ID A0A484DFV9_PERFV Unreviewed; 1374 AA. AC A0A484DFV9; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 29-MAY-2024, entry version 23. DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902}; DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902}; GN ORFNames=EPR50_G00044050 {ECO:0000313|EMBL:TDH14369.1}; OS Perca flavescens (American yellow perch) (Morone flavescens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca. OX NCBI_TaxID=8167 {ECO:0000313|EMBL:TDH14369.1, ECO:0000313|Proteomes:UP000295070}; RN [1] {ECO:0000313|EMBL:TDH14369.1, ECO:0000313|Proteomes:UP000295070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YP-PL-M2 {ECO:0000313|EMBL:TDH14369.1}; RC TISSUE=Blood {ECO:0000313|EMBL:TDH14369.1}; RA Feron R., Morvezen R., Bestin A., Haffray P., Klopp C., Zahm M., Cabau C., RA Roques C., Donnadieu C., Bouchez O., Christie M., Larson W., Guiguen Y.; RT "A chromosome-scale genome assembly of the yellow perch, Perca RT flavescens."; RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases. 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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the plexin family. CC {ECO:0000256|ARBA:ARBA00010297}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}. 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:TDH14369.1}. 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; SCKG01000004; TDH14369.1; -; Genomic_DNA. DR STRING; 8167.A0A484DFV9; -. DR OrthoDB; 1614410at2759; -. DR Proteomes; UP000295070; Chromosome 4. DR GO; GO:0009925; C:basal plasma membrane; IEA:TreeGrafter. DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0005008; F:hepatocyte growth factor receptor activity; IEA:TreeGrafter. DR GO; GO:0007411; P:axon guidance; IEA:UniProt. DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter. DR GO; GO:0001889; P:liver development; IEA:TreeGrafter. DR GO; GO:0031016; P:pancreas development; IEA:TreeGrafter. DR CDD; cd00603; IPT_PCSR; 1. DR CDD; cd01179; IPT_plexin_repeat2; 1. DR CDD; cd05058; PTKc_Met_Ron; 1. DR CDD; cd11248; Sema_MET_like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR002909; IPT_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR002165; Plexin_repeat. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR016201; PSI. DR InterPro; IPR001627; Semap_dom. DR InterPro; IPR036352; Semap_dom_sf. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR PANTHER; PTHR24416:SF614; RECEPTOR PROTEIN-TYROSINE KINASE; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF01437; PSI; 1. DR Pfam; PF01403; Sema; 1. DR Pfam; PF01833; TIG; 2. DR PIRSF; PIRSF000617; TyrPK_HGF-R; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00429; IPT; 3. DR SMART; SM00423; PSI; 1. DR SMART; SM00630; Sema; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF81296; E set domains; 3. DR SUPFAM; SSF103575; Plexin repeat; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF101912; Sema domain; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS51004; SEMA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRSR:PIRSR000617-2, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR000617-3}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Kinase {ECO:0000256|ARBA:ARBA00023137}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000617-2, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170}; KW Reference proteome {ECO:0000313|Proteomes:UP000295070}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, 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}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 24..1374 FT /note="receptor protein-tyrosine kinase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5019824721" FT TRANSMEM 939..962 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 25..508 FT /note="Sema" FT /evidence="ECO:0000259|PROSITE:PS51004" FT DOMAIN 1064..1325 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1353..1374 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1357..1374 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1190 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000617-1" FT BINDING 1070..1078 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2" FT BINDING 1096 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2, FT ECO:0000256|PROSITE-ProRule:PRU10141" FT BINDING 1143..1146 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2" FT BINDING 1194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2" FT MOD_RES 1220 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4" FT MOD_RES 1221 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4" FT MOD_RES 1335 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4" FT MOD_RES 1342 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4" FT DISULFID 96..99 FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3" FT DISULFID 128..136 FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3" FT DISULFID 165..168 FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3" FT DISULFID 291..360 FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3" FT DISULFID 378..399 FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3" FT DISULFID 513..531 FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3" FT DISULFID 519..553 FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3" FT DISULFID 522..538 FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3" FT DISULFID 534..544 FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3" SQ SEQUENCE 1374 AA; 153585 MW; 69739A2E13851482 CRC64; MVHWTSKWGT CVCVQTLLAF ALANCPSLAP SPVNFSVVYT MPFFQARGPI QNIVNNSLYQ EVYVASQNVI EAVNRSLEKV WELRTGPVGS PECQICDLCD IDKDPDFPED TNNQILLLDT LFMYLYSCGS SQYGVCYFHQ LNSNGESPSL SKCLFRKAAN SAVYCPDCVA SPLGTKVTMV EEGQTVYFFV ASTVNDSVTQ RYGRKSISVR RPLATEDGFY SDVRGLTVLP GLRRTYHIEY VYSFFSQEFV YFLSVQRESP DQDSSPFQTR LGRLPRNEWE MKRYREVILE CRFEPKRRRR NVASEPYKDV VYNVVQAAHF GKAGRELAEE LGAEEEDDIL YGVFAVTDDN GVTEHDSALC AFPMDNVNKA IVDGVDDCCE SGPEQLSRGL CHFQPCESCP HESMENNATC RDHPTMVSKP YYRVDLFNRQ MIDVLLTALL VTTIENKTVA HIGTSTGRLL QLVLTRSSPI IFANYSLVEN QRVSSIAAVY SSEYLLFVVG DKMIQVPQRG PGCQHFLTCA MCLTAPKFMG CGWCSGVCSW ESECNRRWRN ESCPPGITGF FPRTAPPDGQ TELTVCGWEF QSPLRPAITS RTHQVRLGQT ACTVLPVKSN NTHFVCKIRS GATELSKPVN ITVEVHEGKV EGRYSIDGKA EMPGFTFVIP NITEIQPNYG PRVGGTLITV TGPHLDAGKT RKVTLNDMPC PIKRVTEPKG NVSSIICLSQ PISEVRDVPL SVFIDKSPVL TTKVFYYKEN PMITAVLPDC SFDRGSKIVI GGENLDSVYR TIIRFKPNES HLKPVTRECI GKSLPTRMEC ISPVFPRDET EEGELSFDMD GALGLWNKEF SYHPYGEPIP FETDGHVLNL YPGFDEVSLH HQKLNLVSSC MTIIMTVAGV DCDAKVLDNE ITCRIPKNMT ITSEGLPVKI SINGQVHNVG TVVRVSNHYM VGVVLGILAA LVAGAVLAFV VMKHLRKTKK ASMVETRLAH SANLSGTNNV ELSPVGDYRR VVSLSPSTPL VGSMVFPSLS FAAGSIDPTL TPLMPSEKIS ISSFRPELLE EVKDVLIPAE MLIVQHHRII GKGHFGTVYH GYFTDHNNRE IHCAVKSLNR ITDVEEVEQF LKEGIIMKGF HHSNVLSLLG ILLPQEGLPL VVLPYMKHGD LRHFIRCEKR NPTVKDLIGF GLQVARGMEY LAQKKFVHRD LAGRNCMLDE SYTVKVADFG MARDVFDKEY YSVQDHRKAK LPVKWMAIES LQTQKFTSKS DVWSFGVLMW EMLTRGASPY PEVDPYDITH YLLKGRRLPQ PQYCPDPLYS IMLQCWDPDP ELRPSFATLV SAVFTILSGL EGEHYISLNV TYVNLDQPRP YPALTESADE YNSTDVEDSG SVSS //