ID A0A4W5LUL8_9TELE Unreviewed; 979 AA.
AC A0A4W5LUL8;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000029672.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000029672.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A4W5LUL8; -.
DR STRING; 62062.ENSHHUP00000029672; -.
DR Ensembl; ENSHHUT00000030902.1; ENSHHUP00000029672.1; ENSHHUG00000018393.1.
DR GeneTree; ENSGT00940000156266; -.
DR Proteomes; UP000314982; Unassembled WGS sequence.
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; cd09550; SAM_EPH-A8; 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:SF7; EPHRIN TYPE-A RECEPTOR 8; 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; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
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; PS00791; RECEPTOR_TYR_KIN_V_2; 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}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000314982};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..979
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021240341"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..198
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 317..422
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 423..518
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 617..878
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 904..968
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 742
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 623..631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 62..180
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 97..107
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 979 AA; 109371 MW; 81E39CD4CBC3F42B CRC64;
YHRCLCSCPC TLFIIVCVSV MNLLDTSSIS GDWGWLTYPS HGWDSINEMD EYFSPIHTYQ
VCNVMSPSQN NWLRTGWIAR DGARRIYIEV KFTLRDCNSM PGVLGTCKET FNLYYYESDR
AVGTAIKETQ FTKIDTIAAD ESFTGVDLGV RRLKLNTEVR GVGPLTRRGF YLAFQDIGAC
IALTSVRVYY KRCSGVGRNL AVFTDVVTGA DSSSLVEVRG QCVDHAEERD TPKMYCSAEG
EWLVPIGKCV CSAGFEEHRE SCIACEVGFY KPVAGDGLCG KCPLQSHSET RAALSCPCDS
SHYRAPTDPL AAPCTRPPTA PVNMISSVNG TSVNLEWGRP LDSGGRSDLL YSVLCQKCSG
EGGVVPVRFV PRQSSLTEPL VTVLNLVAHA NYTFRILAMN AVTHLSNEPP PFASVNITTN
QAAPSQVIAI RQENASQNSV TLLWHEPDQP NGVILEYDVK YYEKDKEQQS YSTLKAKGTT
ARVSGLKPGT RYIFQVRART SAGCGRFSQN VEIQTGKAIP LRYDTMTIIW ICMVLVSGLV
TFLAIVICRK RHCGYSKAFQ DSDEEKMHYQ NGHGAFMLML FILVSFPDAR FYIDPHTYED
PCQAVHEFAR EIEASRIKLE KIIGSGEFGE VCYGRMRLPG KRDIPVALKT LKAGYSDKQR
REFLAEASIM AQFDHPNIIH LEGVVTRSKP VMIITEYMEN GSLDSFLRRH DGQFTIIQLV
GVLRGIAAGM TYLADLGYIH RDLAARNILV NSNLVCKVSD FGLSRVLEDD PDAAYTTSGG
KIPIRWTAPE AIAYRKFSSS SDVWSYGVVM WEVMSYGERP YWNLTNRDVI KSVEEGYRLP
APMSCPGALH TLMLDCWQKD RNERPRFCQI VTVLDKLIRN PENLKSMDTL CTPPMMDRSI
PDFSSCSSVD EWLDTIKMGR YKDHFAVGGY QTLGHVISMN QGDIHRLGVT LMGHQKKIMT
SVQLMRVQVL NRSVPSVHV
//
