Entry - *601380 - EPHRIN A4; EFNA4 - OMIM
 
* 601380

EPHRIN A4; EFNA4


Alternative titles; symbols

EPH-RELATED RECEPTOR TYROSINE KINASE LIGAND 4; EPLG4
LIGAND OF EPH-RELATED KINASE 4; LERK4
EFL4


HGNC Approved Gene Symbol: EFNA4

Cytogenetic location: 1q21.3     Genomic coordinates (GRCh38): 1:155,063,740-155,069,553 (from NCBI)


TEXT

Description

Proteins in the LERK subfamily of ligands, called ephrins, bind to members of the EPH group of receptor tyrosine kinases. The various ephrins are characterized by sequence similarities and the fact that they are attached to the cell membrane by glycosylphosphatidylinositol (GPI) anchors or by a single transmembrane domain (Cerretti et al., 1996). See 179610 for additional information on ephrins and the Eph receptor family.


Cloning and Expression

Using the receptor tyrosine kinase HEK (EPHA3; 179611) as bait to screen a human T-lymphoma HSB-2 cDNA expression library, Kozlosky et al. (1995) cloned LERK4. The deduced 201-amino acid LERK4 protein has a predicted N-terminal signal sequence, an extracellular receptor-binding domain, a spacer region, and a hydrophobic C terminus. The receptor-binding domain has an N-glycosylation site and 6 cysteines predicted to form disulfide bonds, and the C terminus shares structural similarity with GPI-linked proteins. Northern blot analysis detected a 1.4-kb LERK4 transcript in human adult spleen, prostate, ovary, small intestine, and colon and in fetal heart, lung, and kidney.


Gene Structure

Cerretti and Nelson (1998) reported that the mouse Efna4 gene has 4 exons. The gene structures of human EFNA2 (602756) and mouse Efna4, Efna3 (601381), and Efnb1 (300035) are conserved through the first 3 exons.


Mapping

Using fluorescence in situ hybridization, Cerretti et al. (1996) mapped the EPLG4 gene to a cluster on chromosome 1q21-q22, together with EPLG1 (EFNA1; 191164) and EPLG3 (EFNA3; 601381). By interspecific backcross analysis, they mapped the mouse EPLG4 homolog (Epl4) to the central region of mouse chromosome 3.


Gene Function

By analyzing binding kinetics, Kozlosky et al. (1995) found that LERK4 had a single class of binding sites for HEK, but a biphasic binding curve with high- and low-affinity binding components for ELK (EPHB1; 600600).


Molecular Genetics

Associations Pending Confirmation

Merrill et al. (2006) screened 81 DNA samples from patients with nonsyndromic coronal craniosynostosis (see CRS1; 123100) for variation in the coding sequence of EFNA4 and identified 3 heterozygous variants in 3 patients with unicoronal synostosis: 2 were missense mutations, H60Y (rs148289726) and P117T (rs143886639), and the third was a frameshift indel mutation (471_472delCCinsA). Each variant was also present in a clinically unaffected parent, but none were found in 370 northern European control samples or in 151 additional unrelated craniosynostosis patients who had either syndromic features or a different combination of affected cranial sutures. Transfection studies in COS-7 cells showed complete (98%) loss of binding for the P117T mutant and partial (65%) loss for the H60Y mutant compared to wildtype. Using patient fibroblasts, Merrill et al. (2006) demonstrated that the frameshift mutation is expressed in an alternatively spliced minor isoform of EFNA4.


REFERENCES

  1. Cerretti, D. P., Lyman, S. D., Kozlosky, C. J., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Valentine, V., Kirstein, M. N., Shapiro, D. N., Morris, S. W. The genes encoding the Eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3. Genomics 33: 277-282, 1996. [PubMed: 8660976, related citations] [Full Text]

  2. Cerretti, D. P., Nelson, N. 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. Genomics 47: 131-135, 1998. [PubMed: 9465306, related citations] [Full Text]

  3. Kozlosky, C. J., Maraskovsky, E., McGrew, J. T., VandenBos, T., Teepe, M., Lyman, S. D., Srinivasan, S., Fletcher, F. A., Gayle, R. B., III, Cerretti, D. P., Beckmann, M. P. Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins. Oncogene 10: 299-306, 1995. [PubMed: 7838529, related citations]

  4. Merrill, A. E., Bochukova, E. G., Brugger, S. M., Ishii, M., Pilz, D. T., Wall, S. A., Lyons, K. M., Wilkie, A. O. M., Maxson, R. E., Jr. Cell mixing at a neural crest-mesoderm boundary and deficient ephrin-Eph signaling in the pathogenesis of craniosynostosis. Hum. Molec. Genet. 15: 1319-1328, 2006. [PubMed: 16540516, related citations] [Full Text]


Patricia A. Hartz - updated : 05/16/2016
Marla J. F. O'Neill - updated : 7/24/2013
Patti M. Sherman - updated : 7/9/1998
Creation Date:
Alan F. Scott : 8/14/1996
mgross : 05/16/2016
carol : 7/24/2013
carol : 3/17/2003
carol : 7/9/1998
dholmes : 7/9/1998
psherman : 4/23/1998
psherman : 4/20/1998
mark : 8/18/1996
terry : 8/16/1996
mark : 8/14/1996

* 601380

EPHRIN A4; EFNA4


Alternative titles; symbols

EPH-RELATED RECEPTOR TYROSINE KINASE LIGAND 4; EPLG4
LIGAND OF EPH-RELATED KINASE 4; LERK4
EFL4


HGNC Approved Gene Symbol: EFNA4

Cytogenetic location: 1q21.3     Genomic coordinates (GRCh38): 1:155,063,740-155,069,553 (from NCBI)


TEXT

Description

Proteins in the LERK subfamily of ligands, called ephrins, bind to members of the EPH group of receptor tyrosine kinases. The various ephrins are characterized by sequence similarities and the fact that they are attached to the cell membrane by glycosylphosphatidylinositol (GPI) anchors or by a single transmembrane domain (Cerretti et al., 1996). See 179610 for additional information on ephrins and the Eph receptor family.


Cloning and Expression

Using the receptor tyrosine kinase HEK (EPHA3; 179611) as bait to screen a human T-lymphoma HSB-2 cDNA expression library, Kozlosky et al. (1995) cloned LERK4. The deduced 201-amino acid LERK4 protein has a predicted N-terminal signal sequence, an extracellular receptor-binding domain, a spacer region, and a hydrophobic C terminus. The receptor-binding domain has an N-glycosylation site and 6 cysteines predicted to form disulfide bonds, and the C terminus shares structural similarity with GPI-linked proteins. Northern blot analysis detected a 1.4-kb LERK4 transcript in human adult spleen, prostate, ovary, small intestine, and colon and in fetal heart, lung, and kidney.


Gene Structure

Cerretti and Nelson (1998) reported that the mouse Efna4 gene has 4 exons. The gene structures of human EFNA2 (602756) and mouse Efna4, Efna3 (601381), and Efnb1 (300035) are conserved through the first 3 exons.


Mapping

Using fluorescence in situ hybridization, Cerretti et al. (1996) mapped the EPLG4 gene to a cluster on chromosome 1q21-q22, together with EPLG1 (EFNA1; 191164) and EPLG3 (EFNA3; 601381). By interspecific backcross analysis, they mapped the mouse EPLG4 homolog (Epl4) to the central region of mouse chromosome 3.


Gene Function

By analyzing binding kinetics, Kozlosky et al. (1995) found that LERK4 had a single class of binding sites for HEK, but a biphasic binding curve with high- and low-affinity binding components for ELK (EPHB1; 600600).


Molecular Genetics

Associations Pending Confirmation

Merrill et al. (2006) screened 81 DNA samples from patients with nonsyndromic coronal craniosynostosis (see CRS1; 123100) for variation in the coding sequence of EFNA4 and identified 3 heterozygous variants in 3 patients with unicoronal synostosis: 2 were missense mutations, H60Y (rs148289726) and P117T (rs143886639), and the third was a frameshift indel mutation (471_472delCCinsA). Each variant was also present in a clinically unaffected parent, but none were found in 370 northern European control samples or in 151 additional unrelated craniosynostosis patients who had either syndromic features or a different combination of affected cranial sutures. Transfection studies in COS-7 cells showed complete (98%) loss of binding for the P117T mutant and partial (65%) loss for the H60Y mutant compared to wildtype. Using patient fibroblasts, Merrill et al. (2006) demonstrated that the frameshift mutation is expressed in an alternatively spliced minor isoform of EFNA4.


REFERENCES

  1. Cerretti, D. P., Lyman, S. D., Kozlosky, C. J., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Valentine, V., Kirstein, M. N., Shapiro, D. N., Morris, S. W. The genes encoding the Eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3. Genomics 33: 277-282, 1996. [PubMed: 8660976] [Full Text: https://doi.org/10.1006/geno.1996.0192]

  2. Cerretti, D. P., Nelson, N. 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. Genomics 47: 131-135, 1998. [PubMed: 9465306] [Full Text: https://doi.org/10.1006/geno.1997.5088]

  3. Kozlosky, C. J., Maraskovsky, E., McGrew, J. T., VandenBos, T., Teepe, M., Lyman, S. D., Srinivasan, S., Fletcher, F. A., Gayle, R. B., III, Cerretti, D. P., Beckmann, M. P. Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins. Oncogene 10: 299-306, 1995. [PubMed: 7838529]

  4. Merrill, A. E., Bochukova, E. G., Brugger, S. M., Ishii, M., Pilz, D. T., Wall, S. A., Lyons, K. M., Wilkie, A. O. M., Maxson, R. E., Jr. Cell mixing at a neural crest-mesoderm boundary and deficient ephrin-Eph signaling in the pathogenesis of craniosynostosis. Hum. Molec. Genet. 15: 1319-1328, 2006. [PubMed: 16540516] [Full Text: https://doi.org/10.1093/hmg/ddl052]


Contributors:
Patricia A. Hartz - updated : 05/16/2016
Marla J. F. O'Neill - updated : 7/24/2013
Patti M. Sherman - updated : 7/9/1998

Creation Date:
Alan F. Scott : 8/14/1996

Edit History:
mgross : 05/16/2016
carol : 7/24/2013
carol : 3/17/2003
carol : 7/9/1998
dholmes : 7/9/1998
psherman : 4/23/1998
psherman : 4/20/1998
mark : 8/18/1996
terry : 8/16/1996
mark : 8/14/1996