ID G7NV61_MACFA Unreviewed; 489 AA.
AC G7NV61;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Ephrin-A1 {ECO:0000256|ARBA:ARBA00040413};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000040666.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000040666.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000040666.2}
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}.
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 AlphaFoldDB; G7NV61; -.
DR STRING; 9541.ENSMFAP00000040666; -.
DR Ensembl; ENSMFAT00000014934.2; ENSMFAP00000040666.2; ENSMFAG00000041110.2.
DR VEuPathDB; HostDB:ENSMFAG00000041110; -.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00940000159919; -.
DR OrthoDB; 2881104at2759; -.
DR Proteomes; UP000233100; Chromosome 1.
DR Bgee; ENSMFAG00000041110; Expressed in liver and 13 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:InterPro.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:InterPro.
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:UP000233100};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 324..463
FT /note="Ephrin RBD"
FT /evidence="ECO:0000259|PROSITE:PS51551"
FT REGION 107..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 53774 MW; F8651C955A479A4C CRC64;
MPRFSQSIFK SPFARCTRVL SHILRSSVPF NVSKTRTDPS RAQGPACRSC AQALMGWTEA
PLAPAAHVTH SITHSVALYS RHLGDDTISR TKTTLTNRTK TNSRMCVGRG SRAQSPGRGW
GRRRGWERGR PSLGMRGSER CGACQQPRTL QGPRAEQQSR VPYPRVRRLA LASSSLLPHA
TAPRDASPPP GQAYKAPRRP TSERTHSSEQ ICRGRGARFA LSCTPSLLAS PARPSSTSPA
PKPRGSCAPG GARAGGVSGG AGPKAESQGE GARSVSPTLT SPRRKPAGTQ TPRSPASPPG
LARPRAMEFL WAPLLGLCCS LAAADRHTVF WNSSNPKFRN EDYTIHVQLN DYVDIICPHY
EDHSVADAAM ERYILYLVER EEYQLCQPQS KDQVRWQCNR PSAKHGPEKL SEKFQRFTPF
TLGKEFKEGH SYYYISHSPQ AHDNPQEKRL AADDPEVRVL HSIGHSAAPR LFPLAWTVLL
LPLLLLQTP
//
