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Ephrin-A5 (AL-1) (EPH-related receptor tyrosine kinase ligand 7) (LERK-7)

 EFNA5_MOUSE             Reviewed;         228 AA.
O08543; O08544;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
05-DEC-2018, entry version 156.
RecName: Full=Ephrin-A5;
AltName: Full=AL-1;
AltName: Full=EPH-related receptor tyrosine kinase ligand 7;
Short=LERK-7;
Flags: Precursor;
Name=Efna5; Synonyms=Epl7, Eplg7, Lerk7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
PubMed=8903354; DOI=10.1006/dbio.1996.0269;
Flenniken A.M., Gale N.W., Yancopoulos G.D., Wilkinson D.G.;
"Distinct and overlapping expression patterns of ligands for Eph-
related receptor tyrosine kinases during mouse embryogenesis.";
Dev. Biol. 179:382-401(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION IN EPHA8 ACTIVATION, AND INTERACTION WITH EPHA8.
PubMed=9053851; DOI=10.1038/sj.onc.1200857;
Park S., Sanchez M.P.;
"The Eek receptor, a member of the Eph family of tyrosine protein
kinases, can be activated by three different Eph family ligands.";
Oncogene 14:533-542(1997).
[4]
FUNCTION IN CELL ADHESION AND REPULSION, AND EPHA7 RECEPTOR-BINDING.
PubMed=11089974; DOI=10.1038/35041577;
Holmberg J., Clarke D.L., Frisen J.;
"Regulation of repulsion versus adhesion by different splice forms of
an Eph receptor.";
Nature 408:203-206(2000).
[5]
FUNCTION IN INSULIN SECRETION.
PubMed=17448994; DOI=10.1016/j.cell.2007.02.044;
Konstantinova I., Nikolova G., Ohara-Imaizumi M., Meda P., Kucera T.,
Zarbalis K., Wurst W., Nagamatsu S., Lammert E.;
"EphA-Ephrin-A-mediated beta cell communication regulates insulin
secretion from pancreatic islets.";
Cell 129:359-370(2007).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION IN LENS FIBER CELLS MORPHOGENESIS.
PubMed=18948590; DOI=10.1073/pnas.0808987105;
Cooper M.A., Son A.I., Komlos D., Sun Y., Kleiman N.J., Zhou R.;
"Loss of ephrin-A5 function disrupts lens fiber cell packing and leads
to cataract.";
Proc. Natl. Acad. Sci. U.S.A. 105:16620-16625(2008).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[8]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=27446912; DOI=10.3389/fcell.2016.00058;
Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J.,
de Reynies A., Aurade F., Chang T.H., Zammit P.S., Relaix F.;
"Gene expression profiling of muscle stem cells identifies novel
regulators of postnatal myogenesis.";
Front. Cell Dev. Biol. 4:58-58(2016).
[9]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 28-165 ALONE AND IN COMPLEX
WITH EPHB2, GLYCOSYLATION AT ASN-37, AND DISULFIDE BONDS.
PubMed=15107857; DOI=10.1038/nn1237;
Himanen J.P., Chumley M.J., Lackmann M., Li C., Barton W.A.,
Jeffrey P.D., Vearing C., Geleick D., Feldheim D.A., Boyd A.W.,
Henkemeyer M., Nikolov D.B.;
"Repelling class discrimination: ephrin-A5 binds to and activates
EphB2 receptor signaling.";
Nat. Neurosci. 7:501-509(2004).
-!- 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. Induces compartmentalized signaling within a
caveolae-like membrane microdomain when bound to the extracellular
domain of its cognate receptor. This signaling event requires the
activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor
to regulate cell-cell adhesion and cytoskeletal organization. With
the receptor EPHA2 may regulate lens fiber cells shape and
interactions and be important for lens transparency maintenance.
May function actively to stimulate axon fasciculation. The
interaction of EFNA5 with EPHA5 also mediates communication
between pancreatic islet cells to regulate glucose-stimulated
insulin secretion. Cognate/functional ligand for EPHA7, their
interaction regulates brain development modulating cell-cell
adhesion and repulsion. {ECO:0000269|PubMed:11089974,
ECO:0000269|PubMed:17448994, ECO:0000269|PubMed:18948590,
ECO:0000269|PubMed:9053851}.
-!- SUBUNIT: Binds to the receptor tyrosine kinases EPHA2, EPHA3 and
EPHB1. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5
extracellular domain shedding by ADAM10 which regulates the EFNA5-
EPHA3 complex internalization and function (By similarity). Binds
to EPHB2. Interacts with EPHA8; activates EPHA8. {ECO:0000250,
ECO:0000269|PubMed:15107857, ECO:0000269|PubMed:9053851}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}. Membrane, caveola {ECO:0000250}; Lipid-
anchor, GPI-anchor {ECO:0000250}. Note=Compartmentalized in
discrete caveolae-like membrane microdomains. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=O08543-1; Sequence=Displayed;
Name=Short;
IsoId=O08543-2; Sequence=VSP_001449;
-!- TISSUE SPECIFICITY: Expressed in myogenic progenitor cells.
{ECO:0000269|PubMed:27446912}.
-!- DEVELOPMENTAL STAGE: In myogenic progenitor cells, highly
expressed at E11.5 and ceases its expression at the late fetal
stage (E17.5). {ECO:0000269|PubMed:27446912}.
-!- DISRUPTION PHENOTYPE: Mice display cataract an opacification of
the lens. {ECO:0000269|PubMed:18948590}.
-!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U90664; AAB50239.1; -; mRNA.
EMBL; U90665; AAB50240.1; -; mRNA.
EMBL; BC040218; AAH40218.1; -; mRNA.
CCDS; CCDS28934.1; -. [O08543-2]
CCDS; CCDS28935.1; -. [O08543-1]
RefSeq; NP_034239.1; NM_010109.3. [O08543-2]
RefSeq; NP_997537.1; NM_207654.2. [O08543-1]
UniGene; Mm.401670; -.
UniGene; Mm.7978; -.
PDB; 1SHW; X-ray; 2.20 A; A=28-164.
PDB; 1SHX; X-ray; 2.10 A; A/B=28-164.
PDBsum; 1SHW; -.
PDBsum; 1SHX; -.
ProteinModelPortal; O08543; -.
SMR; O08543; -.
IntAct; O08543; 2.
STRING; 10090.ENSMUSP00000076115; -.
iPTMnet; O08543; -.
PhosphoSitePlus; O08543; -.
PaxDb; O08543; -.
PRIDE; O08543; -.
Ensembl; ENSMUST00000076840; ENSMUSP00000076115; ENSMUSG00000048915. [O08543-1]
Ensembl; ENSMUST00000078839; ENSMUSP00000077883; ENSMUSG00000048915. [O08543-2]
GeneID; 13640; -.
KEGG; mmu:13640; -.
UCSC; uc008dfg.2; mouse. [O08543-1]
UCSC; uc008dfh.2; mouse. [O08543-2]
CTD; 1946; -.
MGI; MGI:107444; Efna5.
eggNOG; KOG3858; Eukaryota.
eggNOG; ENOG4111FMJ; LUCA.
GeneTree; ENSGT00940000157299; -.
HOGENOM; HOG000234373; -.
HOVERGEN; HBG051447; -.
InParanoid; O08543; -.
KO; K05462; -.
OMA; CVKTIGV; -.
OrthoDB; EOG091G0IJF; -.
PhylomeDB; O08543; -.
Reactome; R-MMU-2682334; EPH-Ephrin signaling.
Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
ChiTaRS; Efna5; mouse.
EvolutionaryTrace; O08543; -.
PRO; PR:O08543; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000048915; Expressed in 289 organ(s), highest expression level in ear.
CleanEx; MM_EFNA5; -.
Genevisible; O08543; MM.
GO; GO:0005912; C:adherens junction; IDA:MGI.
GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045499; F:chemorepellent activity; IDA:MGI.
GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:0005169; F:neurotrophin TRKB receptor binding; IPI:BHF-UCL.
GO; GO:0007411; P:axon guidance; IDA:MGI.
GO; GO:0007420; P:brain development; ISO:MGI.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IDA:MGI.
GO; GO:1904322; P:cellular response to forskolin; IDA:MGI.
GO; GO:0048668; P:collateral sprouting; IDA:BHF-UCL.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
GO; GO:0048672; P:positive regulation of collateral sprouting; IMP:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0051965; P:positive regulation of synapse assembly; IDA:BHF-UCL.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0022604; P:regulation of cell morphogenesis; ISO:MGI.
GO; GO:0022407; P:regulation of cell-cell adhesion; IDA:UniProtKB.
GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:MGI.
GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
CDD; cd10425; Ephrin-A_Ectodomain; 1.
Gene3D; 2.60.40.420; -; 1.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR031328; Ephrin.
InterPro; IPR034252; Ephrin-A_Ecto.
InterPro; IPR019765; Ephrin_CS.
InterPro; IPR001799; Ephrin_RBD.
PANTHER; PTHR11304; PTHR11304; 1.
Pfam; PF00812; Ephrin; 1.
PRINTS; PR01347; EPHRIN.
ProDom; PD002533; Ephrin; 1.
SUPFAM; SSF49503; SSF49503; 1.
PROSITE; PS01299; EPHRIN_RBD_1; 1.
PROSITE; PS51551; EPHRIN_RBD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
GPI-anchor; Lipoprotein; Membrane; Neurogenesis; Reference proteome;
Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 203 Ephrin-A5.
/FTId=PRO_0000008379.
PROPEP 204 228 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000008380.
DOMAIN 29 162 Ephrin RBD. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
LIPID 203 203 GPI-anchor amidated asparagine.
{ECO:0000255}.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15107857}.
CARBOHYD 162 162 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19656770}.
DISULFID 62 102 {ECO:0000255|PROSITE-ProRule:PRU00884,
ECO:0000269|PubMed:15107857}.
DISULFID 90 151 {ECO:0000255|PROSITE-ProRule:PRU00884,
ECO:0000269|PubMed:15107857}.
VAR_SEQ 163 189 Missing (in isoform Short).
{ECO:0000303|PubMed:8903354}.
/FTId=VSP_001449.
STRAND 30 35 {ECO:0000244|PDB:1SHX}.
HELIX 41 44 {ECO:0000244|PDB:1SHX}.
STRAND 49 52 {ECO:0000244|PDB:1SHX}.
STRAND 57 61 {ECO:0000244|PDB:1SHX}.
STRAND 67 69 {ECO:0000244|PDB:1SHW}.
STRAND 71 73 {ECO:0000244|PDB:1SHW}.
STRAND 77 82 {ECO:0000244|PDB:1SHX}.
HELIX 84 88 {ECO:0000244|PDB:1SHX}.
STRAND 92 102 {ECO:0000244|PDB:1SHX}.
STRAND 108 111 {ECO:0000244|PDB:1SHW}.
STRAND 113 117 {ECO:0000244|PDB:1SHX}.
STRAND 134 144 {ECO:0000244|PDB:1SHX}.
STRAND 148 150 {ECO:0000244|PDB:1SHW}.
STRAND 153 158 {ECO:0000244|PDB:1SHX}.
TURN 161 164 {ECO:0000244|PDB:1SHX}.
SEQUENCE 228 AA; 26339 MW; 85439F5337420022 CRC64;
MLHVEMLTLL FLVLWMCVFS QDPGSKVVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV
FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL
FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK
VENSLEPADD TVHESAEPSR GENAAQTPRI PSRLLAILLF LLAMLLTL


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