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Ephrin-A1 (EPH-related receptor tyrosine kinase ligand 1) (LERK-1) (Immediate early response protein B61) [Cleaved into: Ephrin-A1, secreted form]

 EFNA1_MOUSE             Reviewed;         205 AA.
P52793; P97331;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
05-DEC-2018, entry version 144.
RecName: Full=Ephrin-A1;
AltName: Full=EPH-related receptor tyrosine kinase ligand 1;
Short=LERK-1;
AltName: Full=Immediate early response protein B61;
Contains:
RecName: Full=Ephrin-A1, secreted form;
Flags: Precursor;
Name=Efna1; Synonyms=Epgl1, Epl1, Lerk1;
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].
STRAIN=ICR;
PubMed=7675446;
Takahashi H., Ikeda T.;
"Molecular cloning and expression of rat and mouse B61 gene:
implications on organogenesis.";
Oncogene 11:879-883(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
Morris J.C., Ciarletta A., Morris G.E., Giannotti J., Caruso A.,
Hammett D.J., Finnerty H., Turner K., Wood C.R.;
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; 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).
[5]
FUNCTION.
PubMed=16782872; DOI=10.1128/MCB.02215-05;
Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W.,
Chen J.;
"Essential role of Vav family guanine nucleotide exchange factors in
EphA receptor-mediated angiogenesis.";
Mol. Cell. Biol. 26:4830-4842(2006).
[6]
FUNCTION IN DENDRITIC SPINE MORPHOGENESIS.
PubMed=17143272; DOI=10.1038/nn1811;
Fu W.Y., Chen Y., Sahin M., Zhao X.S., Shi L., Bikoff J.B., Lai K.O.,
Yung W.H., Fu A.K., Greenberg M.E., Ip N.Y.;
"Cdk5 regulates EphA4-mediated dendritic spine retraction through an
ephexin1-dependent mechanism.";
Nat. Neurosci. 10:67-76(2007).
[7]
FUNCTION.
PubMed=18387945; DOI=10.1074/jbc.M709934200;
Fang W.B., Brantley-Sieders D.M., Hwang Y., Ham A.-J.L., Chen J.;
"Identification and functional analysis of phosphorylated tyrosine
residues within EphA2 receptor tyrosine kinase.";
J. Biol. Chem. 283:16017-16026(2008).
[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).
-!- 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. Plays an important role in
angiogenesis and tumor neovascularization. The recruitment of
VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is
critical for EFNA1-induced RAC1 GTPase activation and vascular
endothelial cell migration and assembly. Exerts anti-oncogenic
effects in tumor cells through activation and down-regulation of
EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which
leads to its internalization and degradation. Acts as a negative
regulator in the tumorigenesis of gliomas by down-regulating EPHA2
and FAK. Can evoke collapse of embryonic neuronal growth cone and
regulates dendritic spine morphogenesis.
{ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:17143272,
ECO:0000269|PubMed:18387945}.
-!- SUBUNIT: Monomer. Homodimer. Forms heterodimers with EPHA2. Binds
to the receptor tyrosine kinases EPHA2, EPHA3, EPHA4, EPHA5, EPHA6
and EPHA7. Also binds with low affinity to EPHA1 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q15375:EPHA7 (xeno); NbExp=2; IntAct=EBI-5241529, EBI-1383428;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P20827}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:P20827}.
-!- SUBCELLULAR LOCATION: Ephrin-A1, secreted form: Secreted
{ECO:0000250|UniProtKB:P20827}.
-!- TISSUE SPECIFICITY: Expressed in myogenic progenitor cells.
{ECO:0000269|PubMed:27446912}.
-!- DEVELOPMENTAL STAGE: In myogenic progenitor cells, expressed
during the acquisition of muscle stem cell properties, from E18.5
to adulthood. {ECO:0000269|PubMed:27446912}.
-!- PTM: Undergoes proteolysis by a metalloprotease to give rise to a
soluble monomeric form. {ECO:0000250}.
-!- PTM: N-Glycosylation is required for binding to EPHA2 receptor and
inducing its internalization. {ECO:0000250|UniProtKB:P20827}.
-!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; D38146; BAA07344.1; -; mRNA.
EMBL; U26188; AAA67563.1; -; mRNA.
EMBL; U90662; AAB50237.1; -; mRNA.
EMBL; BC002046; AAH02046.1; -; mRNA.
CCDS; CCDS17501.1; -.
RefSeq; NP_034237.3; NM_010107.4.
UniGene; Mm.15675; -.
ProteinModelPortal; P52793; -.
SMR; P52793; -.
BioGrid; 199389; 3.
IntAct; P52793; 1.
STRING; 10090.ENSMUSP00000029566; -.
iPTMnet; P52793; -.
PhosphoSitePlus; P52793; -.
MaxQB; P52793; -.
PaxDb; P52793; -.
PRIDE; P52793; -.
Ensembl; ENSMUST00000029566; ENSMUSP00000029566; ENSMUSG00000027954.
GeneID; 13636; -.
KEGG; mmu:13636; -.
UCSC; uc008pyo.2; mouse.
CTD; 1942; -.
MGI; MGI:103236; Efna1.
eggNOG; KOG3858; Eukaryota.
eggNOG; ENOG4111FMJ; LUCA.
GeneTree; ENSGT00940000159919; -.
HOGENOM; HOG000234373; -.
HOVERGEN; HBG051447; -.
InParanoid; P52793; -.
KO; K05462; -.
OMA; PIHHQED; -.
OrthoDB; EOG091G0K52; -.
PhylomeDB; P52793; -.
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.
PRO; PR:P52793; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027954; Expressed in 300 organ(s), highest expression level in retina.
CleanEx; MM_EFNA1; -.
ExpressionAtlas; P52793; baseline and differential.
Genevisible; P52793; MM.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0046875; F:ephrin receptor binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
GO; GO:0007411; P:axon guidance; IBA:GO_Central.
GO; GO:0016477; P:cell migration; ISO:MGI.
GO; GO:0003199; P:endocardial cushion to mesenchymal transition involved in heart valve formation; IMP:BHF-UCL.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0003183; P:mitral valve morphogenesis; IMP:BHF-UCL.
GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IDA:UniProtKB.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0043409; P:negative regulation of MAPK cascade; IDA:MGI.
GO; GO:1903051; P:negative regulation of proteolysis involved in cellular protein catabolic process; ISO:MGI.
GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0030182; P:neuron differentiation; IDA:MGI.
GO; GO:0014028; P:notochord formation; IGI:MGI.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:MGI.
GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISO:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:MGI.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0050770; P:regulation of axonogenesis; IDA:MGI.
GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IDA:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISO:MGI.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
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;
Angiogenesis; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
Secreted; Signal; Tumor suppressor.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 182 Ephrin-A1.
/FTId=PRO_0000008355.
CHAIN 18 ? Ephrin-A1, secreted form.
/FTId=PRO_0000389631.
PROPEP 183 205 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000008356.
DOMAIN 18 161 Ephrin RBD. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
LIPID 182 182 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 26 26 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 51 92 {ECO:0000255|PROSITE-ProRule:PRU00884}.
DISULFID 80 140 {ECO:0000255|PROSITE-ProRule:PRU00884}.
CONFLICT 74 74 H -> Y (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 79 79 A -> T (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 81 81 Q -> E (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 91 91 N -> K (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 94 94 R -> Q (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 112 112 T -> S (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 115 115 I -> T (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 138 138 S -> T (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 154 154 N -> S (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 156 156 Q -> H (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 159 159 V -> A (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 181 181 Y -> H (in Ref. 1; BAA07344).
{ECO:0000305}.
CONFLICT 204 204 S -> T (in Ref. 1; BAA07344).
{ECO:0000305}.
SEQUENCE 205 AA; 23802 MW; 5A8F3A6E2091E868 CRC64;
MEFLWAPLLG LCCSLAAADR HIVFWNSSNP KFREEDYTVH VQLNDYLDII CPHYEDDSVA
DAAMERYTLY MVEHQEYVAC QPQSKDQVRW NCNRPSAKHG PEKLSEKFQR FTPFILGKEF
KEGHSYYYIS KPIYHQESQC LKLKVTVNGK ITHNPQAHVN PQEKRLQADD PEVQVLHSIG
YSAAPRLFPL VWAVLLLPLL LLQSQ


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