EFNB2_DANRE
ID EFNB2_DANRE Reviewed; 332 AA.
AC O73874;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ephrin-B2a;
DE Flags: Precursor;
GN Name=efnb2a; Synonyms=efnb2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9765210; DOI=10.1101/gad.12.19.3096;
RA Durbin L., Brennan C., Shiomi K., Cooke J., Barrios A., Shanmugalingam S.,
RA Guthrie B., Lindberg R., Holder N.;
RT "Eph signaling is required for segmentation and differentiation of the
RT somites.";
RL Genes Dev. 12:3096-3109(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11397014; DOI=10.1006/dbio.2001.0281;
RA Chan J., Mably J.D., Serluca F.C., Chen J.N., Goldstein N.B., Thomas M.C.,
RA Cleary J.A., Brennan C., Fishman M.C., Roberts T.M.;
RT "Morphogenesis of prechordal plate and notochord requires intact eph/ephrin
RT b signaling.";
RL Dev. Biol. 234:470-482(2001).
CC -!- FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family
CC of 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 The signaling pathway downstream of the receptor is referred to as
CC forward signaling while the signaling pathway downstream of the ephrin
CC ligand is referred to as reverse signaling. Together with ephb4 may
CC play a central role in heart morphogenesis and angiogenesis through
CC regulation of cell adhesion and cell migration (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds to the receptor tyrosine kinase ephb4.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P52799};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic
CC domain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; AJ004863; CAA06168.1; -; mRNA.
DR EMBL; AF375225; AAK64275.1; -; mRNA.
DR RefSeq; NP_571098.1; NM_131023.1.
DR AlphaFoldDB; O73874; -.
DR SMR; O73874; -.
DR STRING; 7955.ENSDARP00000010432; -.
DR PaxDb; O73874; -.
DR PRIDE; O73874; -.
DR Ensembl; ENSDART00000026011; ENSDARP00000010432; ENSDARG00000020164.
DR GeneID; 30219; -.
DR KEGG; dre:30219; -.
DR CTD; 30219; -.
DR ZFIN; ZDB-GENE-990415-67; efnb2a.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00940000155868; -.
DR HOGENOM; CLU_072080_0_0_1; -.
DR InParanoid; O73874; -.
DR OMA; GSTRHND; -.
DR OrthoDB; 903831at2759; -.
DR PhylomeDB; O73874; -.
DR Reactome; R-DRE-2682334; EPH-Ephrin signaling.
DR Reactome; R-DRE-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DRE-3928664; Ephrin signaling.
DR Reactome; R-DRE-3928665; EPH-ephrin mediated repulsion of cells.
DR SignaLink; O73874; -.
DR PRO; PR:O73874; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000020164; Expressed in immature eye and 71 other tissues.
DR ExpressionAtlas; O73874; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
DR GO; GO:0035475; P:angioblast cell migration involved in selective angioblast sprouting; IMP:ZFIN.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:ZFIN.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007412; P:axon target recognition; IDA:ZFIN.
DR GO; GO:0001568; P:blood vessel development; IGI:ZFIN.
DR GO; GO:0048514; P:blood vessel morphogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0003404; P:optic vesicle morphogenesis; IMP:ZFIN.
DR GO; GO:0050920; P:regulation of chemotaxis; ISS:UniProtKB.
DR GO; GO:0021654; P:rhombomere boundary formation; IGI:ZFIN.
DR GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
DR GO; GO:0008039; P:synaptic target recognition; IEP:ZFIN.
DR CDD; cd10426; Ephrin-B_Ectodomain; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR034255; Ephrin-B_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; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..332
FT /note="Ephrin-B2a"
FT /id="PRO_0000008394"
FT TOPO_DOM 25..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..161
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT REGION 162..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 330..332
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 184..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 86..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 332 AA; 36724 MW; 189ED82372C71C8B CRC64;
MGDSLWRYYF GVLVIACKVN LSRALILDSI YWNTTNTKFV PGQGLVLYPQ IGDKMDIVCP
RVEGGSMEGV EYYKLYMVPL EQLKSCQVTK ADTPLLNCVK PDQDVKFTLK FQEFSPNLWG
LEFFRGKDYY IISTSNGTME GLDNQEGGVC KTKSMKIIMK VGQNPSDPIS PKDYPTSYPP
KHPDLGGKDS KSNEVLKPDA SPHGEDKGDG NKSSSVIGSE VALFACIASA SVIVIIIIIM
LVFLLLKYRR RHRKHSPQHA TTLSLSTLAT PKRGGSGGNN NGSEPSDIII PLRTADSVFC
PHYEKVSGDY GHPVYIVQEM PPQSPANIYY KV
