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Database: UniProt
Entry: A0A099Z5W3_TINGU
LinkDB: A0A099Z5W3_TINGU
Original site: A0A099Z5W3_TINGU 
ID   A0A099Z5W3_TINGU        Unreviewed;      1340 AA.
AC   A0A099Z5W3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=N309_10273 {ECO:0000313|EMBL:KGL77116.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL77116.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL77116.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL77116.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-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; KL889719; KGL77116.1; -; Genomic_DNA.
DR   STRING; 94827.A0A099Z5W3; -.
DR   Proteomes; UP000053641; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043560; F:insulin receptor substrate binding; IEA:InterPro.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
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; 3.
DR   CDD; cd00064; FU; 1.
DR   CDD; cd05061; PTKc_InsR; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR040969; Insulin_TMD.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-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; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF535; INSULIN RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF17870; Insulin_TMD; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000620; Insulin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00261; FU; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50853; FN3; 2.
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|PIRSR:PIRSR000620-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; 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:PIRSR000620-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053641};
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   TRANSMEM        918..942
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          588..690
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          804..911
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          981..1256
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1284..1340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1117
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT   BINDING         991
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1015
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1062..1068
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1121..1122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1135
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL77116.1"
FT   NON_TER         1340
FT                   /evidence="ECO:0000313|EMBL:KGL77116.1"
SQ   SEQUENCE   1340 AA;  151363 MW;  F0C6969CE34B688D CRC64;
     VCRSMDIRNN LTRLNMLENC TVIEGHLQIL LMFKTKPEDF RELSFPKLTM ITDYLLLFRV
     YGLESLKGLF PNLTVIRGTH LFFNYALVIF EMVHLKEIGL YNLMNITRGA VRIEKNNELC
     YLSTIDWSRI LDSVEDNYIV ANKDDKEECG DVCPGTVKGK SNCPPTVING IFIERCWTHD
     RCQRVCPPAC KSQGCTPEGQ CCHSECLGDC TEPNSPEKCV ACRNFYLDGK CVDTCPPGYY
     RFEGWRCVTF SFCQELHNKC KNARESGCHV IHNNECVHEC PSGYIMNSSN LHCTPCAGPC
     PKVCDYGKEK TIDSVTSAQE LRGCTVVNGS LVINIRGGNN IAAELEANLG LIEEISGYLK
     IRRSYALVSL SFFRKLHLIR GETLEAGNYS FYALDNQNLR QLWDWSKHNL TIARGKLFFH
     YNPKLCLSEI HKMEEISGTK GRQERNDIAL KTNGDQASCE NELLKFSSIR TSHDKILLKW
     EPYWPPDFRD LLGFMLFYKE APYQNVTEFD GQDACGSNSW TVVDVDPPPR SNEPKAQAQP
     GWLLRGLKPW TQYAVFVKTL VTFSDERRTY GAKSEIIYVQ TNATVPSVPL DPISVSNSSS
     QIILKWKPPS EPNGNITHYL VFWQQQAEDS ELYELDYCLK GLKLPSRTWS PPFESEDPQK
     YNQSENEDVS GECCSCPKTD SQIQKELEES AFRKTFENYL HNEVFVPRPS RKRRDLGSMA
     NATVVLPTIP SSPNASVAAS ENTDEQKPFE KVKSKESLVI SGLRHFTGYR IELHACNHDA
     QESRCSVAAY VSARTMPEAK ADDIVGPVTH ELVEKNTVHL KWQEPKEPNG LIVLYEVSYG
     RLGETEVRNC AELRKEQVWR SSSVLPLGLT PRGRLEAASA ETPLPSSVFL ATSLAGNGSW
     TEPAYFYVAD YLNAQPNIAV IIVPIIFAII LAGIIGAAYV LVKKRQTEGP TGPLYASSNP
     EYLSASDVYV PDEWEVPRDK ITLLRELGQG SFGMVYEGIA KDIVKGEPET RVAVKTVNES
     ASLRERIEFL NEASVMKGFS CHHVVRLLGV VSKGQPTLVV MELMAHGDLK SYLRSLRPDA
     ENNPGRPPPT LREMIQMAAE IADGMAYLNA KKFVHRDLAA RNCMVAEDFT VKIGDFGMTR
     DIYETDYYRK GGKGLLPVRW MAPESLKDGV FTTYSDVWSF GVVLWEISSL AEQPYQGLSN
     EQVLKFVMDG GYLDQPDNCP ERLHSLMQMC WQYNPKMRPT FIEIIEMLKE DLHPSFHEVS
     FFYSEENKPL ETEEYEMDFE NMESIPLDPS SYSQRDKALG RDDGPSMALK GNYEEHIPYT
     HMNGGKKNGR ILSMPRASPS
//
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