EFNA5_DANRE
ID EFNA5_DANRE Reviewed; 228 AA.
AC P79728;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ephrin-A5b;
DE AltName: Full=AL-1;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 7;
DE Short=LERK-7;
DE AltName: Full=ZfEPHL4;
DE Flags: Precursor;
GN Name=efna5b; Synonyms=al1, efna5, eplg7, lerk7;
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).
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 Induces compartmentalized signaling within a caveolae-like membrane
CC microdomain when bound to the extracellular domain of its cognate
CC receptor. This signaling event requires the activity of the Fyn
CC tyrosine kinase. Activates the epha3 receptor to regulate cell-cell
CC adhesion and cytoskeletal organization. With the receptor epha2 may
CC regulate lens fiber cells shape and interactions and be important for
CC lens transparency maintenance. May function actively to stimulate axon
CC fasciculation (By similarity). Controls axon growth and may be involved
CC in the creation of the retino-tectal map. {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, strongly
CC expressed in the midbrain caudal to the presumptive tectum. At later
CC stages, maintained at the posterior margin of the tectum.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; Y09669; CAA70864.1; -; mRNA.
DR RefSeq; NP_571101.1; NM_131026.2.
DR AlphaFoldDB; P79728; -.
DR SMR; P79728; -.
DR STRING; 7955.ENSDARP00000092347; -.
DR PaxDb; P79728; -.
DR DNASU; 30223; -.
DR GeneID; 30223; -.
DR KEGG; dre:30223; -.
DR CTD; 30223; -.
DR ZFIN; ZDB-GENE-980526-186; efna5b.
DR eggNOG; KOG3858; Eukaryota.
DR InParanoid; P79728; -.
DR OrthoDB; 1094764at2759; -.
DR PhylomeDB; P79728; -.
DR Reactome; R-DRE-2682334; EPH-Ephrin signaling.
DR Reactome; R-DRE-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-DRE-3928665; EPH-ephrin mediated repulsion of cells.
DR PRO; PR:P79728; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0007509; P:mesoderm migration involved in gastrulation; IMP:ZFIN.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
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; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Neurogenesis;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..204
FT /note="Ephrin-A5b"
FT /id="PRO_0000008385"
FT PROPEP 205..228
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008386"
FT DOMAIN 29..162
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT REGION 184..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 204
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 90..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 228 AA; 26595 MW; 74B3406C05418E6E CRC64;
MLQAEMIVFV GVILWMCVFS QEPSSKVMAD RYAVFWNRTN PRFQRGDYHI DVCINDYLDV
YCPHYEDSVP EERTERYVLY MVNYDGYSTC DHTAKGFKRW ECNRPHSPNG PLKFSEKFQL
FTPFSLGFEF RPGREYYYIS SMITETGRRS CLKLKVFVRP PNGCEKTIGV HDRVFVDDKV
DNALEPRDDT SHEAEPSRSD VSTSGLRHQT SRPLLALLLL CISLYLLL
