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P52797 (EFNA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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-A3
Alternative name(s):
EFL-2
EHK1 ligand
Short name=EHK1-L
EPH-related receptor tyrosine kinase ligand 3
Short name=LERK-3
Gene names
Name:EFNA3
Synonyms:EFL2, EPLG3, LERK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length238 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 By similarity.

Subunit structure

Interacts with EPHA8; activates EPHA8.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Tissue specificity

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

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 – 2222 Potential
Chain23 – 214192Ephrin-A3
PRO_0000008369
Propeptide215 – 23824Removed in mature form Potential
PRO_0000008370

Regions

Domain30 – 169140Ephrin RBD

Amino acid modifications

Lipidation2141GPI-anchor amidated glycine Potential
Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation1001N-linked (GlcNAc...) Potential
Disulfide bond63 ↔ 110 By similarity
Disulfide bond99 ↔ 158 By similarity

Natural variations

Natural variant1901V → M.
Corresponds to variant rs17723260 [ dbSNP | Ensembl ].
VAR_048937

Experimental info

Sequence conflict71 – 744Missing in AAA52368. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P52797 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8EFD6AE8FE33FDDA

FASTA23826,350
        10         20         30         40         50         60 
MAAAPLLLLL LLVPVPLLPL LAQGPGGALG NRHAVYWNSS NQHLRREGYT VQVNVNDYLD 

        70         80         90        100        110        120 
IYCPHYNSSG VGPGAGPGPG GGAEQYVLYM VSRNGYRTCN ASQGFKRWEC NRPHAPHSPI 

       130        140        150        160        170        180 
KFSEKFQRYS AFSLGYEFHA GHEYYYISTP THNLHWKCLR MKVFVCCAST SHSGEKPVPT 

       190        200        210        220        230 
LPQFTMGPNV KINVLEDFEG ENPQVPKLEK SISGTSPKRE HLPLAVGIAF FLMTFLAS 

« Hide

References

« Hide 'large scale' references
[1]"Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins."
Kozlosky C.J., Maraskovsky E., McGrew J.T., Vanden Bos T., Teepe M., Lyman S.D., Srinivasan S., Fletcher F.A., Gayle R.B. III, Cerretti D.P., Beckmann M.P.
Oncogene 10:299-306(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity."
Davis S., Gale N.W., Aldrich T.H., Maisonpierre P.C., Lhotak V., Pawson T., Goldfarb M., Yancopoulos G.D.
Science 266:816-819(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Brain and Duodenum.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14187 mRNA. Translation: AAC50078.1.
L37360 mRNA. Translation: AAA52368.1.
AL691442 Genomic DNA. Translation: CAI15318.1.
CH471121 Genomic DNA. Translation: EAW53137.1.
BC017722 mRNA. Translation: AAH17722.1.
BC110406 mRNA. Translation: AAI10407.1.
PIRI38849.
RefSeqNP_004943.1. NM_004952.4.
UniGeneHs.516656.

3D structure databases

ProteinModelPortalP52797.
SMRP52797. Positions 31-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108264. 3 interactions.
IntActP52797. 1 interaction.
MINTMINT-1378559.
STRING9606.ENSP00000357393.

Polymorphism databases

DMDM1706671.

Proteomic databases

PRIDEP52797.

Protocols and materials databases

DNASU1944.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368408; ENSP00000357393; ENSG00000143590.
GeneID1944.
KEGGhsa:1944.
UCSCuc001fhf.3. human.

Organism-specific databases

CTD1944.
GeneCardsGC01P155051.
HGNCHGNC:3223. EFNA3.
HPACAB010494.
MIM601381. gene.
neXtProtNX_P52797.
PharmGKBPA27658.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295575.
HOGENOMHOG000234373.
HOVERGENHBG051447.
InParanoidP52797.
KOK05462.
OrthoDBEOG70W3FD.
PhylomeDBP52797.

Enzyme and pathway databases

SignaLinkP52797.

Gene expression databases

ArrayExpressP52797.
BgeeP52797.
CleanExHS_EFNA3.
GenevestigatorP52797.

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

GeneWikiEFNA3.
GenomeRNAi1944.
NextBio7875.
PROP52797.
SOURCESearch...

Entry information

Entry nameEFNA3_HUMAN
AccessionPrimary (citable) accession number: P52797
Secondary accession number(s): D3DV85, Q0VGC9, Q5SR70
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 117 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM