ID   EFNA1_XENLA             Reviewed;         216 AA.
AC   P52794;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Ephrin-A1;
DE   AltName: Full=EPH-related receptor tyrosine kinase ligand 1;
DE            Short=LERK-1;
DE   AltName: Full=xELF-a;
DE   Flags: Precursor;
GN   Name=efna1; Synonyms=elf, epgl1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND A').
RX   PubMed=8843391; DOI=10.1016/0925-4773(96)00536-9;
RA   Weinstein D.C., Rahman S.M., Ruiz J.C., Hemmati-Brivanlou A.;
RT   "Embryonic expression of eph signalling factors in Xenopus.";
RL   Mech. Dev. 57:133-144(1996).
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   -!- SUBUNIT: Binds to the receptor tyrosine kinases EPHA2, EPHA4, EPHA5,
CC       EPHA6 and EPHA7. Also binds with low affinity to EPHA1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform A]: Membrane {ECO:0000250}; Lipid-
CC       anchor, GPI-anchor {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P52794-1; Sequence=Displayed;
CC       Name=A';
CC         IsoId=P52794-2; Sequence=VSP_001447;
CC   -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00884}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U31204; AAA74485.1; -; mRNA.
DR   EMBL; U31205; AAA74486.1; -; mRNA.
DR   RefSeq; NP_001081390.1; NM_001087921.1. [P52794-2]
DR   AlphaFoldDB; P52794; -.
DR   SMR; P52794; -.
DR   GeneID; 397809; -.
DR   KEGG; xla:397809; -.
DR   CTD; 397809; -.
DR   Xenbase; XB-GENE-6252357; efna1.S.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 397809; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046875; F:ephrin receptor binding; IEA:InterPro.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
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   Alternative splicing; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..195
FT                   /note="Ephrin-A1"
FT                   /id="PRO_0000008359"
FT   PROPEP          196..216
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000008360"
FT   DOMAIN          29..161
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   REGION          162..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           195
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        61..102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   VAR_SEQ         162..216
FT                   /note="TPPPVNVHTPRSHIQSDEPEVPLPGVMKSVAGNSAAPGTPCTLYGLLLAALL
FT                   LRL -> SE (in isoform A')"
FT                   /evidence="ECO:0000303|PubMed:8843391"
FT                   /id="VSP_001447"
SQ   SEQUENCE   216 AA;  24755 MW;  1B3A508E0A7B872E CRC64;
     MMELYRAAVQ LIVGVGLGVG LWLREAQGER HIVFWNSSNY RFMQEDYTVQ VQLNDYLDIV
     CPYYEEGSVA GHTVERYTLF LVDYEEYETC KPKSKDQVRW ECNKPFAPHG PEKFCEKFQK
     FTPFTLGTEF REGRTYYYIS KPIHYHGETC MRLRVHVSGR TTPPPVNVHT PRSHIQSDEP
     EVPLPGVMKS VAGNSAAPGT PCTLYGLLLA ALLLRL