ID A0A1S3S7Y8_SALSA Unreviewed; 1014 AA.
AC A0A1S3S7Y8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=epha7 {ECO:0000313|RefSeq:XP_014060459.1};
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_014060459.1};
RN [1] {ECO:0000313|RefSeq:XP_014060459.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014060459.1};
RG RefSeq;
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}.
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DR RefSeq; XP_014060459.1; XM_014204984.1.
DR AlphaFoldDB; A0A1S3S7Y8; -.
DR GeneID; 106607720; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000087266; Chromosome ssa06.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05066; PTKc_EphR_A; 1.
DR CDD; cd09548; SAM_EPH-A7; 1.
DR Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF9; EPHRIN TYPE-A RECEPTOR 7; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW 2}; Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_014060459.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1014
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010193586"
FT TRANSMEM 549..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..209
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 330..440
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 441..536
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 627..910
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 939..1003
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 752
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 633..641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 73..191
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 108..118
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 1014 AA; 113755 MW; 6122F8E9E13212CA CRC64;
MGSTSIPCLW ITFCIHLCCF MDTGKAQNAK EVILLDSKAQ QTELEWISYP PSGWEEISGL
DENYTPIRTY QVCQVMEPNQ NNWLRTSWIE KGDAQRIFVE LKFTLRDCNS LPGVVGTCKE
TFNLYYQETD SEVGRNIREN QYVKIDTIAA DESFTQGDLG ERKMKLNTEV RIIGPLSRRG
FYLAFQDVGA CIALVSVKVY YKKCWSIIEN LATFPDTVTG SEFSSLVEVE GMCVSDAEEE
ADNSPKMHCS AEGEWLVPIG KCICKAGFHQ KGDACEPCGR GFYKSSSQDL QCSRCPAHSY
NDREGSWRCD CEDGYYRGLS DPPSVACTRP PSAPQNLVYN INQTTVSLEW SPPADTGGRN
DVTYRIMCRR CSWEPEECVP CGGNVGYSPQ QAGLVDTYVS VVDLLAHANY TFEVEAVNGV
SDLSRTQRLF AAVSIATSQA TPSQVSEVIK ERVQQRSIQL SWQEPEQPNG VITEYEIKYY
EKDQKDRIYS TVKSRSTSAT VNNLKPSTAY VFQIRAFTAA GYGTYGPRLE VTTKEEASAT
IVSSEQNPVI IIAVVAVAGT IILVFMVFGF IIGRRHCGYS KADQEGDEEL YFQFKFPGTK
TYIDPETYED PNRAVHQFAK ELDASCIKIE RVIGAGEFGE VCSGRMKLPG KRDMSVAIKT
LKVGYSEKQR RDFLCEASIM GQFDHPNVVH LEGVVTRGKP VMIVIEYMEN GSLDAFLRKH
DGQFTVIQLV GMLRGIAAGM RYLSDMGYVH RDLAARNVLV NSNLVCKVSD FGLSRVIDDD
PEAVYTTTGK MQDIMNLIFT PATDLHFTEQ GGKIPVRWTA MEAIQYRKFT SASDVWSYGI
VMWEVMSYGE RPYWDMSNQD VIKAIEEGYR LPAPMDCPPG LHQLMLDCWQ KDRADRPKFD
QIVGILDKMI RNPNTLKTPV GTCTRPISPL LDQSTPDFTT FRSVGEWLEA IKMERYRDNF
TAAGYSSLDS VARMSIEDVM SLGISLVGHQ KKIMSSIQTM RAQMLHLHGT GIQV
//
