UniProt: A0A091RP86

Database: UniProt
Entry: A0A091RP86_NESNO

LinkDB:  A0A091RP86_NESNO 
Original site:  A0A091RP86_NESNO

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (22)   
   InterPro (12)   
   Pfam (2)   
   PROSITE (5)   
   SMART (3)   
All databases (32)   

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ID   A0A091RP86_NESNO        Unreviewed;      2310 AA.
AC   A0A091RP86;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN   ORFNames=N333_13516 {ECO:0000313|EMBL:KFQ43939.1};
OS   Nestor notabilis (Kea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX   NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ43939.1, ECO:0000313|Proteomes:UP000053840};
RN   [1] {ECO:0000313|EMBL:KFQ43939.1, ECO:0000313|Proteomes:UP000053840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ43939.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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         ECO:0000256|RuleBase:RU000312};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily.
CC       {ECO:0000256|RuleBase:RU000312}.
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DR   EMBL; KK928139; KFQ43939.1; -; Genomic_DNA.
DR   RefSeq; XP_010015820.1; XM_010017518.1.
DR   GeneID; 104408031; -.
DR   KEGG; nnt:104408031; -.
DR   CTD; 6098; -.
DR   OrthoDB; 4577877at2759; -.
DR   Proteomes; UP000053840; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00063; FN3; 7.
DR   CDD; cd05044; PTKc_c-ros; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF527; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ROS; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 9.
DR   SMART; SM00135; LY; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 5.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF63825; YWTD domain; 3.
DR   PROSITE; PS50853; FN3; 7.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000313|EMBL:KFQ43939.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053840};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000312};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..2310
FT                   /note="Tyrosine-protein kinase receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001879393"
FT   TRANSMEM        1876..1899
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          113..206
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          209..297
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          574..674
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          955..1047
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1051..1158
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1573..1671
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1672..1767
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1962..2241
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1760..1784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1997
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   2310 AA;  260575 MW;  3EC4A77FF81CA196 CRC64;
     MRNACLWDLP LNRLAAFYCV WISAVNCTFS RNCQNLCTSN LEGELGITNL CNVSDITGAC
     TQGCQFWNAT VQINCPLKCN KTYTRACETV SCKFGCSRAE DAYGIEAQNY LNEPGAPFAS
     TIGTHNVTLG WKPANISGVK YIIQWKFNQL PGDWRYTEVV SKASYTVKDL QAFTEYVFRV
     VWIITSQLQL HSPSSPSYRT HAFGAPTTAP IIKTIQSSSP NTVEVSWSPP LFPNGLIVGY
     NLLLTSEKHE LLRASRGHSF QFYSTFPNNT YRFSIVAVNE VGAGPPAEAN ITTPESRVKE
     KPAWLFLSRN QSLRKRNTEH FLEATQCLQN GIINHNITGI SVSVYQQLVY FSEGNSIWVK
     GAANMSDVSD LMLFYAGWGN ITSISVDWLY QRIFFVMNEK IHVCHLENCT AAEDITPLYV
     TSPRKVIADP YNGYLFCLLE DGIYRANLQL CPGTASTASP VVKSSALRDF MINFQSKRLI
     IFNKTEQTFV SGFLDGSEFH TLRSHVPLHD VESFVYEDNT FTVTDGWAVF HEEVSPLGSS
     SFNEYIVDCN LAYPEYFGFD NLVFYGASTQ PFPSPTPPRL VTALFGLDQA VICWRPPEYT
     IGTSPSAWQN WTYDVKVSSQ HPPEEEWVFS NISDTRFTVK ELTSFTAYEV LVRAVSPAGE
     GPWSETFRGT TLEEAEEEPY MLAVGAEGLW KQRLDSYGPG ELLYPHIRNI SDLDWYNDTL
     YWINSMGEVQ TWSLNKREAT TRNTYVSDVR NARILAFDWL GQCLYWAGKA NTIYRKSLLR
     GHIDIVAHVL FLVKDLVVDS VNGYLYWATM YSVESARLNG EEYLMLQEQL QFSGKQVVGL
     TLDLTYGLLY WLVQDSLCLN LYRVSLRKEG CGNAIITEFA AWSTSEISQG ALEYYSGRLF
     WINSLHFITT QEVNQSLSIP FSQPAEFATF TLVHTSLKPL PGNFSFTPKV IPDSVPESSF
     RIKGNSSSFH IIWSPTNVEW GTVFYCVGSK ALQFSESEWC LHPHNLTVPF YRVDWLEPFT
     LFDFTVTPYT YWGKAPTTSV SLRAPEGVPS APTNPRIYVL QNNLHESSDT VSVEFRWDRP
     EMENGVLLQF RVYYQLWNQS DTANTFTEWN MSNVKPTLTL FSLTNVLPSL TVRFQVQAFT
     SAGPGPLSDI AERNSSDLFP VPSLITVSAN KLCLTDIDNN HTIWELSAKI NVKDICYTAN
     DDKAYYIAED SIFLLNTQTA SKFQFFKDAY LHNATAITVD WIARHLFVAL KTPWSENQIF
     FIDLELKIKS LKALNIQLGR SNSTVSSLLS YPFLSRLYWM EELDYGSRMF YYDILNNTMH
     HVLGYVSVEE QMRNSCTCNV AEAELGRPMS IDVSDSKNPQ LLFIRGRDEI WASDVDGCHC
     WRVTKIPGFQ GKKIGSLTVD KKFVYWSSET KEYTEIWLAN KERTGHFLQK RANHELKILA
     YSSAVQLYPD KRCLIPLTNI EKPTILDTTN TSFMLSLPSV TPQQLCPGIL QPTPMYLVFL
     EQMTNNHMNS SYRLSALQQK TLEFQGSIAI IDNLQPFSSY VIQVAVKNYY SDEEVLPMAK
     ETIGTTLYGV PEAVDSIKTV VLSDTTISIS WKEPLKPNGP LESIRYQISV NLLLSVPATP
     LRKSEFPNGM LAWSVHGLQS GTNNLFKVLA FHPDENWFSE SVPVIVKTFE TPPAPFNIVP
     RNTSFQLQWR APLHVNETSF WFELRKWQTK SDWFSPATTA CTADLVYTCN LTGTLPSTNY
     FVRVTVVYVT GVKSTSSSTS FKTTAGVPSK PGVPKRAEDT KNSVQWEKAD DNGSNLTYYI
     LESRKQSDNT SKVKFLWEVV YNGSCASICM WKAKNLDGTF QFRVAAANVL GLGEYSDTSE
     DIILGEDTMI SLDATIAVAV VTGVVMLGLT VVMLFGFVWH QRWKSRKQAL PGHIVFVKED
     KELAQLRGMI ETVGLANACY AVSILPSQEE IESLPAFPRD KLNLHKLLGS GAFGEVYEGT
     AVDILAHGSG EYKVAVKTLK KGATDHEKSE FLKEAHLMSN FDHPHILKLL GVCLLNEPQY
     LILELMEGGD LLSYLRGARK QKLQSPLLTV TDLLDICLDI CKGCVYLEKM HFIHRDLAAR
     NCLVSEKEYE SSSRVVKIGD FGLARDIYKN DYYRKRGEGL LPVRWMAPES LIDGVFTNRS
     DVWAFGVLVW ETLTLGQQPY PGFSNTEVLH HVRSGGRLES PNNCPDDLCD LMTRCWAQEP
     HNRPTFSYIQ DKLQEVRHSP LSFIHYLKDK EAATGVVNQA FEDSDVPCAD SDSILSATLV
     ETRNQEGLNY LVFVKEGNQD QGSISSAELS
//

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