ID A0A3Q3MDX6_9TELE Unreviewed; 202 AA.
AC A0A3Q3MDX6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Ephrin-A4-like {ECO:0000313|Ensembl:ENSMAMP00000020986.2};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000020986.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000020986.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-
CC anchor, GPI-anchor {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 AlphaFoldDB; A0A3Q3MDX6; -.
DR STRING; 205130.ENSMAMP00000020986; -.
DR Ensembl; ENSMAMT00000021527.2; ENSMAMP00000020986.2; ENSMAMG00000014099.2.
DR GeneTree; ENSGT00940000160040; -.
DR InParanoid; A0A3Q3MDX6; -.
DR Proteomes; UP000261640; Unplaced.
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:SF42; EPHRIN-A4; 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:UP000261640};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..164
FT /note="Ephrin RBD"
FT /evidence="ECO:0000259|PROSITE:PS51551"
SQ SEQUENCE 202 AA; 22782 MW; 71A73F22A846AE7D CRC64;
MGSPLWTPAA LTTWKVTIFL FNIISAAVAK RHVVYWNSTN TRLTAGDLSI QVNLNDYLDI
YCPYYPNKEI LGPGQPETLA LFLVGEAYFQ GCVETRRAIK RWECNTPYAP FGPVRFSEKI
QRFTPFSLGF EFLPGQHYYY SSLPADEGPP LPCMKLRVTV CCEPTSGESK QKQETALRSS
AYSLRTASPT LLFILTLFLL TT
//
