ID A0A3Q3WLM3_MOLML Unreviewed; 338 AA.
AC A0A3Q3WLM3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ephrin RBD domain-containing protein {ECO:0000259|PROSITE:PS51551};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000018631.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000018631.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q3WLM3; -.
DR STRING; 94237.ENSMMOP00000018631; -.
DR Ensembl; ENSMMOT00000018932.1; ENSMMOP00000018631.1; ENSMMOG00000014110.1.
DR OMA; IYWNSMN; -.
DR Proteomes; UP000261620; 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 Reference proteome {ECO:0000313|Proteomes:UP000261620};
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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..338
FT /note="Ephrin RBD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018542351"
FT TRANSMEM 225..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..171
FT /note="Ephrin RBD"
FT /evidence="ECO:0000259|PROSITE:PS51551"
FT REGION 176..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 96..160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 338 AA; 36613 MW; D2C3AE18FEE2EFD8 CRC64;
GGIVRVEMAC GGSGNGLRIL LMFLLDLLGT AASNMEPVYW NSLNERFRDD KGYVLYPQIG
DRLDLICPPL DTARSTPEYE FYKLYLVSSR EQADRCEVTG PPNIVLTCDE PNRERRFTIK
FQEFSPNLWG HEFKSMHDYY IIATSDGTRQ GLESLRGGVC ATQGMKVVLK VGQSPYGLAP
KKEPPAGRTT NRNPGGAGNS TQSRGPNSFG GEGGGENGPL QPSNIALIAG AAGGSAFLLL
VTTVICVVCY RRRHAKHSDT HHPPLSLSSL TSPKRGGGGG ISSSNNNGSE PSDIIIPLRT
SDSAYCPHYE KVSGDYGHPV YIVQEMPPQS PANIYYKV
//
