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 27-MAR-2024, entry version 108.
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 STRING; 9031.ENSGALP00000045853; -.
DR GlyCosmos; P52802; 3 sites, No reported glycans.
DR GeneID; 395831; -.
DR KEGG; gga:395831; -.
DR CTD; 1943; -.
DR VEuPathDB; HostDB:geneid_395831; -.
DR InParanoid; P52802; -.
DR OMA; CPHYEIP; -.
DR OrthoDB; 2881104at2759; -.
DR PhylomeDB; P52802; -.
DR PRO; PR:P52802; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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; Cupredoxins - blue copper proteins; 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; EPHRIN; 1.
DR PANTHER; PTHR11304:SF4; EPHRIN-A2; 1.
DR Pfam; PF00812; Ephrin; 1.
DR PRINTS; PR01347; EPHRIN.
DR SUPFAM; SSF49503; Cupredoxins; 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
//
