ID A0A556UYM0_BAGYA Unreviewed; 1041 AA. AC A0A556UYM0; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 24-JUL-2024, entry version 22. DE RecName: Full=Fibroblast growth factor receptor 4 {ECO:0000256|ARBA:ARBA00039655}; DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902}; GN ORFNames=Baya_11009 {ECO:0000313|EMBL:TSP68524.1}; OS Bagarius yarrelli (Goonch) (Bagrus yarrelli). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes; OC Sisoridae; Sisorinae; Bagarius. OX NCBI_TaxID=175774 {ECO:0000313|EMBL:TSP68524.1, ECO:0000313|Proteomes:UP000319801}; RN [1] {ECO:0000313|EMBL:TSP68524.1, ECO:0000313|Proteomes:UP000319801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JWS20170419001 {ECO:0000313|EMBL:TSP68524.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:TSP68524.1}; RX PubMed=31274158; RA Jiang W., Lv Y., Cheng L., Yang K., Chao B., Wang X., Li Y., Pan X., RA You X., Zhang Y., Yang J., Li J., Zhang X., Liu S., Sun C., Yang J., RA Shi Q.; RT "Whole-Genome Sequencing of the Giant Devil Catfish, Bagarius yarrelli."; RL Genome Biol. Evol. 11:2071-2077(2019). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; CC Evidence={ECO:0000256|ARBA:ARBA00001171}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. CC Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Endosome CC {ECO:0000256|ARBA:ARBA00004177}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {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:TSP68524.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VCAZ01000078; TSP68524.1; -; Genomic_DNA. DR AlphaFoldDB; A0A556UYM0; -. DR Proteomes; UP000319801; Unassembled WGS sequence. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0017134; F:fibroblast growth factor binding; IEA:TreeGrafter. DR GO; GO:0005007; F:fibroblast growth factor receptor activity; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:TreeGrafter. DR GO; GO:0070857; P:regulation of bile acid biosynthetic process; IEA:TreeGrafter. DR CDD; cd05857; IgI_2_FGFR; 1. DR CDD; cd05099; PTKc_FGFR4; 1. DR Gene3D; 6.10.250.1740; -; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 4. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR050122; RTK. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR PANTHER; PTHR24416:SF343; FIBROBLAST GROWTH FACTOR RECEPTOR 4; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF07679; I-set; 2. DR Pfam; PF13927; Ig_3; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 5. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00409; IG; 4. DR SMART; SM00408; IGc2; 4. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; Immunoglobulin; 4. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50835; IG_LIKE; 4. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Endosome {ECO:0000256|ARBA:ARBA00022753}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319}; KW Kinase {ECO:0000256|ARBA:ARBA00023137}; KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:TSP68524.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000319801}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; 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 TRANSMEM 600..620 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 139..236 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 256..343 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 377..470 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 479..579 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 697..985 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 348..367 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..25 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 349..363 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 842 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1" FT BINDING 733 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT BINDING 847 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3" FT BINDING 860 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3" SQ SEQUENCE 1041 AA; 116997 MW; C13BE2CE0AF62FED CRC64; MVQFNQKHRV HTEFPKEKRE RETNPGKTVA EAISISVKTA GCWTFVACVL AAEGNLHYKV GLSITTIVNP RPVFSSTGRY PEVSNAWSQR LSGLQEKRFL GKMWSIWKFF ITLCLAEFVL SKSITTQAIR AKDSRVHRPT LQPGFPENTT VLLGGQAKLV CKVHRPATTR LQWFKRDKDR LGPDGSPLLK PLTLLQDNIS KVNILPLVNV TLEDAGEYIC MAKNSAGRTS NSAWVEVLTE ILLAKSVDQL TVAENPTEVS EELSEDTSEH LLLEPGDVLK LRCDTNRPGA VHWFKGDIRV QHSGRIQIKA GVIEITDARY EDSGVYVCMV RGSREPLRNF TITVADAVGS GDDDEDAGQE DSVTETENDQ VFISKGPYWT HIQRMEKKLY AVPAGNTVKF RCPATGSPTP SIRWLKNGRE FRGEHRIGGI KLRHQHWSLV MESVVPSDRG NYTCVVENKY GSITHSYLLD VLERSPHRPI LQAGLPTNTT AVVGGDAQFH CKVYSDAQPH IQWLKHIEIN GSRYGPDGIP YVKVVKTGSL NMSEVEVLYL TNITMEDAGE YTCLAGNSIG FSHQSAWLTV LSEEDVAKEM DLMETKYTDI IIYASGFLAL VMAIVIVVLC RMQTHPSREH FDALPVQKLS KFPLRRQYSV ESNSSGKSSA SLMRVARLSS SCSPMLAGVM EFELPYDPDW EFPRENLTLG KPLGEGCFGQ VVRAEAYGIN RDNPEQVTTV AVKMLKDDAT DKDLADLISE MELMKGMDKH KNIINLLGVC TQEGPLYVLV EYASKGSLRE YLRARRPPGM DYTFDVTKVP EEQLTFKDLL SCAYQVARGM EYLASKRCIH RDLAARNVLV TEDNVMKIAD FGLARGVHQI DYYKKTTNGR LPVKWMAPEA LFDRVYTHQS DVWSFGVLMW EIFTLGGSPY PGIPVEELFK LLKEGHRMDK PSNCTHELYM KMRECWHAVP TQRPTFKQLV EELDRVLLSI SDEYLDLSTP FEQYSPSCED TSSSCSSDND SVFTHDALST DPCLLGYHDV RSRIDVKTSL R //