ID A0A3B3Q5W4_9TELE Unreviewed; 329 AA.
AC A0A3B3Q5W4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Ephrin-B3-like {ECO:0000313|Ensembl:ENSPKIP00000001548.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000001548.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000001548.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A3B3Q5W4; -.
DR STRING; 1676925.ENSPKIP00000001548; -.
DR Ensembl; ENSPKIT00000025469.1; ENSPKIP00000001548.1; ENSPKIG00000019805.1.
DR GeneTree; ENSGT00940000160323; -.
DR OrthoDB; 5402021at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR019765; Ephrin_CS.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; EPHRIN; 1.
DR PANTHER; PTHR11304:SF34; EPHRIN-B3; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004375};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..329
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017422258"
FT TRANSMEM 217..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..168
FT /note="Ephrin RBD"
FT /evidence="ECO:0000259|PROSITE:PS51551"
FT REGION 173..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 93..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 329 AA; 35479 MW; 7DD8DA77B104A192 CRC64;
MATPARHGAS NLSLLAVFLM DILGISATNM EPIYWNSLNK RFTDSRGYIL YPQIGDRLDL
ICPGSDRPGP LAPAEYEYYK LYLLSSREQA EHCEVTGTPN LLLTCDKPSS DTRFTIKFQE
FSPNLWGHEF KTMQDYYIIA TSDGTRQGLD SMRGGVCLTQ GMKVVLKVGQ NPYGLPPKPA
KPDSGQPYSR KPGAPGNSSL AEGAAEGENG PLSHSNVALI AGAAGGSACV LLASAVLCVV
CYRRRRSKPS ESRHPPLSLS SLASPKRGGG AIAAGNNNGS EPSDIIIPLR APDSAYCPHY
EKVSGDYGHP VYIVQEMPPQ NPANIYYKV
//
