EFNA1_RAT
ID EFNA1_RAT Reviewed; 205 AA.
AC P97553; Q6NS29;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ephrin-A1;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 1;
DE Short=LERK-1;
DE AltName: Full=Immediate early response protein B61;
DE Contains:
DE RecName: Full=Ephrin-A1, secreted form;
DE Flags: Precursor;
GN Name=Efna1; Synonyms=Epgl1, Lerk1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7675446;
RA Takahashi H., Ikeda T.;
RT "Molecular cloning and expression of rat and mouse B61 gene: implications
RT on organogenesis.";
RL Oncogene 11:879-883(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; D38056; BAA07242.1; -; mRNA.
DR EMBL; BC070514; AAH70514.1; -; mRNA.
DR RefSeq; NP_446051.2; NM_053599.2.
DR AlphaFoldDB; P97553; -.
DR SMR; P97553; -.
DR STRING; 10116.ENSRNOP00000027920; -.
DR GlyGen; P97553; 1 site.
DR PaxDb; P97553; -.
DR PRIDE; P97553; -.
DR GeneID; 94268; -.
DR KEGG; rno:94268; -.
DR UCSC; RGD:620388; rat.
DR CTD; 1942; -.
DR RGD; 620388; Efna1.
DR VEuPathDB; HostDB:ENSRNOG00000020573; -.
DR eggNOG; KOG3858; Eukaryota.
DR HOGENOM; CLU_081598_2_0_1; -.
DR InParanoid; P97553; -.
DR OMA; GQNSAMR; -.
DR OrthoDB; 1094764at2759; -.
DR PhylomeDB; P97553; -.
DR Reactome; R-RNO-2682334; EPH-Ephrin signaling.
DR Reactome; R-RNO-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
DR PRO; PR:P97553; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000020573; Expressed in lung and 19 other tissues.
DR Genevisible; P97553; RN.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; NAS:RGD.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0003199; P:endocardial cushion to mesenchymal transition involved in heart valve formation; ISO:RGD.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0003183; P:mitral valve morphogenesis; ISO:RGD.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:RGD.
DR GO; GO:1903051; P:negative regulation of proteolysis involved in protein catabolic process; ISO:RGD.
DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0014028; P:notochord formation; ISO:RGD.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:RGD.
DR GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0045765; P:regulation of angiogenesis; ISO:RGD.
DR GO; GO:0050770; P:regulation of axonogenesis; ISO:RGD.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
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 Angiogenesis; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Secreted; Signal;
KW Tumor suppressor.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..182
FT /note="Ephrin-A1"
FT /id="PRO_0000008357"
FT CHAIN 18..?
FT /note="Ephrin-A1, secreted form"
FT /id="PRO_0000389633"
FT PROPEP 183..205
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008358"
FT DOMAIN 18..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"
FT CONFLICT 18
FT /note="A -> V (in Ref. 1; BAA07242)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="T -> S (in Ref. 1; BAA07242)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="W -> V (in Ref. 1; BAA07242)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="A -> V (in Ref. 1; BAA07242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 205 AA; 23763 MW; E9ED3F73AE7FC4CA CRC64;
MEFLWAPLLG LCCSLAAADR HIVFWNSSNP KFREEDYTVH VQLNDYLDII CPHYEDDSVA
DAAMERYTLY MVEHQEYVTC EPQSKDQVRW KCNQPSAKHG PEKLSEKFQR FTPFTLGKEF
KEGHSYYYIS KPIYHQETQC LKLKVTVNGK ITHSPHAHAN PQEKRLQADD PEVQVLHSIG
HSAAPRLFPL VWAVLLLPLL LLQTQ
