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Database: UniProt
Entry: R0K979_ANAPL
LinkDB: R0K979_ANAPL
Original site: R0K979_ANAPL 
ID   R0K979_ANAPL            Unreviewed;      1198 AA.
AC   R0K979;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
DE   Flags: Fragment;
GN   ORFNames=Anapl_04840 {ECO:0000313|EMBL:EOB06821.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB06821.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|Proteomes:UP000296049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749191; DOI=10.1038/ng.2657;
RA   Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA   Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA   Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA   Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA   Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA   Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA   Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA   Rao M., Pitel F., Wang J., Li N.;
RT   "The duck genome and transcriptome provide insight into an avian influenza
RT   virus reservoir species.";
RL   Nat. Genet. 45:776-783(2013).
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; KB742580; EOB06821.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0K979; -.
DR   Proteomes; UP000296049; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00112; LDLa; 1.
DR   CDD; cd06263; MAM; 1.
DR   CDD; cd05036; PTKc_ALK_LTK; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR000998; MAM_dom.
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:SF276; ALK TYROSINE KINASE RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF12810; Gly_rich; 1.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50060; MAM_2; 1.
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}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Kinase {ECO:0000313|EMBL:EOB06821.1};
KW   Membrane {ECO:0000256|RuleBase:RU000312};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW   Receptor {ECO:0000256|RuleBase:RU000312, ECO:0000313|EMBL:EOB06821.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|RuleBase:RU000312};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          53..215
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          692..968
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          439..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1006..1026
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1061..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         726
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EOB06821.1"
FT   NON_TER         1198
FT                   /evidence="ECO:0000313|EMBL:EOB06821.1"
SQ   SEQUENCE   1198 AA;  129488 MW;  AAE273368FCC317C CRC64;
     SLGSASVSKM ALEGSFICWN GTSIRLGQAC DFIRDCLEGE DEGDMCKNLP PGFYCSFEEG
     DCGWIHSSSA SRASPWRIGS PDYDRFPSIE GCGLIFDTSK APAAANTAIT STAFPAPLRN
     SPCEASPSLR MSWLIHGVLL GNISLVLVEN KTGKEQSRTL WHSANSKGLG IWQWLILPLP
     DILDRFWFQI IASWEEGSDA IIAFDNVSLS LDCYLTINGE KIPRSTTPDS SNLLTSRGGK
     KKTAILFLGV QSMLVLISDH WLFTTCGASG PYGPTQSQCN NAYRNSNLSV VVGAEGILQG
     IQIWRVPATN TYSISGYGAA GGKGGKNTMV RSHGVSVLGI FDLQKDDTLY ILVGQQGEDA
     CPSTNDVIQK VCIGENNVIE EEIRVNRSVN EWAGGGGGGG GATYIFKMEN GEPVPLIIAA
     GGGGRAYRAK TDTFHPERLE NDSSVPGLNG NSGAAGGGGG WNDNTSFLWS GKSLLEGATG
     GRSCPQAMKK WGWETRGGFG GGGGGCSSGG GGGGYIGGNA AEDNDPEMDG EDGVSFINPI
     GTLYTPALKV TEGHGEVDIR LHLNCSHCEM DECRVDPETQ KVICFCEPGT ELAEDGVSCV
     AEPVVHLPLS LVLSVVTSAL VAALILAFSG IMIVYRRKHQ ELQAMQMELQ SPEYKLSKLR
     TSTIMTDYNP NYCFAGKTTS ISDLKEVPRK NISLIRGLGH GAFGEVYEGQ VAGIPSDPTP
     LQVAVKTLPE VCSEQDELDF LMEALIISKF NHQNIVRCIG VSLQALPRFI LLELMAGGDL
     KSFLRETRPR PNQPSSLSML DLLHVARDIA CGCQYLEENH FIHRDIAARN CLLTCRGPGR
     VAKIGDFGMA RDIYRASYYR KGGCAMLPVK WMPPEAFMEG IFTSKTDTWS FGVLLWEIFS
     LGYMPYPSKS NQEVLEFVTN GGRMDPPKNC PGPVYRIMTQ CWQHQPEDRP NFAIILERIE
     YCTQDPDVIN TALPVEYGPS VEEEEKVAIH PEDPEGIPPL LVSAHQDRKD DKQTLPSPPP
     LPSAITAGKA LGKAGALEPP VPGKVQSASA GGHINMAYTQ SNPPSELHKG RGSRNKPTNL
     WNPTYGSWFA EKQASRNNPL LEKEMPEREN LGHEGNCTVG PNIVTGRLPG SSLLLEPSSL
     TASVKEVPLF RLRHFPCGNV NYGYQQQGLP LEASTPPCAS SYEDPALRNK SHITQHGP
//
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