EFNA2_DANRE
ID EFNA2_DANRE Reviewed; 195 AA.
AC P79727; Q4V9Q0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ephrin-A2;
DE AltName: Full=ELF-1;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 6;
DE Short=LERK-6;
DE AltName: Full=ZfEPHL3;
DE Flags: Precursor;
GN Name=efna2; Synonyms=eplg6, lerk6;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9043080; DOI=10.1242/dev.124.3.655;
RA Brennan C., Monschau B., Lindberg R., Guthrie B., Drescher U.,
RA Bonhoeffer F., Holder N.;
RT "Two Eph receptor tyrosine kinase ligands control axon growth and may be
RT involved in the creation of the retinotectal map in the zebrafish.";
RL Development 124:655-664(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the receptor tyrosine kinases epha2, epha3, epha4 and
CC epha5. Interacts with epha8; activates epha8 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widespread expression in the embryo.
CC -!- DEVELOPMENTAL STAGE: Expressed in the presumptive midbrain of
CC developing embryos from the six-somite stage. By 24 hours, expressed
CC throughout the midbrain including the region of the presumptive tectum.
CC At later stages, expressed in a graded fashion throughout the tectum.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; Y09668; CAA70863.1; -; mRNA.
DR EMBL; BC096783; AAH96783.1; -; mRNA.
DR RefSeq; NP_571097.1; NM_131022.2.
DR AlphaFoldDB; P79727; -.
DR SMR; P79727; -.
DR STRING; 7955.ENSDARP00000040277; -.
DR PaxDb; P79727; -.
DR Ensembl; ENSDART00000040278; ENSDARP00000040277; ENSDARG00000031372.
DR GeneID; 30218; -.
DR KEGG; dre:30218; -.
DR CTD; 30218; -.
DR ZFIN; ZDB-GENE-990415-66; efna2a.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00940000160040; -.
DR HOGENOM; CLU_081598_3_1_1; -.
DR InParanoid; P79727; -.
DR OMA; MMLCQLG; -.
DR OrthoDB; 1094764at2759; -.
DR PhylomeDB; P79727; -.
DR PRO; PR:P79727; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000031372; Expressed in midbrain and 27 other tissues.
DR ExpressionAtlas; P79727; baseline.
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; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030316; P:osteoclast differentiation; 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; 2.
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; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Neurogenesis;
KW Reference proteome; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..174
FT /note="Ephrin-A2"
FT /id="PRO_0000008367"
FT PROPEP 175..195
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008368"
FT DOMAIN 24..157
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT LIPID 174
FT /note="GPI-anchor amidated cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 85..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 195 AA; 22688 MW; 9EE284FEB61D0C42 CRC64;
MELSLVVFTV VCWVSVWSDD RIISDRHAVY WNSSNSRFWQ GEYTVAVSIN DYLDVYCPYY
ESPQPHSRME RYILFMVNHD GYLTCEHRMR GFKRWECNRP QSPDGPLRFS EKFQLFTPFS
LGFEFRPGHE YYYISSPHPN HAGKPCLKLK VYVKPTSSGY ESPEPFLTDQ SQRCGADGPC
LAVLMLLLVF LLAGV
