ID A0A3Q2UXX3_HAPBU Unreviewed; 221 AA.
AC A0A3Q2UXX3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ephrin-A3-like {ECO:0000313|Ensembl:ENSHBUP00000002824.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000002824.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000002824.1}
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 RefSeq; XP_005936141.1; XM_005936079.1.
DR RefSeq; XP_014193508.1; XM_014338022.1.
DR STRING; 8153.ENSHBUP00000002817; -.
DR Ensembl; ENSHBUT00000011416.1; ENSHBUP00000002817.1; ENSHBUG00000004048.1.
DR Ensembl; ENSHBUT00000011423.1; ENSHBUP00000002824.1; ENSHBUG00000004048.1.
DR GeneID; 102311097; -.
DR CTD; 117506; -.
DR GeneTree; ENSGT00940000161355; -.
DR OMA; VYICCST; -.
DR OrthoDB; 2881104at2759; -.
DR Proteomes; UP000264840; 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:SF5; EPHRIN-A3; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00884}; 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:UP000264840};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..221
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041089113"
FT DOMAIN 24..156
FT /note="Ephrin RBD"
FT /evidence="ECO:0000259|PROSITE:PS51551"
FT DISULFID 57..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 221 AA; 25375 MW; AE8545CCD03C9CBF CRC64;
MALVALSLWV LISLTWANLL QVSANRHTVY WNSSNIHLRR EGYTMQVNVN DYLDIYCPHY
NDSQRMVGTG EQYVLYMVSY RGYRSCDPQM GFKRWECNRP HAPHAPIKFS EKFQRYSAFS
LGYEFHVGQE YYYISTPTHH HGRACLRLRV YVCCSTASDV DDEPGPTDGV YTLRPGLKID
ELAEFNPVIP KLEKSVSGSS PSRDRLLLTV TMLFLAALCI S
//
