EFNA5_RAT
ID EFNA5_RAT Reviewed; 228 AA.
AC P97605;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Ephrin-A5;
DE AltName: Full=AL-1;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 7;
DE Short=LERK-7;
DE Flags: Precursor;
GN Name=Efna5; Synonyms=Eplg7, Lerk7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley;
RX PubMed=7748564; DOI=10.1016/0896-6273(95)90335-6;
RA Winslow J.W., Moran P., Valverde J., Shih A., Yuan J.Q., Wong S.C.,
RA Tsai S.P., Goddard A., Henzel W.J., Hefti F., Beck K.D., Caras I.W.;
RT "Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor
RT involved in axon bundle formation.";
RL Neuron 14:973-981(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Li Y.Y., McTiernan C.F., Feldman A.M.;
RT "rLERK7, rat ligand for Eph-related receptor tyrosine kinase.";
RL Submitted (MAR-1998) 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. Induces compartmentalized
CC signaling within a caveolae-like membrane microdomain when bound to the
CC extracellular domain of its cognate receptor. This signaling event
CC requires the activity of the Fyn tyrosine kinase. Activates the EPHA3
CC receptor to regulate cell-cell adhesion and cytoskeletal organization.
CC With the receptor EPHA2 may regulate lens fiber cells shape and
CC interactions and be important for lens transparency maintenance. May
CC function actively to stimulate axon fasciculation. The interaction of
CC EFNA5 with EPHA5 also mediates communication between pancreatic islet
CC cells to regulate glucose-stimulated insulin secretion.
CC Cognate/functional ligand for EPHA7, their interaction regulates brain
CC development modulating cell-cell adhesion and repulsion (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the receptor tyrosine kinases EPHA2, EPHA3, EPHB1 and
CC EPHB2. Interacts with EPHA8; activates EPHA8. Forms a ternary EFNA5-
CC EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by
CC ADAM10 which regulates the EFNA5-EPHA3 complex internalization and
CC function (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Membrane, caveola {ECO:0000250}; Lipid-anchor,
CC GPI-anchor {ECO:0000250}. Note=Compartmentalized in discrete caveolae-
CC like membrane microdomains. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, placenta and lung.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; U69279; AAC05801.1; -; mRNA.
DR RefSeq; NP_446355.1; NM_053903.1.
DR AlphaFoldDB; P97605; -.
DR SMR; P97605; -.
DR GlyGen; P97605; 1 site.
DR PhosphoSitePlus; P97605; -.
DR PaxDb; P97605; -.
DR GeneID; 116683; -.
DR KEGG; rno:116683; -.
DR UCSC; RGD:620391; rat.
DR CTD; 1946; -.
DR RGD; 620391; Efna5.
DR eggNOG; KOG3858; Eukaryota.
DR InParanoid; P97605; -.
DR OrthoDB; 1094764at2759; -.
DR PhylomeDB; P97605; -.
DR Reactome; R-RNO-2682334; EPH-Ephrin signaling.
DR Reactome; R-RNO-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
DR PRO; PR:P97605; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045499; F:chemorepellent activity; ISO:RGD.
DR GO; GO:0046875; F:ephrin receptor binding; IDA:RGD.
DR GO; GO:0005169; F:neurotrophin TRKB receptor binding; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007413; P:axonal fasciculation; NAS:RGD.
DR GO; GO:0007420; P:brain development; IMP:RGD.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; ISO:RGD.
DR GO; GO:1904322; P:cellular response to forskolin; ISO:RGD.
DR GO; GO:0007417; P:central nervous system development; NAS:RGD.
DR GO; GO:0048668; P:collateral sprouting; ISO:RGD.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISO:RGD.
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:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISO:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:RGD.
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; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Neurogenesis; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..203
FT /note="Ephrin-A5"
FT /id="PRO_0000008381"
FT PROPEP 204..228
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008382"
FT DOMAIN 29..162
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT REGION 186..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 203
FT /note="GPI-anchor amidated asparagine"
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; 26358 MW; 855985532D580022 CRC64;
MLHVEMLTLL FLVLWMCVFS QDPGSKVVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV
FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL
FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV RDRVFDVNDK
VENSLEPADD TVHESAEPSR GENAAQTPRI PSRLLAILLF LLAMLLTL
