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Database: UniProt
Entry: L5LSI9_MYODS
LinkDB: L5LSI9_MYODS
Original site: L5LSI9_MYODS 
ID   L5LSI9_MYODS            Unreviewed;       346 AA.
AC   L5LSI9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Ephrin-B1 {ECO:0000256|ARBA:ARBA00040452};
GN   ORFNames=MDA_GLEAN10002870 {ECO:0000313|EMBL:ELK29012.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK29012.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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   EMBL; KB108638; ELK29012.1; -; Genomic_DNA.
DR   RefSeq; XP_006765418.1; XM_006765355.1.
DR   AlphaFoldDB; L5LSI9; -.
DR   GeneID; 102774481; -.
DR   KEGG; myd:102774481; -.
DR   CTD; 1947; -.
DR   eggNOG; KOG3858; Eukaryota.
DR   OrthoDB; 5402021at2759; -.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046875; F:ephrin receptor binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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:SF17; EPHRIN-B1; 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   Reference proteome {ECO:0000313|Proteomes:UP000010556};
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..346
FT                   /note="Ephrin-B1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003970611"
FT   TRANSMEM        238..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..164
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51551"
FT   REGION          194..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        89..153
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00884"
SQ   SEQUENCE   346 AA;  37894 MW;  EA721FAB002622B6 CRC64;
     MARSGQLWLG KWLVAMVVLA LCRLATPLAK NLEPVSWSSL NPKFLSGKGL VIYPKIGDKL
     DIICPRAEAG RPYEYYKLYL VRPEQAAACS TVLDPNVLVT CNRPEQEIRF TIKFQEFSPN
     YMGLEFKKHH DYYITSTSNG SLEGLENREG GVCRTRTMKI IMKVGQDPNA VTPEQLTTSP
     PNKEADNTIK MATQAPGSRG SLGDSDGKHE TVNQEEKSGP GGSGGSSGDS DSFFNSKVAL
     FAAVGAGCVI FLLIIIFLTV LLLKLRKRHR KHTQQRAPAL SLSTLASPKG GSGTAGTEPS
     DIIIPLRTTE NNYCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV
//
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