ID A0A3P8QEC0_ASTCA Unreviewed; 230 AA.
AC A0A3P8QEC0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Ephrin-A4-like {ECO:0000313|Ensembl:ENSACLP00000027885.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000027885.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000027885.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000027885.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3P8QEC0; -.
DR STRING; 8154.ENSACLP00000027885; -.
DR Ensembl; ENSACLT00000028536.1; ENSACLP00000027885.1; ENSACLG00000018915.1.
DR GeneTree; ENSGT00940000162071; -.
DR Proteomes; UP000265100; Chromosome 11.
DR Bgee; ENSACLG00000018915; Expressed in anal fin and 4 other cell types or tissues.
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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 29..164
FT /note="Ephrin RBD"
FT /evidence="ECO:0000259|PROSITE:PS51551"
SQ SEQUENCE 230 AA; 25535 MW; 68CB384845B80265 CRC64;
LQISVVGVQK KAGEKTTIVF FNIISAVVAK RHTVFWNSTN TRLTAGDLSV QLNFNDYLDI
HCPHYPNEEA VGHGQPETLA LYLVGEESFQ GCVETRGAIK RWECNTPFAP YGPVRFSEKI
QRFTPFSLGF EFLPGRHYYY SSLPTDEGPP LPCMKLRVTV CCQCLTRPPP DSPTPPPQTP
PHSTSPIFPV FSLSLCCISI STVIHRLPVF PFLFFAPSLS RTRCAASALG
//
