ID A0A6A5EJP9_PERFL Unreviewed; 992 AA.
AC A0A6A5EJP9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=PFLUV_G00208330 {ECO:0000313|EMBL:KAF1376223.1};
OS Perca fluviatilis (European perch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8168 {ECO:0000313|EMBL:KAF1376223.1, ECO:0000313|Proteomes:UP000465112};
RN [1] {ECO:0000313|EMBL:KAF1376223.1, ECO:0000313|Proteomes:UP000465112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:KAF1376223.1};
RA Roques C., Zahm M., Cabau C., Klopp C., Bouchez O., Donnadieu C., Kuhl H.,
RA Gislard M., Guendouz S., Journot L., Haffray P., Bestin A., Morvezen R.,
RA Feron R., Wen M., Jouanno E., Herpin A., Schartl M., Postlethwait J.,
RA Schaerlinger B., Chardard D., Lecocq T., Poncet C., Jaffrelo L.,
RA Lampietro C., Guiguen Y.;
RT "A chromosome-scale genome assembly of the European perch, Perca
RT fluviatilis.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF1376223.1}.
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DR EMBL; VHII01000018; KAF1376223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A5EJP9; -.
DR Proteomes; UP000465112; 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; 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; 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; 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}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000465112};
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..992
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025444663"
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..888
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 917..981
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 992 AA; 111063 MW; 9FA67AC0CCEC7A79 CRC64;
MLSRSIPCLW ITFCLHLCCH VDSGEAQNAK EVILLDSKAQ QTDLEWISYP PNGWEEISGL
DENYTPIRTY QVCQVMEPNQ NNWLRTNWIE KGNAQRIFVE LKFTLRDCNS LPGVVGTCKE
TFNLYYQETD SEVGRSLREN QYVKIDTIAA DESFTQGDLG ERKMKLNTEV RIIGPLSRRG
FYLAFQDVGA CIALVSVKVY YKKCWSIIEN LATFPDTVTG SEFSSLVEVE GMCVSDAEEE
ADNSPKMHCS AEGEWLVPIG KCICKAGFHQ KGDACEPCGR GFYKSSSQDL QCSRCPAHSL
NDREGSWRCD CEDGYYRALS DPPSVACTRP PSAPQNLVYN INQTSVSLEW GPPADTGGRN
DVTYRVVCRR CSWDPEECVP CGPNVGYSPA QSGLVDTYVT VVDLLAHANY TFEVEAVNGV
SDLSRTQRLF AAVSIATGQA APSQVSEVIK EKVQQRSIQL SWQEPQQPNG VITEYEIKYY
EKDQKDRVYS TVRSRSTSAT VNNLKPSTAY VFQIRAFTEA GYGTYGPRLE ITTKEETTAA
IVSSEQNPVI IIAVVAVAGT IILVFMVFGF IIGRRHCGYS KADQEGDEEL YFQFKFPGTK
TYIDPETYED PNRAVHQFAK ELDASCIKIE RVIGAGEFGE VCSGRLKLPG KRDVSVAIKT
LKVGYTEKQR RDFLCEASIM GQFDHPNVVH LEGVVTRGKP VMIVIEYMEN GSLDGFLRKH
DGQFTVIQLV GMLRGIAAGM RYLSDMGYVH RDLAARNILV NSNLVCKVSD FGLSRVIDDD
PEAVYTTTGG KIPVRWTAPE AIQYRKFTSA SDVWSYGIVM WEVMSYGERP YWDMSNQDVI
KAIEEGYRLP APMDCPPGLH QLMLDCWQKD RAERPKFDQI VGILDKMIRN PNTLKTPVGT
CTRPISPLLD QSTPDFTAFC SVGEWLEAIK MERYRDNFTA AGYSSLESVA RMSIEDVMSL
GITLVGHQKK IMSSIQTMRA QMLHLHGTGI QV
//
