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P52798 (EFNA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin-A4
Alternative name(s):
EPH-related receptor tyrosine kinase ligand 4
Short name=LERK-4
Gene names
Name:EFNA4
Synonyms:EPLG4, LERK4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 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. May play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils.

Subcellular location

Isoform 1: Cell membrane; Lipid-anchorGPI-anchor.

Isoform 2: Secreted Probable.

Tissue specificity

Expressed in the adult spleen, lymph node, prostate, ovary, small intestine, and colon, and in fetal heart, lung, liver and kidney. Also detected in hematopoietic cell lines.

Sequence similarities

Belongs to the ephrin family.

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P52798-1)

Also known as: GPI-anchored;

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.
Isoform 2 (identifier: P52798-2)

Also known as: Secreted;

The sequence of this isoform differs from the canonical sequence as follows:
     157-201: KSESAHPVGS...LLILRLLRIL → NLPSHPKEPE...VPIQTDKMEH
Isoform 3 (identifier: P52798-3)

The sequence of this isoform differs from the canonical sequence as follows:
     157-201: KSESAHPVGS...LLILRLLRIL → RARVLPRSPG...LAGACPLITG
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.7
Chain26 – 170145Ephrin-A4
PRO_0000008373
Propeptide171 – 20131Removed in mature form Potential
PRO_0000008374

Regions

Domain26 – 155130Ephrin RBD

Amino acid modifications

Lipidation1701GPI-anchor amidated serine Potential
Glycosylation331N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 99 By similarity
Disulfide bond86 ↔ 144 By similarity

Natural variations

Alternative sequence157 – 20145KSESA…LLRIL → NLPSHPKEPESSQDPLEEEG SLLPALGVPIQTDKMEH in isoform 2.
VSP_001448
Alternative sequence157 – 20145KSESA…LLRIL → RARVLPRSPGGGGIPAACTG GANSDRQDGALMGEIRGSEV TLAGACPLITG in isoform 3.
VSP_046707

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (GPI-anchored) [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: ABE8D5443A9AF28D

FASTA20122,386
        10         20         30         40         50         60 
MRLLPLLRTV LWAAFLGSPL RGGSSLRHVV YWNSSNPRLL RGDAVVELGL NDYLDIVCPH 

        70         80         90        100        110        120 
YEGPGPPEGP ETFALYMVDW PGYESCQAEG PRAYKRWVCS LPFGHVQFSE KIQRFTPFSL 

       130        140        150        160        170        180 
GFEFLPGETY YYISVPTPES SGQCLRLQVS VCCKERKSES AHPVGSPGES GTSGWRGGDT 

       190        200 
PSPLCLLLLL LLLILRLLRI L 

« Hide

Isoform 2 (Secreted) [UniParc].

Checksum: D0817324CC728EF5
Show »

FASTA19321,699
Isoform 3 [UniParc].

Checksum: 67767F6020B4530B
Show »

FASTA20722,584

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] (ISOFORM 1).
[2]"A splice variant of human ephrin-A4 encodes a soluble molecule that is secreted by activated human B lymphocytes."
Aasheim H.-C., Munthe E., Funderud S., Smeland E.B., Beiske K., Logtenberg T.
Blood 95:221-230(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: B-cell.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"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].
[5]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].
[6]"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] (ISOFORM 1).
[7]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-40.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14188 mRNA. Translation: AAC50079.1.
AJ006352 mRNA. Translation: CAA06992.1.
AJ006353 mRNA. Translation: CAA06993.1.
CR533569 mRNA. Translation: CAG38600.1.
AL691442 Genomic DNA. No translation available.
CH471121 Genomic DNA. Translation: EAW53138.1.
CH471121 Genomic DNA. Translation: EAW53139.1.
BC107483 mRNA. Translation: AAI07484.1.
PIRI38850.
RefSeqNP_005218.1. NM_005227.2.
NP_872631.1. NM_182689.1.
NP_872632.2. NM_182690.2.
UniGeneHs.449913.
Hs.639422.

3D structure databases

ProteinModelPortalP52798.
SMRP52798. Positions 24-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108265. 1 interaction.
DIPDIP-48295N.
IntActP52798. 1 interaction.
STRING9606.ENSP00000403005.

PTM databases

PhosphoSiteP52798.

Polymorphism databases

DMDM1706672.

Proteomic databases

PaxDbP52798.
PRIDEP52798.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359751; ENSP00000352789; ENSG00000243364. [P52798-2]
ENST00000368409; ENSP00000357394; ENSG00000243364. [P52798-1]
ENST00000427683; ENSP00000414378; ENSG00000243364. [P52798-3]
GeneID1945.
KEGGhsa:1945.
UCSCuc001fhc.3. human.
uc001fhd.3. human. [P52798-1]
uc001fhe.3. human. [P52798-2]

Organism-specific databases

CTD1945.
GeneCardsGC01P155036.
HGNCHGNC:3224. EFNA4.
HPACAB021350.
MIM601380. gene.
neXtProtNX_P52798.
PharmGKBPA27659.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266803.
HOGENOMHOG000234373.
HOVERGENHBG051447.
InParanoidP52798.
KOK05462.
OMACCKESKS.
OrthoDBEOG70W3FD.
PhylomeDBP52798.

Enzyme and pathway databases

SignaLinkP52798.

Gene expression databases

ArrayExpressP52798.
BgeeP52798.
CleanExHS_EFNA4.
GenevestigatorP52798.

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

GeneWikiEFNA4.
GenomeRNAi1945.
NextBio7879.
PROP52798.
SOURCESearch...

Entry information

Entry nameEFNA4_HUMAN
AccessionPrimary (citable) accession number: P52798
Secondary accession number(s): C9JHJ8 expand/collapse secondary AC list , G3XAK2, O95457, Q5SR71, Q6FI57
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 124 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 chromosome 1

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