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Database: UniProt
Entry: A0A3Q3G0G5_KRYMA
LinkDB: A0A3Q3G0G5_KRYMA
Original site: A0A3Q3G0G5_KRYMA 
ID   A0A3Q3G0G5_KRYMA        Unreviewed;       334 AA.
AC   A0A3Q3G0G5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Ephrin B2 {ECO:0000313|Ensembl:ENSKMAP00000017972.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000017972.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000017972.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   RefSeq; XP_017296854.1; XM_017441365.1.
DR   AlphaFoldDB; A0A3Q3G0G5; -.
DR   STRING; 37003.ENSKMAP00000017972; -.
DR   Ensembl; ENSKMAT00000018223.1; ENSKMAP00000017972.1; ENSKMAG00000013384.1.
DR   GeneID; 108251174; -.
DR   KEGG; kmr:108251174; -.
DR   CTD; 30219; -.
DR   GeneTree; ENSGT00940000155868; -.
DR   OMA; GSTRHND; -.
DR   OrthoDB; 5402021at2759; -.
DR   Proteomes; UP000264800; 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   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        223..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..160
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51551"
FT   REGION          161..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        85..149
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00884"
SQ   SEQUENCE   334 AA;  37285 MW;  1387085C34C134F1 CRC64;
     MTMWRYYYFG VLVAAFRLDL VRPLILESIY WNTTNTKFVP GQGVVLYPQI GDKLDIVCPR
     VDGGVGDSVE YYKVYMVPRE QLESCTITKA DTPLLNCVKP DQDVKFTLKF QEFSPNLWGL
     EFFRGKDYYI ISTSNGTMEG IDNQEGGVCK TKSMKIVMKV GQNPSDPISP KDNPTRVTYP
     TKPSSDKDHR NNDVLEKPDV ASREDKDNNE NGGKSSSAIG SEVAIFVGIA SGSVIFIIII
     IMLVLLLLKY RRRHRKHSPQ HTATLSLSTL ATPKRSGGGG NNNGSEPSDI IIPLRTADSV
     FCPHYEKVSG DYGHPVYIVQ EMPPQSPANI YYKV
//
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