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

 EFNA5_HUMAN             Reviewed;         228 AA.
P52803;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
20-JUN-2018, entry version 149.
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=EPLG7, LERK7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7748564; DOI=10.1016/0896-6273(95)90335-6;
Winslow J.W., Moran P., Valverde J., Shih A., Yuan J.Q., Wong S.C.,
Tsai S.P., Goddard A., Henzel W.J., Hefti F., Beck K.D., Caras I.W.;
"Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor
involved in axon bundle formation.";
Neuron 14:973-981(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9245480; DOI=10.1006/cyto.1997.0199;
Kozlosky C.J., Vanden Bos T., Park L.S., Cerretti D.P.,
Carpenter M.K.;
"LERK-7: a ligand of the Eph-related kinases is developmentally
regulated in the brain.";
Cytokine 9:540-549(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[4]
FUNCTION.
PubMed=10601038; DOI=10.1101/gad.13.23.3125;
Davy A., Gale N.W., Murray E.W., Klinghoffer R.A., Soriano P.,
Feuerstein C., Robbins S.M.;
"Compartmentalized signaling by GPI-anchored ephrin-A5 requires the
Fyn tyrosine kinase to regulate cellular adhesion.";
Genes Dev. 13:3125-3135(1999).
[5]
FUNCTION IN CELL-CELL ADHESION, EPHA3-BINDING, AND SUBCELLULAR
LOCATION.
PubMed=11870224;
Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M.,
Down M., Boyd A.W., Alewood P.F., Lackmann M.;
"Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-
expressing 293T and melanoma cells by CrkII and Rho-mediated
signalling.";
J. Cell Sci. 115:1059-1072(2002).
[6]
IDENTIFICATION IN A COMPLEX WITH ADAM10 AND EPHA3.
PubMed=16239146; DOI=10.1016/j.cell.2005.08.014;
Janes P.W., Saha N., Barton W.A., Kolev M.V., Wimmer-Kleikamp S.H.,
Nievergall E., Blobel C.P., Himanen J.P., Lackmann M., Nikolov D.B.;
"Adam meets Eph: an ADAM substrate recognition module acts as a
molecular switch for ephrin cleavage in trans.";
Cell 123:291-304(2005).
[7]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-189, GLYCOSYLATION AT
ASN-37, AND DISULFIDE BONDS.
PubMed=17400922; DOI=10.1110/ps.062665807;
Nikolov D.B., Li C., Lackmann M., Jeffrey P., Himanen J.P.;
"Crystal structure of the human ephrin-A5 ectodomain.";
Protein Sci. 16:996-1000(2007).
-!- 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:10601038,
ECO:0000269|PubMed:11870224}.
-!- SUBUNIT: Binds to EPHB2. Interacts with EPHA8; activates EPHA8 (By
similarity). 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. {ECO:0000250,
ECO:0000269|PubMed:16239146}.
-!- INTERACTION:
P29317:EPHA2; NbExp=6; IntAct=EBI-1753674, EBI-702104;
P54764:EPHA4; NbExp=2; IntAct=EBI-1753674, EBI-5773557;
Q9BSE4:HERPUD2; NbExp=4; IntAct=EBI-1753674, EBI-2868124;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11870224};
Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11870224}. Membrane,
caveola {ECO:0000269|PubMed:11870224}; Lipid-anchor, GPI-anchor
{ECO:0000269|PubMed:11870224}. Note=Compartmentalized in discrete
caveolae-like membrane microdomains.
-!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
-----------------------------------------------------------------------
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EMBL; U26403; AAB60377.1; -; mRNA.
EMBL; BC075054; AAH75054.1; -; mRNA.
EMBL; BC075055; AAH75055.1; -; mRNA.
CCDS; CCDS4097.1; -.
PIR; I58170; I58170.
RefSeq; NP_001953.1; NM_001962.2.
UniGene; Hs.288741; -.
PDB; 2X11; X-ray; 4.83 A; B=27-166.
PDB; 3MX0; X-ray; 3.51 A; B/D=28-165.
PDB; 4BK5; X-ray; 4.00 A; C=27-166.
PDB; 4BKA; X-ray; 5.30 A; C=27-166.
PDB; 4L0P; X-ray; 2.26 A; B=27-166.
PDB; 4M4R; X-ray; 3.13 A; B/D/F/H=27-165.
PDBsum; 2X11; -.
PDBsum; 3MX0; -.
PDBsum; 4BK5; -.
PDBsum; 4BKA; -.
PDBsum; 4L0P; -.
PDBsum; 4M4R; -.
ProteinModelPortal; P52803; -.
SMR; P52803; -.
BioGrid; 108266; 31.
DIP; DIP-48296N; -.
IntAct; P52803; 12.
STRING; 9606.ENSP00000328777; -.
iPTMnet; P52803; -.
PhosphoSitePlus; P52803; -.
BioMuta; EFNA5; -.
DMDM; 1706678; -.
EPD; P52803; -.
MaxQB; P52803; -.
PaxDb; P52803; -.
PeptideAtlas; P52803; -.
PRIDE; P52803; -.
ProteomicsDB; 56539; -.
Ensembl; ENST00000333274; ENSP00000328777; ENSG00000184349.
GeneID; 1946; -.
KEGG; hsa:1946; -.
UCSC; uc003kol.3; human.
CTD; 1946; -.
DisGeNET; 1946; -.
EuPathDB; HostDB:ENSG00000184349.12; -.
GeneCards; EFNA5; -.
HGNC; HGNC:3225; EFNA5.
HPA; CAB013282; -.
HPA; HPA054047; -.
MIM; 601535; gene.
neXtProt; NX_P52803; -.
OpenTargets; ENSG00000184349; -.
PharmGKB; PA27660; -.
eggNOG; KOG3858; Eukaryota.
eggNOG; ENOG4111FMJ; LUCA.
GeneTree; ENSGT00390000015107; -.
HOGENOM; HOG000234373; -.
HOVERGEN; HBG051447; -.
InParanoid; P52803; -.
KO; K05462; -.
OMA; TERYILY; -.
OrthoDB; EOG091G0IJF; -.
PhylomeDB; P52803; -.
Reactome; R-HSA-2682334; EPH-Ephrin signaling.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
SignaLink; P52803; -.
SIGNOR; P52803; -.
ChiTaRS; EFNA5; human.
EvolutionaryTrace; P52803; -.
GeneWiki; EFNA5; -.
GeneWiki; Ephrin-A5; -.
GenomeRNAi; 1946; -.
PRO; PR:P52803; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000184349; -.
CleanEx; HS_EFNA5; -.
ExpressionAtlas; P52803; baseline and differential.
Genevisible; P52803; HS.
GO; GO:0005912; C:adherens junction; IEA:Ensembl.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0045499; F:chemorepellent activity; IEA:Ensembl.
GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:0005168; F:neurotrophin TRKA receptor binding; NAS:BHF-UCL.
GO; GO:0005169; F:neurotrophin TRKB receptor binding; NAS:BHF-UCL.
GO; GO:0005170; F:neurotrophin TRKC receptor binding; NAS:BHF-UCL.
GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; NAS:BHF-UCL.
GO; GO:0007411; P:axon guidance; IBA:GO_Central.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
GO; GO:1904322; P:cellular response to forskolin; IEA:Ensembl.
GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IDA:MGI.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0048672; P:positive regulation of collateral sprouting; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; NAS:BHF-UCL.
GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0022604; P:regulation of cell morphogenesis; IDA:MGI.
GO; GO:0022407; P:regulation of cell-cell adhesion; IDA:UniProtKB.
GO; GO:0051893; P:regulation of focal adhesion assembly; IDA: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; ISS:UniProtKB.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IDA:UniProtKB.
GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
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; Cell membrane; Complete proteome; Developmental protein;
Differentiation; Disulfide bond; Glycoprotein; GPI-anchor;
Lipoprotein; Membrane; Neurogenesis; Polymorphism; Reference proteome;
Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 203 Ephrin-A5.
/FTId=PRO_0000008377.
PROPEP 204 228 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000008378.
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:17400922}.
DISULFID 62 102 {ECO:0000269|PubMed:17400922}.
DISULFID 90 151 {ECO:0000269|PubMed:17400922}.
VARIANT 55 55 N -> K (in dbSNP:rs469062).
/FTId=VAR_012035.
STRAND 31 35 {ECO:0000244|PDB:4L0P}.
HELIX 41 43 {ECO:0000244|PDB:4L0P}.
STRAND 44 46 {ECO:0000244|PDB:4L0P}.
STRAND 49 52 {ECO:0000244|PDB:4L0P}.
STRAND 57 61 {ECO:0000244|PDB:4L0P}.
HELIX 71 73 {ECO:0000244|PDB:4L0P}.
STRAND 76 82 {ECO:0000244|PDB:4L0P}.
HELIX 84 89 {ECO:0000244|PDB:4L0P}.
TURN 93 95 {ECO:0000244|PDB:4L0P}.
STRAND 96 102 {ECO:0000244|PDB:4L0P}.
STRAND 108 111 {ECO:0000244|PDB:4M4R}.
STRAND 113 117 {ECO:0000244|PDB:4L0P}.
STRAND 135 144 {ECO:0000244|PDB:4L0P}.
STRAND 153 158 {ECO:0000244|PDB:4L0P}.
HELIX 161 164 {ECO:0000244|PDB:4L0P}.
SEQUENCE 228 AA; 26297 MW; 6893B1CCACFF3F57 CRC64;
MLHVEMLTLV FLVLWMCVFS QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV
FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL
FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK
VENSLEPADD TVHESAEPSR GENAAQTPRI PSRLLAILLF LLAMLLTL


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