ID A0A2K6CQ76_MACNE Unreviewed; 205 AA.
AC A0A2K6CQ76;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Ephrin-A1 {ECO:0000256|ARBA:ARBA00040413};
GN Name=EFNA1 {ECO:0000313|Ensembl:ENSMNEP00000025767.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000025767.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000025767.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00037186}.
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.
CC {ECO:0000256|ARBA:ARBA00038586}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00884, ECO:0000256|RuleBase:RU004375}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00884}.
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DR RefSeq; XP_011767991.1; XM_011769689.1.
DR AlphaFoldDB; A0A2K6CQ76; -.
DR STRING; 9545.ENSMNEP00000025767; -.
DR Ensembl; ENSMNET00000050043.1; ENSMNEP00000025767.1; ENSMNEG00000036345.1.
DR GeneID; 105497996; -.
DR KEGG; mni:105497996; -.
DR CTD; 1942; -.
DR GeneTree; ENSGT00940000159919; -.
DR OMA; HYTHEEV; -.
DR OrthoDB; 2881104at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000036345; Expressed in liver and 12 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
DR GO; GO:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0003199; P:endocardial cushion to mesenchymal transition involved in heart valve formation; IEA:Ensembl.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0003183; P:mitral valve morphogenesis; IEA:Ensembl.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:1903051; P:negative regulation of proteolysis involved in protein catabolic process; IEA:Ensembl.
DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0014028; P:notochord formation; IEA:Ensembl.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0045765; P:regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004375};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..205
FT /note="Ephrin-A1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014333630"
FT DOMAIN 18..155
FT /note="Ephrin RBD"
FT /evidence="ECO:0000259|PROSITE:PS51551"
SQ SEQUENCE 205 AA; 23852 MW; F0D19927E19E4E2F CRC64;
MEFLWAPLLG LCCSLAAADR HTVFWNSSNP KFRNEDYTIH VQLNDYVDII CPHYEDHSVA
DAAMERYILY LVEREEYQLC QPQSKDQVRW QCNRPSAKHG PEKLSEKFQR FTPFTLGKEF
KEGHSYYYIS KPIHQQEDRC LRLKVTVNGK ITHSPQAHDN PQEKRLAADD PEVRVLHSIG
HSAAPRLFPL AWTVLLLPLL LLQTP
//
