GenomeNet

Database: UniProt
Entry: Q9U5A8_BOMMO
LinkDB: Q9U5A8_BOMMO
Original site: Q9U5A8_BOMMO 
ID   Q9U5A8_BOMMO            Unreviewed;      1472 AA.
AC   Q9U5A8;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN   Name=BIR {ECO:0000313|EMBL:AAF21243.1};
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091 {ECO:0000313|EMBL:AAF21243.1};
RN   [1] {ECO:0000313|EMBL:AAF21243.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Ovary vitellogenic follicles {ECO:0000313|EMBL:AAF21243.1};
RA   Lindstrom-Dinnetz I., Iatrou K.;
RT   "Cloning and functional characterization of an insulin receptor-like mRNA
RT   expressed in the silkmoth ovary.";
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p50T {ECO:0000313|Proteomes:UP000005204};
RX   PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG   International Silkworm Genome Consortium;
RT   "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL   Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN   [3] {ECO:0000313|EnsemblMetazoa:NP_001037011.1}
RP   IDENTIFICATION.
RC   STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:NP_001037011.1};
RG   EnsemblMetazoa;
RL   Submitted (JUN-2022) to UniProtKB.
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   -!- 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}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily.
CC       {ECO:0000256|RuleBase:RU000312}.
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; AF025542; AAF21243.1; -; mRNA.
DR   RefSeq; NP_001037011.1; NM_001043546.1.
DR   SMR; Q9U5A8; -.
DR   EnsemblMetazoa; NM_001043546.1; NP_001037011.1; GeneID_692560.
DR   GeneID; 692560; -.
DR   KEGG; bmor:692560; -.
DR   CTD; 42549; -.
DR   HOGENOM; CLU_000288_166_5_1; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
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: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: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; 2.
DR   CDD; cd00064; FU; 1.
DR   CDD; cd05032; PTKc_InsR_like; 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   InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
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   PIRSF; PIRSF000620; Insulin_receptor; 1.
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; PS51257; PROKAR_LIPOPROTEIN; 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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000620-
KW   2}; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000620-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW   ECO:0000256|RuleBase:RU000312};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005204};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000312};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          663..767
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          909..1014
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1082..1360
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1426..1472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1433..1451
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1221
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT   BINDING         1092
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1163..1169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1225..1226
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ   SEQUENCE   1472 AA;  164583 MW;  CB6631C67906AF8E CRC64;
     MLEVRRGVMR RACDRLGWPA VACALLIACA RTYAGTEVVP ARGVCPSMDL RNNPDQIRRL
     EGCRVIEGQL SIVLMERATN KIFDNMSFPQ LREVTGYILI YKTKGLRNLG DLFPNLPVVR
     GMQLFKDFAL VIFDNEHLEA LGLNSLMKIE RGGVRIQHND RLCYTNTIDW SRITRDDAEI
     IVRSNYDTRL CGLCPNAQSR VEEDHRQSLP QCPADTKGKL LCWDEKHCQK ICPSACGDHG
     CMSNGTCCNS ACLGGCDGPL ASNCFVCKKF SFEYGSEMTC MESCPGGTYE LSRRCVTEQE
     CRSMSPPPQP VGAADSTYFR FAIKVPAYKT FNSSRCLFMC PSGYMEVGNE TNATCQPCPR
     SGCVRECLGG KIDSVATAEQ FRGCTHIKGK MEFTLRSSGG KTLSLLESAL GEIREIHGCL
     QVTRSYPLVS LMFLKKLRKI IANPSEDKGE ALHIINNENL ELLWDWSTYG PIEIIGSCYI
     HSNPKLCYTQ LMPLMNMSYP KTNFTELEVS QDSNGYQASC LPDVLKLSVS ELTQIAVVLT
     WDVYCPDDMR KLLGYSLYFM ATEKNVSLYD QRDACSDIWK VLDKPIEETR KVNRNAKPSH
     ARNKTEVIFN PCADMQPLFY PITQLRPYTR YAAYVKTYTT IQDRKGAQSS IIYFRTLPMQ
     PSPPTAVTVE LLTPHSIFIK WSPPTMPNGT IILYHVEVQA NSYNRPQILA GNINYCGNPS
     ILANMIKASL EEAPETPEEK ITGDVKNGVC ACKEEAKPSL RFSTRAEEER VDSINFENEL
     QNQVYRKSER VNPKIHKSID GTSKVKRSVD HSLNSMLVKL TENNSPRPGL NYSNITDDEG
     YVKSLYYELD GSTRTLTVKN MRHFTWYTVN IWACRNKDLN ETDPVYAENW CSVRAYNTFR
     TLELPNADVV SNFQVEIMPA NKTLPEVNVT WEPPLNPNGF VVAYNVHYSR IEDSAQGPDV
     GLQSCITVDD YEANGHGYVL KTLSPGNYSV KVTPITVSGA GNVSEEIYVF IPERVSESGH
     AWAWGVGAGG VVLALLVGAA VWYARRGLMS HAEASKLFAS VNPEYVPTVY VPDEWEVTRD
     SIHFIRELGQ GSFGMVYEGI AKEIVKGKPE TRCAIKTVNE HATDRERIEF LNEASVMKAF
     DTFHVVRLLG VVSRGQPTLV VMELMERGDL KTYLRSMRPD AEGSLPSSPP VPPTLQNILQ
     MAIEIADGMA YLSAKKFVHR DLAARNCMVA GDLTVKVGDF GMTRDIYETD YYRKGTKGLM
     PVRWMSPESL KDGVFSSSSD AWSYGVVLWE MATLAMQPYQ GLSNEQVLRY VVEGGVMERP
     EQCPDRLYEL MRACWTHRPS ARPTFLQLVA DLVPHAMPYF RHRSFFHSPQ GQELYALQRS
     ALDEEQELPE VDVGAVATGS VSNLFGVSGR LASWVRELSS LRSRGSDDAA AEPLQPLPPP
     GTSPAPILAP APAIKGPNGV LRDSHSARFR NH
//
DBGET integrated database retrieval system