EFNA2_MOUSE
ID EFNA2_MOUSE Reviewed; 209 AA.
AC P52801;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ephrin-A2;
DE AltName: Full=CEK7-ligand;
DE Short=CEK7-L;
DE AltName: Full=ELF-1;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 6;
DE Short=LERK-6;
DE Flags: Precursor;
GN Name=Efna2; Synonyms=Elf1, Epl6, Eplg6, Lerk6;
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].
RC STRAIN=Swiss Webster; TISSUE=Brain;
RX PubMed=7522971; DOI=10.1016/0092-8674(94)90408-1;
RA Cheng H.J., Flanagan J.G.;
RT "Identification and cloning of ELF-1, a developmentally expressed ligand
RT for the Mek4 and Sek receptor tyrosine kinases.";
RL Cell 79:157-168(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7876076; DOI=10.1074/jbc.270.8.3467;
RA Shao H., Lou L., Pandey A., Verderame M.F., Siever D.A., Dixit V.M.;
RT "cDNA cloning and characterization of a Cek7 receptor protein-tyrosine
RT kinase ligand that is identical to the ligand (ELF-1) for the Mek-4 and Sek
RT receptor protein-tyrosine kinases.";
RL J. Biol. Chem. 270:3467-3470(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 [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 FUNCTION IN BONE REMODELING.
RX PubMed=19299512; DOI=10.1074/jbc.m807598200;
RA Irie N., Takada Y., Watanabe Y., Matsuzaki Y., Naruse C., Asano M.,
RA Iwakura Y., Suda T., Matsuo K.;
RT "Bidirectional signaling through ephrinA2-EphA2 enhances osteoclastogenesis
RT and suppresses osteoblastogenesis.";
RL J. Biol. Chem. 284:14637-14644(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. With the EPHA2 receptor may
CC play a role in bone remodeling through regulation of osteoclastogenesis
CC and osteoblastogenesis. {ECO:0000269|PubMed:19299512,
CC ECO:0000269|PubMed:9053851}.
CC -!- SUBUNIT: Binds to the receptor tyrosine kinases EPHA3, EPHA4 and EPHA5.
CC Interacts with EPHA8; activates EPHA8. {ECO:0000269|PubMed:9053851}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in myogenic progenitor cells.
CC {ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: In myogenic progenitor cells, highly expressed, at
CC least as early as 11.5 dpc, expression decreases gradually until
CC adulthood. {ECO:0000269|PubMed:27446912}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; U14941; AAA53636.1; -; mRNA.
DR EMBL; U14752; AAA68520.1; -; mRNA.
DR EMBL; BC048697; AAH48697.1; -; mRNA.
DR CCDS; CCDS24013.1; -.
DR PIR; A54984; A54984.
DR RefSeq; NP_031935.3; NM_007909.3.
DR AlphaFoldDB; P52801; -.
DR SMR; P52801; -.
DR STRING; 10090.ENSMUSP00000003154; -.
DR GlyGen; P52801; 3 sites.
DR PhosphoSitePlus; P52801; -.
DR PaxDb; P52801; -.
DR PRIDE; P52801; -.
DR ProteomicsDB; 277800; -.
DR Antibodypedia; 3919; 414 antibodies from 31 providers.
DR DNASU; 13637; -.
DR Ensembl; ENSMUST00000003154; ENSMUSP00000003154; ENSMUSG00000003070.
DR GeneID; 13637; -.
DR KEGG; mmu:13637; -.
DR UCSC; uc007gcg.2; mouse.
DR CTD; 1943; -.
DR MGI; MGI:102707; Efna2.
DR VEuPathDB; HostDB:ENSMUSG00000003070; -.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00940000160040; -.
DR HOGENOM; CLU_081598_3_1_1; -.
DR InParanoid; P52801; -.
DR OMA; NPRFFRG; -.
DR OrthoDB; 1094764at2759; -.
DR PhylomeDB; P52801; -.
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; 13637; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Efna2; mouse.
DR PRO; PR:P52801; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P52801; protein.
DR Bgee; ENSMUSG00000003070; Expressed in floor plate of midbrain and 207 other tissues.
DR Genevisible; P52801; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
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:0046849; P:bone remodeling; IDA:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0021772; P:olfactory bulb development; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IDA:UniProtKB.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..184
FT /note="Ephrin-A2"
FT /id="PRO_0000008363"
FT PROPEP 185..209
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008364"
FT DOMAIN 30..170
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT LIPID 184
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 98..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 209 AA; 23586 MW; F1997545F25B9ABC CRC64;
MAPAQRPLLP LLLLLLPLRA RNEDPARANA DRYAVYWNRS NPRFQVSAVG DGGGYTVEVS
INDYLDIYCP HYGAPLPPAE RMERYILYMV NGEGHASCDH RQRGFKRWEC NRPAAPGGPL
KFSEKFQLFT PFSLGFEFRP GHEYYYISAT PPNLVDRPCL RLKVYVRPTN ETLYEAPEPI
FTSNSSCSGL GGCHLFLTTV PVLWSLLGS
