ID A0A3P8Z6E5_ESOLU Unreviewed; 1370 AA.
AC A0A3P8Z6E5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000024048.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000024048.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000024048.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR RefSeq; XP_010867222.1; XM_010868920.2.
DR RefSeq; XP_010867223.1; XM_010868921.2.
DR STRING; 8010.ENSELUP00000024048; -.
DR Ensembl; ENSELUT00000035400.2; ENSELUP00000024048.1; ENSELUG00000022848.2.
DR GeneID; 105009497; -.
DR KEGG; els:105009497; -.
DR GeneTree; ENSGT00940000157842; -.
DR InParanoid; A0A3P8Z6E5; -.
DR OMA; WIQTQTA; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000265140; LG17.
DR Bgee; ENSELUG00000022848; Expressed in nose and 12 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007411; P:axon guidance; IEA:UniProt.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00102; IPT; 1.
DR CDD; cd01179; IPT_plexin_repeat2; 1.
DR CDD; cd05058; PTKc_Met_Ron; 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|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000617-
KW 2};
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:UP000265140};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1370
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018296051"
FT TRANSMEM 936..961
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..509
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT DOMAIN 1059..1323
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1351..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-1"
FT BINDING 1065..1073
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1092
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1139..1142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT MOD_RES 1216
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1217
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1331
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1338
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 131..139
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 167..170
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 292..360
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 1370 AA; 151910 MW; 3A3249902C452178 CRC64;
MVPWATILVT CVWMQTVKAS GLDACPKTPR TEVDFTVNYS IPHFQTIKPI QNVVVNPEKQ
DIYVASQNVI EAVSGQLNKL WELRTGPVGS PECLTCQLCG IETDPGDSLD TDNKVLLLDP
ALYDTPYLYS CGSSKHGVCY LHELNLDGTP PTSQCLFRKD ANSPSHCPDC LASPLGTEAV
IVEDGYTAYF FVAATLNESV AQRYGRQSIS IRRPLSTTDG FELTTPGLTV LPKYQNSYQI
DYIYSFSAGS YVYFLSVQRE NLLDSAGYQT RLGRLPVKDI EMGMYREIVL ECRYKLKRRR
RSEGKSFQDI VYNGLQAAHF SSAGKELAAE LGVGENEGIL YGTFAVTDTS GRPYSNSAMC
AFSLALVDEA IDKGVEDCCR SSTEQLSRGL CQYQPCESCP HESSEDNASC PNKPTLVSKP
FNRVDLFERL FNNVLLTSVL VTIHDIHTLA HIGTKDGRLL QLILRRSSPI FFANYTLAEG
MEVSRKAAVH SNKSLLFVVG NKLFSVSPRG PGCKHFLTCS KCLAAPQFTG CGWCSGSCSR
QEECPAQWTN EACAPVITEF FPKTAPRDGE TELTVCGWEF QTSQHTTINK GNPWVKVGET
PCTVLSKSRT QLVCTLHRAV PSPSENLTIT LRISEGKVEG SYRIVGQGQI TGFTFVVPNI
TDITPDYGPQ IGGTLVTLTG SHLNSGMKRF VTVGDQDCPI QSVSEGTGSL STIVCLSKGV
TELKTVPLSV SIDKYLVSTD KTFQYKVNPE ISKIQPACSF TSGSKIVIEG MNLDSAYNTV
ITYYSDKSNQ QPLQRVCTGT ATRMRLECFA PAFPRNETDK GYLNIAMDGA ANLMQQPFEY
HPEASITSFE DEGNVLRLSH GQTEVSLHHN KLNMVSHCMK INMTIGGVDC GVQVLGNELT
CRIPKHVVIP SEGLPVTVFV NGRVYEVGTV VLANNYLTLA FVMLGVVTMS CVGCLVVYIA
MKRVKRKKKV KLETRLARMS GHTRMASNRD LSSSNGDYRH EMFYHNSQTS GSGGVVLNGL
VYAANYDPSA VPLISLDTLR SGLLEEVKDV LIPADMLQVH RNQVIGKGHF GTVYHGYLTD
INQEQLIHCA VKSLNRITGL EEVEQFLREG ILMKKFNHAN VLSLLGILLP QDGLPLVVLP
YMKHGDLRHF IRCERRNPTV KDLIGFGLQV AKGMEYLAQK KFVHRDLAAR NCMLDETFTV
KVADFGMARD VFDKEYYSIQ DHKKAKLPVK WMAIESLQTQ KFTTKSDVWS FGVLMWELLT
RGASPYPEVD PYDITHFLMR GRRLPQPQFC PDALYSVMLE CWDPEPEFRP DFRTLDQEVQ
EILSRLEGEH YISLNVTYVN LDQPRPYPAL TASADEAEAS GLDSDSAMSS
//
