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Database: UniProt
Entry: A0A1S3RJ48_SALSA
LinkDB: A0A1S3RJ48_SALSA
Original site: A0A1S3RJ48_SALSA 
ID   A0A1S3RJ48_SALSA        Unreviewed;       336 AA.
AC   A0A1S3RJ48;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Ephrin-B1 {ECO:0000256|ARBA:ARBA00040452};
GN   Name=LOC106603306 {ECO:0000313|RefSeq:XP_014052295.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014052295.1};
RN   [1] {ECO:0000313|RefSeq:XP_014052295.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014052295.1};
RG   RefSeq;
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   RefSeq; XP_014052295.1; XM_014196820.1.
DR   AlphaFoldDB; A0A1S3RJ48; -.
DR   STRING; 8030.ENSSSAP00000084964; -.
DR   PaxDb; 8030-ENSSSAP00000084964; -.
DR   Ensembl; ENSSSAT00000172428; ENSSSAP00000172432; ENSSSAG00000068796.
DR   GeneID; 106603306; -.
DR   KEGG; sasa:106603306; -.
DR   OMA; YKLYMVR; -.
DR   OrthoDB; 5402021at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa04.
DR   Bgee; ENSSSAG00000068796; Expressed in pharyngeal gill and 11 other cell types or tissues.
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: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   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:UP000087266};
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..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..336
FT                   /note="Ephrin-B1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010273708"
FT   TRANSMEM        230..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..161
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51551"
FT   REGION          167..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        86..150
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00884"
SQ   SEQUENCE   336 AA;  37299 MW;  70812AF4A96CA886 CRC64;
     MAGSGSNWKY YLWILTVLCR SLLPFAKSLE SVIWNSQNPK FQYGKGLVIY PEIGDKLDII
     CPKADMGRPY EFYKLYLVKK DQADQCSTVM DPNVLVNCNK PEKDIKFTIK FQEFSPNYMG
     LEFKKNINYF ITSTSNGTLE GLENREGGVC NTLSMKIVMK VGQDPNTVVP DPVITDKPSE
     DQDNTVKETT TSPNKKKGGS GGAVEPGNKD TMNQDNKSNS AEGIFASKPA LFAAIGAGCV
     IFLLIIIILI VLLIKLRKRN RKHTQQRTTA LSLSTLASPK CSGNAGSEPS DIIIPLRTTE
     NNYCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV
//
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