ID A0A3Q0SM91_AMPCI Unreviewed; 329 AA.
AC A0A3Q0SM91;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Ephrin-B2a {ECO:0000313|Ensembl:ENSACIP00000024027.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000024027.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000024027.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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; A0A3Q0SM91; -.
DR STRING; 61819.ENSACIP00000024027; -.
DR Ensembl; ENSACIT00000024663.1; ENSACIP00000024027.1; ENSACIG00000018664.1.
DR GeneTree; ENSGT00940000155868; -.
DR OMA; GSTRHND; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046875; F:ephrin receptor binding; IEA:InterPro.
DR GO; GO:0035475; P:angioblast cell migration involved in selective angioblast sprouting; IEA:Ensembl.
DR GO; GO:0007412; P:axon target recognition; IEA:Ensembl.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:InterPro.
DR GO; GO:0003404; P:optic vesicle morphogenesis; IEA:Ensembl.
DR GO; GO:0021654; P:rhombomere boundary formation; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0008039; P:synaptic target recognition; IEA:Ensembl.
DR CDD; cd10426; Ephrin-B_Ectodomain; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 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; EPHRIN; 1.
DR PANTHER; PTHR11304:SF18; EPHRIN-B2; 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 Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00884}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004375};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 218..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..171
FT /note="Ephrin RBD"
FT /evidence="ECO:0000259|PROSITE:PS51551"
FT REGION 172..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 96..160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 329 AA; 36442 MW; CF794AC3FB0A7866 CRC64;
LAGLKARRLT MGDSMWRYYF GVLFIAFKVD LCRALILESI YWNTTNTKFV PGQGVVLYPQ
IGDKLDIVCP RVDGGVGEGV EYYKVYMVPR EQLESCTITK ADTPLLNCVK PDQDVKFTLK
FQEFSPNLWG LEFFRGKDYY IISTSNGTME GIDNQEGGVC KTKSMKIIMK VGQNPSDPVS
PKDPTRVPHP PPHPFDKDPN NPNEVSDGKS SSVMGSEAAI FVAIASGSVI LIIIIVVLVL
LLLKYRRRHR KHSPQHAATL SLSTLATPKR SGGGGNNNGS EPSDIIIPLR TADSVFCPHY
EKVSGDYGHP VYIVQEMPPQ SPANIYYKV
//