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O35393

- EFNB3_MOUSE

UniProt

O35393 - EFNB3_MOUSE

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Protein

Ephrin-B3

Gene

Efnb3

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. ephrin receptor binding Source: RefGenome

GO - Biological processi

  1. adult walking behavior Source: MGI
  2. axon choice point recognition Source: MGI
  3. axon guidance Source: MGI
  4. ephrin receptor signaling pathway Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-B3
Gene namesi
Name:Efnb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:109196. Efnb3.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 340313Ephrin-B3PRO_0000008396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi62 ↔ 104PROSITE-ProRule annotation
Disulfide bondi92 ↔ 156PROSITE-ProRule annotation
Glycosylationi210 – 2101N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO35393.
PaxDbiO35393.
PRIDEiO35393.

PTM databases

PhosphoSiteiO35393.

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

BgeeiO35393.
CleanExiMM_EFNB3.
ExpressionAtlasiO35393. baseline and differential.
GenevestigatoriO35393.

Interactioni

Subunit structurei

Interacts with GRIP1 and GRIP2.By similarity

Protein-protein interaction databases

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

Structurei

Secondary structure

1
340
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 463
Beta strandi57 – 626
Beta strandi80 – 845
Helixi87 – 904
Beta strandi99 – 1035
Beta strandi107 – 1093
Beta strandi111 – 1199
Beta strandi134 – 1396
Turni145 – 1495
Helixi155 – 1584
Beta strandi162 – 1665

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D12X-ray3.00B/E29-169[»]
ProteinModelPortaliO35393.
SMRiO35393. Positions 29-169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35393.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 227200ExtracellularSequence AnalysisAdd
BLAST
Topological domaini249 – 34092CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei228 – 24821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 167140Ephrin RBDPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi338 – 3403PDZ-bindingSequence Analysis

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

eggNOGiNOG268537.
HOGENOMiHOG000220931.
HOVERGENiHBG051448.
InParanoidiO35393.
KOiK05463.
OMAiPGKENMP.
OrthoDBiEOG7288S5.
PhylomeDBiO35393.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF025288 mRNA. Translation: AAC53537.1 .
BC052001 mRNA. Translation: AAH52001.1 .
BC058617 mRNA. Translation: AAH58617.1 .
CCDSi CCDS24896.1.
RefSeqi NP_031937.1. NM_007911.5.
UniGenei Mm.249637.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3D12 X-ray 3.00 B/E 29-169 [» ]
ProteinModelPortali O35393.
SMRi O35393. Positions 29-169.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-44833N.
IntActi O35393. 3 interactions.
MINTi MINT-1793420.
STRINGi 10090.ENSMUSP00000004036.

PTM databases

PhosphoSitei O35393.

Proteomic databases

MaxQBi O35393.
PaxDbi O35393.
PRIDEi O35393.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004036 ; ENSMUSP00000004036 ; ENSMUSG00000003934 .
GeneIDi 13643.
KEGGi mmu:13643.
UCSCi uc007jqi.2. mouse.

Organism-specific databases

CTDi 1949.
MGIi MGI:109196. Efnb3.

Phylogenomic databases

eggNOGi NOG268537.
HOGENOMi HOG000220931.
HOVERGENi HBG051448.
InParanoidi O35393.
KOi K05463.
OMAi PGKENMP.
OrthoDBi EOG7288S5.
PhylomeDBi O35393.

Miscellaneous databases

EvolutionaryTracei O35393.
NextBioi 284350.
PROi O35393.
SOURCEi Search...

Gene expression databases

Bgeei O35393.
CleanExi MM_EFNB3.
ExpressionAtlasi O35393. baseline and differential.
Genevestigatori O35393.

Family and domain databases

Gene3Di 2.60.40.420. 1 hit.
InterProi IPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view ]
PANTHERi PTHR11304. PTHR11304. 1 hit.
Pfami PF00812. Ephrin. 1 hit.
[Graphical view ]
PRINTSi PR01347. EPHRIN.
ProDomi PD002533. Ephrin. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF49503. SSF49503. 1 hit.
PROSITEi PS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube."
    Bergemann A.D., Zhang L., Chiang M.-K., Brambilla R., Klein R., Flanagan J.G.
    Oncogene 16:471-480(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  3. "Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons."
    Imondi R., Wideman C., Kaprielian Z.
    Development 127:1397-1410(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210.

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: October 29, 2014
This is version 112 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

External Data

Dasty 3