ID A0A1S3T4F7_SALSA Unreviewed; 208 AA.
AC A0A1S3T4F7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Ephrin-A2-like isoform X1 {ECO:0000313|RefSeq:XP_014071452.1};
GN Name=LOC106613575 {ECO:0000313|RefSeq:XP_014071452.1};
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_014071452.1};
RN [1] {ECO:0000313|RefSeq:XP_014071452.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014071452.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-
CC anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}.
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_014071452.1; XM_014215977.1.
DR AlphaFoldDB; A0A1S3T4F7; -.
DR STRING; 8030.ENSSSAP00000032663; -.
DR PaxDb; 8030-ENSSSAP00000032663; -.
DR Ensembl; ENSSSAT00000058128; ENSSSAP00000032663; ENSSSAG00000040879.
DR GeneID; 106613575; -.
DR KEGG; sasa:106613575; -.
DR OMA; NPRFFRG; -.
DR OrthoDB; 2881104at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
DR Bgee; ENSSSAG00000040879; Expressed in brain and 10 other cell types or tissues.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046875; F:ephrin receptor binding; IEA:InterPro.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:InterPro.
DR CDD; cd10425; Ephrin-A_Ectodomain; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR034252; Ephrin-A_Ecto.
DR InterPro; IPR019765; Ephrin_CS.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; EPHRIN; 1.
DR PANTHER; PTHR11304:SF4; EPHRIN-A2; 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 GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
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}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..208
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010291880"
FT DOMAIN 34..167
FT /note="Ephrin RBD"
FT /evidence="ECO:0000259|PROSITE:PS51551"
FT DISULFID 67..107
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 208 AA; 24178 MW; AD4DB7DCA11C2364 CRC64;
MDKNYLAFQM ELTFMVVALL SWVAVWADDS KIISDRYAVY WNSTNPRFLH GEYTVEVAIN
DYLDIYCPHY EDPLPLERME RYILFMVNYD GYTTCDHRMK GFKRWECNRP QSPNGPLKFS
EKFQLFTPFS LGFEFRPGHE YYYISSPHPN LVGKPCLKLK VYVKPTNDSV YESPEPFLTD
DSTGGCCMAV PCLSLMLAML LTLLLSCS
//