ID   EFNA2_CHICK             Reviewed;         200 AA.
AC   P52802;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
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   Flags: Precursor;
GN   Name=EFNA2; Synonyms=ELF1, EPLG6, LERK6;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7634327; DOI=10.1016/0092-8674(95)90426-3;
RA   Cheng H.J., Nakamoto M., Bergemann A.D., Flanagan J.G.;
RT   "Complementary gradients in expression and binding of ELF-1 and Mek4 in
RT   development of the topographic retinotectal projection map.";
RL   Cell 82:371-381(1995).
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 EPHA3, EPHA4 and EPHA5.
CC       Interacts with EPHA8; activates EPHA8 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in a gradient across the tectum being
CC       more strongly expressed at the posterior pole.
CC   -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00884}.
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DR   EMBL; L40932; AAC42229.1; -; mRNA.
DR   RefSeq; NP_990314.1; NM_204983.1.
DR   AlphaFoldDB; P52802; -.
DR   SMR; P52802; -.
DR   GeneID; 395831; -.
DR   KEGG; gga:395831; -.
DR   CTD; 1943; -.
DR   VEuPathDB; HostDB:geneid_395831; -.
DR   InParanoid; P52802; -.
DR   OrthoDB; 1094764at2759; -.
DR   PhylomeDB; P52802; -.
DR   PRO; PR:P52802; -.
DR   Proteomes; UP000000539; Unplaced.
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:0046849; P:bone remodeling; 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; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..175
FT                   /note="Ephrin-A2"
FT                   /id="PRO_0000008365"
FT   PROPEP          176..200
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000008366"
FT   DOMAIN          28..161
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   LIPID           175
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        61..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   DISULFID        89..150
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ   SEQUENCE   200 AA;  23049 MW;  8FAB1AE5E45EED96 CRC64;
     MPRWEAAALL AAIVGVCVWS DDPGKVISDR YAVYWNRSNP RFHRGDYTVE VSINDYLDIY
     CPHYEEPLPA ERMERYVLYM VNYEGHASCD HRQKGFKRWE CNRPDSPSGP LKFSEKFQLF
     TPFSLGFEFR PGHEYYYISA SPLNVVDRPC LKLKVYVRPT NDSLYESPEP IFTSNNSCCS
     LAVPRAVLVA APVFWTLLGS