Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O43921 (EFNA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin-A2
Alternative name(s):
EPH-related receptor tyrosine kinase ligand 6
Short name=LERK-6
HEK7 ligand
Short name=HEK7-L
Gene names
Name:EFNA2
Synonyms:EPLG6, LERK6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. With the EPHA2 receptor may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis By similarity.

Subunit structure

Binds to the receptor tyrosine kinases EPHA3, EPHA4 and EPHA5. Interacts with EPHA8; activates EPHA8. Ref.4

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Potential.

Sequence similarities

Belongs to the ephrin family.

Contains 1 ephrin RBD (ephrin receptor-binding) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 188164Ephrin-A2
PRO_0000008361
Propeptide189 – 21325Removed in mature form Potential
PRO_0000008362

Regions

Domain34 – 174141Ephrin RBD

Amino acid modifications

Lipidation1881GPI-anchor amidated asparagine Potential
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Disulfide bond73 ↔ 114 Ref.4
Disulfide bond102 ↔ 163 Ref.4

Experimental info

Sequence conflict61R → A in CAA07435. Ref.2
Sequence conflict25 – 262RA → PP in CAA07435. Ref.2
Sequence conflict29 – 302AA → RR in CAA07435. Ref.2

Secondary structure

....................... 213
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O43921 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 33C9FB1A8168B2D0

FASTA21323,878
        10         20         30         40         50         60 
MAPAQRPLLP LLLLLLPLPP PPFARAEDAA RANSDRYAVY WNRSNPRFHA GAGDDGGGYT 

        70         80         90        100        110        120 
VEVSINDYLD IYCPHYGAPL PPAERMEHYV LYMVNGEGHA SCDHRQRGFK RWECNRPAAP 

       130        140        150        160        170        180 
GGPLKFSEKF QLFTPFSLGF EFRPGHEYYY ISATPPNAVD RPCLRLKVYV RPTNETLYEA 

       190        200        210 
PEPIFTSNNS CSSPGGCRLF LSTIPVLWTL LGS 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the genes for mouse LERK-3/Ephrin-A3 (Epl3), mouse LERK-4/Ephrin-A4 (Epl4), and human LERK-6/Ephrin-A2 (EPLG6): conservation of intron/exon structure."
Cerretti D.P., Nelson N.
Genomics 47:131-135(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning, chromosomal mapping, and tissue expression of the gene encoding the human Eph-family kinase ligand ephrin-A2."
Aasheim H.-C., Pedeutour F., Grosgeorge J., Logtenberg T.
Biochem. Biophys. Res. Commun. 252:378-382(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Structural plasticity of EPH receptor A4 facilitates cross-class ephrin signaling."
Bowden T.A., Aricescu A.R., Nettleship J.E., Siebold C., Rahman-Huq N., Owens R.J., Stuart D.I., Jones E.Y.
Structure 17:1386-1397(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 33-177 IN COMPLEX WITH EPHA4, DISULFIDE BONDS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U92896, U92893, U92894 Genomic DNA. Translation: AAC39577.1.
AJ007292 mRNA. Translation: CAA07435.1.
AC004258 Genomic DNA. Translation: AAC04896.1.
PIRJE0322.
RefSeqNP_001396.2. NM_001405.3.
UniGeneHs.741510.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WO3X-ray2.35B33-173[»]
ProteinModelPortalO43921.
SMRO43921. Positions 33-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108263. 5 interactions.
DIPDIP-48293N.
IntActO43921. 2 interactions.
MINTMINT-7013470.
STRING9606.ENSP00000215368.

Chemistry

ChEMBLCHEMBL1795109.

PTM databases

PhosphoSiteO43921.

Proteomic databases

PaxDbO43921.
PRIDEO43921.

Protocols and materials databases

DNASU1943.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215368; ENSP00000215368; ENSG00000099617.
GeneID1943.
KEGGhsa:1943.
UCSCuc002lry.2. human.

Organism-specific databases

CTD1943.
GeneCardsGC19P001286.
HGNCHGNC:3222. EFNA2.
HPACAB005178.
MIM602756. gene.
neXtProtNX_O43921.
PharmGKBPA27657.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG252953.
HOGENOMHOG000234373.
HOVERGENHBG051447.
InParanoidO43921.
KOK05462.
OMACSSPGGC.
OrthoDBEOG70W3FD.
PhylomeDBO43921.

Enzyme and pathway databases

SignaLinkO43921.

Gene expression databases

ArrayExpressO43921.
BgeeO43921.
CleanExHS_EFNA2.
GenevestigatorO43921.

Family and domain databases

Gene3D2.60.40.420. 1 hit.
InterProIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view]
PANTHERPTHR11304. PTHR11304. 1 hit.
PfamPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSPR01347. EPHRIN.
ProDomPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF49503. SSF49503. 1 hit.
PROSITEPS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO43921.
GeneWikiEFNA2.
GenomeRNAi1943.
NextBio7871.
PMAP-CutDBO43921.
PROO43921.
SOURCESearch...

Entry information

Entry nameEFNA2_HUMAN
AccessionPrimary (citable) accession number: O43921
Secondary accession number(s): O76020
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM