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Protein

Ephrin-A3

Gene

EFNA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. 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 (By similarity).By similarity

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • transmembrane-ephrin receptor activity Source: ProtInc

GO - Biological processi

  • axon guidance Source: GO_Central
  • cell-cell signaling Source: ProtInc
  • ephrin receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143590-MONOMER.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP52797.
SIGNORiP52797.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-A3
Alternative name(s):
EFL-2
EHK1 ligand
Short name:
EHK1-L
EPH-related receptor tyrosine kinase ligand 3
Short name:
LERK-3
Gene namesi
Name:EFNA3
Synonyms:EFL2, EPLG3, LERK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3223. EFNA3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi1944.
OpenTargetsiENSG00000143590.
PharmGKBiPA27658.

Polymorphism and mutation databases

BioMutaiEFNA3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000000836923 – 214Ephrin-A3Add BLAST192
PropeptideiPRO_0000008370215 – 238Removed in mature formSequence analysisAdd BLAST24

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi38N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi63 ↔ 110PROSITE-ProRule annotation
Glycosylationi67N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi99 ↔ 158PROSITE-ProRule annotation
Glycosylationi100N-linked (GlcNAc...)Sequence analysis1
Lipidationi214GPI-anchor amidated glycineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

EPDiP52797.
PaxDbiP52797.
PeptideAtlasiP52797.
PRIDEiP52797.

PTM databases

PhosphoSitePlusiP52797.

Expressioni

Tissue specificityi

Expressed in brain, skeletal muscle, spleen, thymus, prostate, testis, ovary, small intestine, and peripheral blood leukocytes.

Gene expression databases

BgeeiENSG00000143590.
CleanExiHS_EFNA3.
GenevisibleiP52797. HS.

Organism-specific databases

HPAiCAB010494.

Interactioni

Subunit structurei

Interacts with EPHA8; activates EPHA8.

Binary interactionsi

WithEntry#Exp.IntActNotes
MEOX2A4D1273EBI-722730,EBI-10172134
NOTCH2NLQ7Z3S93EBI-722730,EBI-945833

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108264. 6 interactors.
IntActiP52797. 4 interactors.
MINTiMINT-1378559.
STRINGi9606.ENSP00000357393.

Structurei

3D structure databases

ProteinModelPortaliP52797.
SMRiP52797.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 169Ephrin RBDPROSITE-ProRule annotationAdd BLAST140

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.
InParanoidiP52797.
KOiK05462.
OMAiQGSKRWE.
OrthoDBiEOG091G0XCP.
PhylomeDBiP52797.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P52797-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAPLLLLL LLVPVPLLPL LAQGPGGALG NRHAVYWNSS NQHLRREGYT
60 70 80 90 100
VQVNVNDYLD IYCPHYNSSG VGPGAGPGPG GGAEQYVLYM VSRNGYRTCN
110 120 130 140 150
ASQGFKRWEC NRPHAPHSPI KFSEKFQRYS AFSLGYEFHA GHEYYYISTP
160 170 180 190 200
THNLHWKCLR MKVFVCCAST SHSGEKPVPT LPQFTMGPNV KINVLEDFEG
210 220 230
ENPQVPKLEK SISGTSPKRE HLPLAVGIAF FLMTFLAS
Length:238
Mass (Da):26,350
Last modified:October 1, 1996 - v1
Checksum:i8EFD6AE8FE33FDDA
GO
Isoform 2 (identifier: P52797-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-196: TSHSGEKPVPTLPQFTMGPNVKINVLE → K

Note: No experimental confirmation available.
Show »
Length:212
Mass (Da):23,575
Checksum:i275AA7F0383A5074
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71 – 74Missing in AAA52368 (PubMed:7973638).Curated4

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_048937190V → M.Corresponds to variant rs17723260dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_055483170 – 196TSHSG…INVLE → K in isoform 2. 1 PublicationAdd BLAST27

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14187 mRNA. Translation: AAC50078.1.
L37360 mRNA. Translation: AAA52368.1.
AK316248 mRNA. Translation: BAH14619.1.
AL691442 Genomic DNA. Translation: CAI15318.1.
CH471121 Genomic DNA. Translation: EAW53137.1.
BC017722 mRNA. Translation: AAH17722.1.
BC110406 mRNA. Translation: AAI10407.1.
CCDSiCCDS1090.1. [P52797-1]
PIRiI38849.
RefSeqiNP_004943.1. NM_004952.4. [P52797-1]
UniGeneiHs.516656.

Genome annotation databases

EnsembliENST00000368408; ENSP00000357393; ENSG00000143590. [P52797-1]
GeneIDi1944.
KEGGihsa:1944.
UCSCiuc001fhf.3. human. [P52797-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14187 mRNA. Translation: AAC50078.1.
L37360 mRNA. Translation: AAA52368.1.
AK316248 mRNA. Translation: BAH14619.1.
AL691442 Genomic DNA. Translation: CAI15318.1.
CH471121 Genomic DNA. Translation: EAW53137.1.
BC017722 mRNA. Translation: AAH17722.1.
BC110406 mRNA. Translation: AAI10407.1.
CCDSiCCDS1090.1. [P52797-1]
PIRiI38849.
RefSeqiNP_004943.1. NM_004952.4. [P52797-1]
UniGeneiHs.516656.

3D structure databases

ProteinModelPortaliP52797.
SMRiP52797.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108264. 6 interactors.
IntActiP52797. 4 interactors.
MINTiMINT-1378559.
STRINGi9606.ENSP00000357393.

PTM databases

PhosphoSitePlusiP52797.

Polymorphism and mutation databases

BioMutaiEFNA3.

Proteomic databases

EPDiP52797.
PaxDbiP52797.
PeptideAtlasiP52797.
PRIDEiP52797.

Protocols and materials databases

DNASUi1944.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368408; ENSP00000357393; ENSG00000143590. [P52797-1]
GeneIDi1944.
KEGGihsa:1944.
UCSCiuc001fhf.3. human. [P52797-1]

Organism-specific databases

CTDi1944.
DisGeNETi1944.
GeneCardsiEFNA3.
HGNCiHGNC:3223. EFNA3.
HPAiCAB010494.
MIMi601381. gene.
neXtProtiNX_P52797.
OpenTargetsiENSG00000143590.
PharmGKBiPA27658.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52797.
KOiK05462.
OMAiQGSKRWE.
OrthoDBiEOG091G0XCP.
PhylomeDBiP52797.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143590-MONOMER.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP52797.
SIGNORiP52797.

Miscellaneous databases

GeneWikiiEFNA3.
GenomeRNAii1944.
PROiP52797.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143590.
CleanExiHS_EFNA3.
GenevisibleiP52797. HS.

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 nameiEFNA3_HUMAN
AccessioniPrimary (citable) accession number: P52797
Secondary accession number(s): B7ZAD3
, D3DV85, Q0VGC9, Q5SR70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.