EFNA4_MOUSE
ID EFNA4_MOUSE Reviewed; 206 AA.
AC O08542; O55218;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ephrin-A4;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 4;
DE Short=LERK-4;
DE Flags: Precursor;
GN Name=Efna4; Synonyms=Epl4, Eplg4, Lerk4;
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 [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 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 May play a role in the interaction between activated B-lymphocytes and
CC dendritic cells in tonsils (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
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; U90663; AAB50238.1; -; mRNA.
DR EMBL; U92890; AAC39962.1; -; Genomic_DNA.
DR EMBL; U92889; AAC39962.1; JOINED; Genomic_DNA.
DR CCDS; CCDS38489.1; -.
DR RefSeq; NP_031936.2; NM_007910.2.
DR AlphaFoldDB; O08542; -.
DR SMR; O08542; -.
DR IntAct; O08542; 2.
DR MINT; O08542; -.
DR STRING; 10090.ENSMUSP00000029674; -.
DR GlyConnect; 2292; 1 N-Linked glycan (1 site).
DR GlyGen; O08542; 2 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; O08542; -.
DR PaxDb; O08542; -.
DR PRIDE; O08542; -.
DR ProteomicsDB; 277768; -.
DR Antibodypedia; 34875; 293 antibodies from 29 providers.
DR DNASU; 13639; -.
DR Ensembl; ENSMUST00000029674; ENSMUSP00000029674; ENSMUSG00000028040.
DR GeneID; 13639; -.
DR KEGG; mmu:13639; -.
DR UCSC; uc008pys.1; mouse.
DR CTD; 1945; -.
DR MGI; MGI:106643; Efna4.
DR VEuPathDB; HostDB:ENSMUSG00000028040; -.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00940000162071; -.
DR HOGENOM; CLU_081598_3_0_1; -.
DR InParanoid; O08542; -.
DR OMA; VCCKESR; -.
DR OrthoDB; 1094764at2759; -.
DR PhylomeDB; O08542; -.
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; 13639; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Efna4; mouse.
DR PRO; PR:O08542; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O08542; protein.
DR Bgee; ENSMUSG00000028040; Expressed in maxillary prominence and 119 other tissues.
DR ExpressionAtlas; O08542; baseline and differential.
DR Genevisible; O08542; 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; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..175
FT /note="Ephrin-A4"
FT /id="PRO_0000008375"
FT PROPEP 176..206
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008376"
FT DOMAIN 26..158
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..43
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT LIPID 175
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 86..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT CONFLICT 1..4
FT /note="MRLL -> MLLRLGLIYPPTRPPAPPGPLV (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 22861 MW; 43501971DD1C6EA5 CRC64;
MRLLPLLRTV LWAALLGSRL PGCSSLRHPI YWNSSNPRLL RGDAVVELGF NDYLDIFCPH
YESPGPPEGP ETFALYMVDW SGYEACTAEG ANAFQRWNCS MPFAPFSPVR FSEKIQRYTP
FPLGFEFLPG ETYYYISVPT PESPGRCLRL QVSVCCKESG SSHESAHPVG SPGESGTSGW
RGGHAPSPLC LLLLLLLPIL RLLRVL
