ID EFNA1_PIG Reviewed; 205 AA.
AC Q06AS9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 08-NOV-2023, entry version 82.
DE RecName: Full=Ephrin-A1;
DE Contains:
DE RecName: Full=Ephrin-A1, secreted form;
DE Flags: Precursor;
GN Name=EFNA1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Liu G.Y.;
RL Submitted (AUG-2006) 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 Plays an important role in angiogenesis and tumor neovascularization.
CC The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by
CC phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase
CC activation and vascular endothelial cell migration and assembly. Exerts
CC anti-oncogenic effects in tumor cells through activation and down-
CC regulation of EPHA2. Activates EPHA2 by inducing tyrosine
CC phosphorylation which leads to its internalization and degradation.
CC Acts as a negative regulator in the tumorigenesis of gliomas by down-
CC regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal
CC growth cone and regulates dendritic spine morphogenesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Homodimer. Forms heterodimers with EPHA2. Binds to
CC the receptor tyrosine kinases EPHA2, EPHA3, EPHA4, EPHA5, EPHA6 and
CC EPHA7. Also binds with low affinity to EPHA1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20827};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P20827}.
CC -!- SUBCELLULAR LOCATION: [Ephrin-A1, secreted form]: Secreted
CC {ECO:0000250|UniProtKB:P20827}.
CC -!- PTM: Undergoes proteolysis by a metalloprotease to give rise to a
CC soluble monomeric form. {ECO:0000250}.
CC -!- PTM: N-Glycosylation is required for binding to EPHA2 receptor and
CC inducing its internalization. {ECO:0000250|UniProtKB:P20827}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; DQ917646; ABI97191.1; -; mRNA.
DR RefSeq; NP_001116582.1; NM_001123110.1.
DR AlphaFoldDB; Q06AS9; -.
DR SMR; Q06AS9; -.
DR STRING; 9823.ENSSSCP00000006959; -.
DR GlyCosmos; Q06AS9; 1 site, No reported glycans.
DR PaxDb; 9823-ENSSSCP00000006959; -.
DR PeptideAtlas; Q06AS9; -.
DR GeneID; 100144501; -.
DR KEGG; ssc:100144501; -.
DR CTD; 1942; -.
DR eggNOG; KOG3858; Eukaryota.
DR InParanoid; Q06AS9; -.
DR OrthoDB; 2881104at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
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; 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:SF19; EPHRIN-A1; 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 Angiogenesis; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Secreted; Signal;
KW Tumor suppressor.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..182
FT /note="Ephrin-A1"
FT /id="PRO_0000288608"
FT CHAIN 19..?
FT /note="Ephrin-A1, secreted form"
FT /id="PRO_0000389632"
FT PROPEP 183..205
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000288609"
FT DOMAIN 19..151
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT LIPID 182
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 80..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 205 AA; 23745 MW; 91D08A935741D56C CRC64;
MEFLWAPLLG LCCSLAAADR HTVFWNSSEP KFWNEDYTVH VRLNDYLDII CPHYEDDSVA
EAAMERYTLY LVEREQYQLC QPQSKDQVRW QCNQPNARHG PEKLSEKFQR FTPFTLGKEF
KEGHSYYYIS KPIHHQEDQC LKLKVTVSGK ITHSPQAHAN PQEKRLPADD PEVQVLHSIG
HSAAPRLSPL AWAVLLLPFL LLQTS
//
