EFNA3_MOUSE
ID EFNA3_MOUSE Reviewed; 230 AA.
AC O08545; O55217; Q08AV0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ephrin-A3;
DE AltName: Full=EHK1 ligand;
DE Short=EHK1-L;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 3;
DE Short=LERK-3;
DE Flags: Precursor;
GN Name=Efna3; Synonyms=Epl3, Eplg3, Lerk3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-230.
RC STRAIN=129;
RX PubMed=9465306; DOI=10.1006/geno.1997.5088;
RA Cerretti D.P., Nelson N.;
RT "Characterization of the genes for mouse LERK-3/Ephrin-A3 (Epl3), mouse
RT LERK-4/Ephrin-A4 (Epl4), and human LERK-6/Ephrin-A2 (EPLG6): conservation
RT of intron/exon structure.";
RL Genomics 47:131-135(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 60-121.
RX PubMed=8903354; DOI=10.1006/dbio.1996.0269;
RA Flenniken A.M., Gale N.W., Yancopoulos G.D., Wilkinson D.G.;
RT "Distinct and overlapping expression patterns of ligands for Eph-related
RT receptor tyrosine kinases during mouse embryogenesis.";
RL Dev. Biol. 179:382-401(1996).
RN [4]
RP FUNCTION IN EPHA8 ACTIVATION, AND INTERACTION WITH EPHA8.
RX PubMed=9053851; DOI=10.1038/sj.onc.1200857;
RA Park S., Sanchez M.P.;
RT "The Eek receptor, a member of the Eph family of tyrosine protein kinases,
RT can be activated by three different Eph family ligands.";
RL Oncogene 14:533-542(1997).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-38.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT "Gene expression profiling of muscle stem cells identifies novel regulators
RT of postnatal myogenesis.";
RL Front. Cell Dev. Biol. 4:58-58(2016).
CC -!- FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of
CC receptor tyrosine kinases which are crucial for migration, repulsion
CC and adhesion during neuronal, vascular and epithelial development.
CC Binds promiscuously Eph receptors residing on adjacent cells, leading
CC to contact-dependent bidirectional signaling into neighboring cells.
CC The signaling pathway downstream of the receptor is referred to as
CC forward signaling while the signaling pathway downstream of the ephrin
CC ligand is referred to as reverse signaling.
CC {ECO:0000269|PubMed:9053851}.
CC -!- SUBUNIT: Interacts with EPHA8; activates EPHA8.
CC {ECO:0000269|PubMed:9053851}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Expressed in myogenic progenitor cells.
CC {ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: In myogenic progenitor cells, highly expressed at
CC 11.5 dpc and ceases its expression at the late fetal stage (17.5 dpc).
CC {ECO:0000269|PubMed:27446912}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; BC107002; AAI07003.1; -; mRNA.
DR EMBL; BC125003; AAI25004.1; -; mRNA.
DR EMBL; U92885; AAC39961.1; -; Genomic_DNA.
DR EMBL; U90666; AAB50241.1; -; mRNA.
DR CCDS; CCDS38488.1; -.
DR RefSeq; NP_034238.1; NM_010108.1.
DR AlphaFoldDB; O08545; -.
DR SMR; O08545; -.
DR STRING; 10090.ENSMUSP00000029673; -.
DR GlyConnect; 2291; 5 N-Linked glycans (1 site).
DR GlyGen; O08545; 4 sites, 5 N-linked glycans (1 site).
DR iPTMnet; O08545; -.
DR PhosphoSitePlus; O08545; -.
DR MaxQB; O08545; -.
DR PaxDb; O08545; -.
DR PRIDE; O08545; -.
DR ProteomicsDB; 277801; -.
DR Antibodypedia; 4186; 357 antibodies from 31 providers.
DR DNASU; 13638; -.
DR Ensembl; ENSMUST00000029673; ENSMUSP00000029673; ENSMUSG00000028039.
DR GeneID; 13638; -.
DR KEGG; mmu:13638; -.
DR UCSC; uc008pyq.1; mouse.
DR CTD; 1944; -.
DR MGI; MGI:106644; Efna3.
DR VEuPathDB; HostDB:ENSMUSG00000028039; -.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00940000161355; -.
DR InParanoid; O08545; -.
DR OMA; EYNPFVP; -.
DR OrthoDB; 1094764at2759; -.
DR PhylomeDB; O08545; -.
DR Reactome; R-MMU-2682334; EPH-Ephrin signaling.
DR Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR BioGRID-ORCS; 13638; 6 hits in 75 CRISPR screens.
DR PRO; PR:O08545; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O08545; protein.
DR Bgee; ENSMUSG00000028039; Expressed in lip and 212 other tissues.
DR ExpressionAtlas; O08545; baseline and differential.
DR Genevisible; O08545; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISO:MGI.
DR GO; GO:0045664; P:regulation of neuron differentiation; IEA:Ensembl.
DR CDD; cd10425; Ephrin-A_Ectodomain; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR034252; Ephrin-A_Ecto.
DR InterPro; IPR019765; Ephrin_CS.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; PTHR11304; 1.
DR Pfam; PF00812; Ephrin; 1.
DR PRINTS; PR01347; EPHRIN.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..206
FT /note="Ephrin-A3"
FT /id="PRO_0000008371"
FT PROPEP 207..230
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008372"
FT DOMAIN 30..161
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT LIPID 206
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 91..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT CONFLICT 62
FT /note="Y -> I (in Ref. 3; AAB50241)"
FT /evidence="ECO:0000305"
FT CONFLICT 76..77
FT /note="EQ -> DR (in Ref. 3; AAB50241)"
FT /evidence="ECO:0000305"
FT CONFLICT 89..90
FT /note="RT -> QP (in Ref. 3; AAB50241)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="Y -> W (in Ref. 3; AAB50241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 25632 MW; C08AAA0D84B0D795 CRC64;
MAAAPLLLLL LLVPVPLLPL LAQGPGGALG NRHAVYWNSS NQHLRREGYT VQVNVNDYLD
IYCPHYNSSG PGGGAEQYVL YMVNLSGYRT CNASQGSKRW ECNRQHASHS PIKFSEKFQR
YSAFSLGYEF HAGQEYYYIS TPTHNLHWKC LRMKVFVCCA STSHSGEKPV PTLPQFTMGP
NVKINVLEDF EGENPQVPKL EKSISGTSPK REHLPLAVGI AFFLMTLLAS
