ID G3ER34_SOLIN Unreviewed; 1432 AA.
AC G3ER34;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=InR-1 {ECO:0000313|EMBL:ADZ56367.1};
OS Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Solenopsis.
OX NCBI_TaxID=13686 {ECO:0000313|EMBL:ADZ56367.1};
RN [1] {ECO:0000313|EMBL:ADZ56367.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21797944; DOI=10.1111/j.1365-2583.2011.01094.x;
RA Lu H.L., Pietrantonio P.V.;
RT "Insect insulin receptors: insights from sequence and caste expression
RT analyses of two cloned hymenopteran insulin receptor cDNAs from the fire
RT ant.";
RL Insect Mol. Biol. 20:637-649(2011).
RN [2] {ECO:0000313|EMBL:ADZ56367.1}
RP NUCLEOTIDE SEQUENCE.
RA Lu H.-L., Pietrantonio P.V.;
RL Submitted (FEB-2011) 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}.
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DR EMBL; JF304723; ADZ56367.1; -; mRNA.
DR RefSeq; NP_001291529.1; NM_001304600.1.
DR EnsemblMetazoa; NM_001304600.1; NP_001291529.1; LOC105207962.
DR GeneID; 105207962; -.
DR KEGG; soc:105207962; -.
DR OrthoDB; 1614410at2759; -.
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:0022008; P:neurogenesis; IEA:UniProt.
DR GO; GO:0000003; P:reproduction; IEA:UniProt.
DR CDD; cd00063; FN3; 3.
DR CDD; cd00064; FU; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
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 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; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
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, ECO:0000313|EMBL:ADZ56367.1};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1432
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003443296"
FT TRANSMEM 1026..1048
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 576..687
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 923..1021
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1085..1344
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 92..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1432 AA; 163244 MW; 5CD838B134F88AEE CRC64;
MKTRKSLLPI VLLCVTMASL AFCQEKRWPK AATKHRDKSA KGKYDPDYVD RIWQEEEEED
SAELYDRSSA ATGYYDSRSM DTMAAYRNNR AIEKSRSTDV RPKNNQQSSQ SSNLPKSHTK
SSEEVGREKG RRYKNMTIGD GICQSIDIRN SVDSFSVLKD CRVIEGFLQI VLIENNTEAD
FENVTFPELR EITGYFLLYR VDGLKSLIKL FPNLEVIRGD ILLTDYAFMI YEMKNLQEIG
LTNLTKISRG GVRIEKNPAL CFTNTVNWSL IVPAGENFIK DNRNEQSCPH VKGCSQCPGG
YCWTAQRCQK LERPKCHEQC LGECYGPSDT ECYVCKHYRH EGRCIENCPP NLYAYLSRRC
ISKDECQDMN HIRRLTKTEE IQIWRPFKNS CVTQCPDGYE DYVDDKNITA CQVCTGQCRK
FSKGAIIRHI SDAQSFRGIT VVKGALEFQI RNGNPNIMNE LADAFSLIEE ITEYLKITHS
FPITSLSFFK KLKVIKGEGL DLNNASLVVL DNPNLSSLFP PSQTITIENG RLFFHYNPKL
CLSKIEQFGK MVNITNFTDL EVQPESNGDK VACNIVNINI TVKKREADHV ILSWDSYKPP
EGQQLLNYLL NYIETENENI TYEANACGNN TWQIIDVGIP SWNSTVSKYI SNLKPYTKYA
AYVKTFTARN KKNSKNSFVT PVGQSEIIFF RTKSAIPSVP TNVTSTAISD SEILLKWAPP
VYPNGPIGYY MITSMIRLDD EKLVASRDYC VDTLVNEAKK EEIHEVTIKT SLAVSARTEV
ISNSNSCCVK DTTPKKSELF CHKNVTISNL SPGWKDYCIF NNYNSPESKF YDMTNNLSAS
MQEEKKSATD VSANAGSGNH LNEVRLYNAS SQNNTYLLEN LRHYSLYTIT IAACGVKIDG
NTPMCSSIQY ANIRTLKRLS SDDVQNVKVH VTNNTIVEVI WESVKDPNAF TVSYTIEYTN
LDVKDAKRST ECMPYIGHKE SYINHYIRNL SPGRYSLRIR STSLAGDGTF TNVVYFSVGL
SDNNQIMIVT LLILVLLFIV VLVIMLLIRN RQKKKTQERL IASVNPDYIE TKYVVDNWEV
PRENVEILEE LGLGNFGMVY RGYLDGTGQV AIKTISENAS QREKNEFLNE ASVMKNFSTW
HIIKLLGVVS MGNPPFVIME LMENGDLKTY LRRIRDTQMV PNESRIIRMA AEIADGMAYL
ESKKFVHRDL AARNCMVSKD LVCKIGDFGM ARDIYETDYY KIGKKGLLPI RWMAPENLSD
GVFTSDSDVW SFGVVLYEIL TLAEIPYQGF SNEEVLHHVL RKGMLNIPRN CPETIQKLTE
KCFKWRPSER PTFMEIVSEL EPFLGQDFCE KSFYHSDEGI EIRSLGIKKV YHNAAPIRFH
WGHETARWVK DFEDNVTLLD QMKAGTSRGR IFKNGFQHFG NVTNFEDVPL DR
//
