ID A0A0N0U3X6_9HYME Unreviewed; 1670 AA.
AC A0A0N0U3X6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=WN51_02650 {ECO:0000313|EMBL:KOX70594.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX70594.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX70594.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX70594.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX70594.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) 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; KQ435859; KOX70594.1; -; Genomic_DNA.
DR STRING; 166423.A0A0N0U3X6; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000053105; 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: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; 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.
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, ECO:0000313|EMBL:KOX70594.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1670
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005859796"
FT TRANSMEM 1171..1196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 695..810
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1063..1166
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1230..1483
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 206..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..991
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1670 AA; 190413 MW; 055F8480829277CA CRC64;
METRCLLMIV VFLCAAMSLA CCQSNGISSR TSIGDDNDEI RRYEADYTDG SNEETMLENH
EADLDSDDPF YEQIVSYRSN RAIDVFSYQR EDDRLFITIY VDDIVSDDHE SIKNVKTELA
NDFDTKEIYS KKVERRTNGC HTVCTSMNED FTLEKGDSTE NQSSPNAKPL KPSFLNVQTN
LDHGLYLTSN PEVNSLPQMM NRSTEANTKL TEQSGQKPNL PKSSTKATET VVREKGRRRV
SNKHVMIGDG ICQSIDIRNS ASAFGILKDC RVIEGFLQIV LIENNSERDF QPISFPKLRE
ITGYILLYRL NGLKSLNNLF PNLEVIRGDI LLTDYAFMVY EMQNLQELTL SGAESTGNSF
LQIGLKKLTE ISRGSVRIEK NPALCYTTLN WSFIVSAGEI VIKDNGEEAS CPGCSHCPGG
YCWTSQYCQR TEKPKCHDQC LGECLGSTES ECYVCKHYRH EGKCVETCPS HLYSYLSRRC
VTKDECVGMN RLRRVILEDG QAWRPFNGSC VTHCPDGYED ALDENNMTTC RACVNSCRKV
SHGALIRHIS DTQSFRGITV VKGALEFQIR NGNPSIMNEL SEAFGRVEEI TEYLKITHSF
PITSLNFFKK LKVIKGEKLD TNNASLSVLD NPNLSSLFPP GQEIKIENGR LFFHYNPKLC
LSTIKQLSVM VNITNYTDLE VQPQSNGEKV ACDIVNINIT VKNLGPDYAD LMWDSYEPPE
GHKLLSYLLN YIETENENIT YEMNACGGNK TWQIVDVDIP KWNTTVSKHI SSLKPYTKYA
VYVKTLNARS SKFVEPVGQS RIIFFRTRST IPSPPTNVLS MSLSDTEILV KWEPPLFPNG
RIGYYMVSSV VIYEDDNLIF TRDYCNDTLE DELEPDQLVV PDVTVKTPVA NRLSCCSKNT
NGYVVTSKKF EIFCHENTTI SYISPGWKDY CVYNTYNNNN NNNKNNKNVH DQFYELTNNL
STPRPEDEEE KEEEEEEEEE KEEEEEEEEE TDTFKSKGSN VMDKHALTYN VSDRNEFVIK
NLSHYTRYII SVAACGVKIN KLSMCSSIQY TFARTKKRVH ADDVKNVKVQ VTNNTIVEVF
WDSVKDPNAM TVSYTIEYTN LDVKDAKKST ECVRNLRIPR KDTLSAVNSY FIKNLSPGKY
SLRVRSTSLA GDGNFSNVVY FSIGLSNTTP ITLIAVIAVV VLLAILTVLF ASLRYYRKKK
KQERLIASVN PDYIETKYVI DEWEVPRENV EILEELGLGN FGMVYRGVYD KNTPVAIKTI
SKTASPREKN EFLNEASVMK NFSTFHIIKL IGVVSIENPP FVIMELMENG DLKTYLRRIR
DTHLVPDACR IMRMAAEIAD GMAYLESKKY VHRDLAARNC MVSKDLVCKI GDFGMARDVY
ETDYYKIGRK GLLPIRWMAP ENLSDGVFTS DSDVWSFGVV LYEILTLAEI PYQGFSNEEV
LSHVNIPRSC PENIQKIMEK CFKWRPSDRP TFMEVVSELE PFLGQDFYEK SFYHSTEGVE
SRNSGMKKPY HHAAPIRFHW ANETARWVKE FEDNVTLLDQ TKAGTSRGRI FKNGFQHFGN
QVYINEVLPW KEKAFKNRRE ENVCLQIAII YLEETSERQK LPSNNEFAVF CEEASGRGHA
HVQAVSAVKS TGNEFCEWYD TEENFEGPNS EVILRGCISC CDIIERHEVK
//
