Protein

Ephrin-B3

Gene

Efnb3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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
  • T cell costimulation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:109196. Efnb3.

Subcellular locationi

Topology

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

GO - Cellular componenti

Complete GO annotation...

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...)1 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.

Developmental stagei

Expressed in the floor plate throughout the period of commissural axon pathfinding.

Gene expression databases

BgeeiENSMUSG00000003934.
CleanExiMM_EFNB3.
ExpressionAtlasiO35393. baseline and differential.
GenevisibleiO35393. MM.

Interactioni

Subunit structurei

Interacts with GRIP1 and GRIP2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-44833N.
IntActiO35393. 3 interactors.
MINTiMINT-1793420.
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
Contains 1 ephrin RBD (ephrin receptor-binding) domain.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

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.

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

DIPiDIP-44833N.
IntActiO35393. 3 interactors.
MINTiMINT-1793420.
STRINGi10090.ENSMUSP00000004036.

PTM databases

iPTMnetiO35393.
PhosphoSitePlusiO35393.

Proteomic databases

PaxDbiO35393.
PeptideAtlasiO35393.
PRIDEiO35393.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1949.
MGIiMGI:109196. Efnb3.

Phylogenomic databases

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

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.

Miscellaneous databases

EvolutionaryTraceiO35393.
PROiO35393.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000003934.
CleanExiMM_EFNB3.
ExpressionAtlasiO35393. baseline and differential.
GenevisibleiO35393. 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 nameiEFNB3_MOUSE
AccessioniPrimary (citable) accession number: O35393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 132 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.