ID D0UYA5_DROME Unreviewed; 2040 AA.
AC D0UYA5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 Name=InR {ECO:0000313|EMBL:ACY01712.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:ACY01712.1};
RN [1] {ECO:0000313|EMBL:ACY01712.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Isoline SL5_82 {ECO:0000313|EMBL:ACY01712.1};
RX PubMed=20074316; DOI=10.1111/j.1365-294X.2009.04508.x;
RA Paaby A.B., Blacket M.J., Hoffmann A.A., Schmidt P.S.;
RT "Identification of a candidate adaptive polymorphism for Drosophila life
RT history by parallel independent clines on two continents.";
RL Mol. Ecol. 19:760-774(2010).
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; GQ927239; ACY01712.1; -; Genomic_DNA.
DR VEuPathDB; VectorBase:FBgn0285896; -.
DR HOGENOM; CLU_000288_166_2_1; -.
DR ChiTaRS; InR; fly.
DR ExpressionAtlas; D0UYA5; baseline and differential.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
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:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0022008; P:neurogenesis; IEA:UniProt.
DR GO; GO:0000003; P:reproduction; IEA:UniProt.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00064; FU; 1.
DR CDD; cd05032; PTKc_InsR_like; 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; 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; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF525; INSULIN-LIKE RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00261; FU; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
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; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1160..1255
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1321..1609
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 179..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1640..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1738..1821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1836..1912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1970..2040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1778..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1970..1991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2025..2040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1355
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:ACY01712.1"
FT NON_TER 2040
FT /evidence="ECO:0000313|EMBL:ACY01712.1"
SQ SEQUENCE 2040 AA; 228468 MW; 916480298D1CF41C CRC64;
MLLDTCCCRQ AVEAVDSPAS SEEAYSSSNS SSCQASSEIS AEEVWFLSHD DIVLCRRPKF
DEVETTGKKR DVKCSGHQCS NECDDGSTKN NRQQRENFNI FSNCHNILRT LQSLLLLMFN
CGIFNKRRRR QHQQQHHHYQ HHHQQHLQRQ QANVSYTKFL LLLQTLAAAT TRLSLSPKNY
KQQQQLQHNQ QLPRATPQQK QQEKDRHKCF HYKHNYSYSP GISLLLFILL ANTLAIQAVV
LPAHQQHLLH NDIADGLDKT ALSVSGTQTR WPRSESNPTM RLSQNVKPCK SMDIRNMVSH
FNQLENCTVI EGFLLIDLIN DASPLNRSFP KLTEVTDYII IYRVTGLHSL SKIFPNLSVI
RGNKLFDGYA LVVYSNFDLM DLGLHKLRSI TRGGVRIEKN HKLCYDRTID WLEILAENET
QLVVLTENGK EKECRLSKCP GEIRIEEGHD NTAIEGELNA SCQLHNNRRL CWNSKLCQTK
CPEKCRNNCI DEHTCCSQDC LGGCVIDKNG NESCISCRNV SFNNICMDSC PKGYYQFDSR
CVTANECITL TKFETNSVYS GIPYNGQCIT HCPTGYQKSE NKRMCEPCPG GKCDKECSSG
LIDSLERARE FHGCTIITGT EPLTISIKRE SGAHVMDELK YGLAAVHKIQ SSLMVHLTYG
LKSLKFFQSL TEISGDPPMD ADKYALYVLD NRDLDELWGP NQTVFIRKGG VFFHFNPKLC
VSTINQLLPM LASKPKFFEK SDVGADSNGN RGSCGTAVLN VTLQSVGANS AMLNVTTKVE
IGEPQKPSNA TIVFKDPRAF IGFVFYHMID PYGNSTKSSD DPCDDRWKVS SPEKSGVMVL
SNLIPYTNYS YYVRTMAISS ELTNAESDVK NFRTNPGRPS KVTEVVATAI SDSKINVTWS
YLDKPYGVLT RYFIKAKLIN RPTRNNNRDY CTEPLVKAME NDLPATTPTK KISDPLAGDC
KCVEGSKKTS SQEYDDRKVQ AGMEFENALQ NFIFVPNIRK SKNGSSDKSD GAEGAALDSN
AIPNGGATNP SRRRRDVALE PELDDVEGSV LLRHVRSITD DTDAFFEKDD ENTYKDEEDL
SSNKQFYEVF AKELPPNQTY FVFEKLRHFT RYAIFVVACR EEIPSEKLRD TSFKKSLCSD
YDTVFQTTKR KKFADIVMDL KVDLEHANNT ESPVRVRWTP PVDPNGEIVT YEVAYKLQKP
DQVEEKKCIP AADFNQTAGY LIKLNEGLYS FRVRANSIAG YGDFTEVEHI KVEPPPSYAK
VFFWLLGIGL AFLIVSLFGY VCYLHKRKVP SNDLHMNTEV NPFYASMQYI PDDWEVLREN
IIQLAPLGQG SFGMVYEGIL KSFPPNGVDR ECAIKTVNEN ATDRERTNFL SEASVMKEFD
TYHVVRLLGV CSRGQPALVV MELMKKGDLK SYLRAHRPEE RDEAMMTYLN RIGVTGNVQP
PTYGRIYQMA IEIADGMAYL AAKKFVHRDL AARNCMVADD LTVKIGDFGM TRDIYETDYY
RKGTKGLLPV RWMPPESLRD GVYSSASDVF SFGVVLWEMA TLAAQPYQGL SNEQVLRYVI
DGGVMERPEN CPDFLHKLMQ RCWHHRSSAR PSFLDIIAYL EPQCPNSQFK EVSFYHSEAG
LQHREKERKE RNQLDAFAAV PLDQDLQDRE QQEDATTPLR MGDYQQNSSL DQPPESPIAM
VDDQGSHLPF SLPSGFIASS TPDGQTVMAT AFQNIPAAQG DISATYVVPD ADALDGDRGY
EIYDPSPKCA ELPTSRSGST GGGKLSGEQH LLPRKGRQPT IMSSSMPDDV IGGSSLQPST
ASAASSNASS HTGRPSLKKT VADSVRNKAN FINRHLFNHK RTGSNASHKS NASNAPSTSS
NTNLTSHPVA MGNLGTIESG GSGSAGSYTG TPRFYTPSAT PGGGSGMAIS DNPNYRLLDE
SIASEQATIL TTSSPNPNYE MMHPPTSLVS TNPNYMPMNE TPVQMAGVTI SHNPNYQPMQ
APLNARQSQS SSDEDNEQEE DDDVDDEHVE HIKMERMPLS RPRQRALPSK TQPPRSRSVS
//
