ID A0A091F769_CORBR Unreviewed; 1341 AA.
AC A0A091F769;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE Flags: Fragment;
GN ORFNames=N302_05592 {ECO:0000313|EMBL:KFO64687.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO64687.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO64687.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO64687.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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; KK719666; KFO64687.1; -; Genomic_DNA.
DR STRING; 85066.A0A091F769; -.
DR Proteomes; UP000052976; 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 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; 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; PF00041; fn3; 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; 3.
DR SMART; SM00261; FU; 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; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 4: Predicted;
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000620-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:KFO64687.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 919..943
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 817..912
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 982..1257
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 707..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 992
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1016
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1063..1069
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:KFO64687.1"
FT NON_TER 1341
FT /evidence="ECO:0000313|EMBL:KFO64687.1"
SQ SEQUENCE 1341 AA; 151724 MW; 4A6ACF19A4CCCF90 CRC64;
VCRSMDIRNN LTRLNMLENC TVIEGHLQIL LMFKTKPEDF RELSFPKLTM ITDYLLLFRV
YGLESLKGLF PNLTVIRGTR LFFNYALVIF EMVHLKEIGL YNLMNITRGA VRIEKNNELC
YLSTIDWSRI LDSVEDNYIV ANKDDKEECG DVCPGTVKGK SNCPPTVING IFIERCWTHD
RCQRVCPPAC KSQGCTSDGQ CCHSECLGDC TEPNDPDKCV ACRNFYLDGR CVDNCPPGHY
RFEGWRCVTF SFCQELHNKC KNARESGCHV IHNNECVHEC PSGYIMNSSN LHCTPCAGPC
PKVCDFGKEK 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 VYWQQQAEDS ELYELDYCLK GLKLPSRTWS PPFESEDPQK
YNQSEAEDVS GECCSCPKTD SQIQKELEES AFRKTFENYL HNEVFVPRRR NSTREGRGKQ
GRPSRKRRDL SSVANSTVVL PTIPSSPNNS AAAEGAEEQK PFEKVLSKES LVISGLRHFT
GYRIELHACN HDAQESRCSV AAYVSARTMP EAKADDIVGP VSHELVEKNT VHLKWQEPKE
PNGLIVLYEV NYGRLGETEE AHFCVSRKHF ASESGCKLRG LQPGNYSVRI RATSLAGNGS
WTEPTYFYVA DYLNAQPNIA VIIVPIIFAI IIAGIIGAAY VLVKKRQTEG PTGPLYASSN
PEYISASDVY VPDEWEVPRD KITLLRELGQ GSFGMVYEGI AKDIVKGEPE TRVAVKTVNE
SASLRERIEF LNEASVMKGF SCHHVVRLLG VVSKGQPTLV VMELMAHGDL KSYLRSLRPE
AENNPGRPPP TLREMIQMAA EIADGMAYLN AKKFEKGNVL NVNHEVTDEC RLGFGNFGMT
RDIYETDYYR KGGKGLLPVR WMAPESLKDG VFTTYSDVWS FGVVLWEISS LAEQPYQGLS
NEQVLKFVMD GGYLDQPDNC PERLHSLMQM CWQYNPKMRP TFIEIIEMLK EDLHPSFQEV
SFFYSEENKP LETEEYEMDF ENMESIPLDP SSYSQRDKVL GRDNGPSMAL KGNYEEHIPY
THMNGGKKNG RILSMPRSSP S
//