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Database: UniProt
Entry: B0XG56_CULQU
LinkDB: B0XG56_CULQU
Original site: B0XG56_CULQU 
ID   B0XG56_CULQU            Unreviewed;       749 AA.
AC   B0XG56;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=6052339 {ECO:0000313|EnsemblMetazoa:CPIJ018269-PA};
GN   ORFNames=CpipJ_CPIJ018269 {ECO:0000313|EMBL:EDS27231.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS27231.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS27231.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ018269-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ018269-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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};
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DR   EMBL; DS232991; EDS27231.1; -; Genomic_DNA.
DR   RefSeq; XP_001868628.1; XM_001868593.1.
DR   AlphaFoldDB; B0XG56; -.
DR   STRING; 7176.B0XG56; -.
DR   EnsemblMetazoa; CPIJ018269-RA; CPIJ018269-PA; CPIJ018269.
DR   GeneID; 6052339; -.
DR   KEGG; cqu:CpipJ_CPIJ018269; -.
DR   VEuPathDB; VectorBase:CPIJ018269; -.
DR   VEuPathDB; VectorBase:CQUJHB010416; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   HOGENOM; CLU_000288_74_1_1; -.
DR   InParanoid; B0XG56; -.
DR   OMA; SIGNSHH; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0022008; P:neurogenesis; IEA:UniProt.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
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:SF550; FIBROBLAST GROWTH FACTOR RECEPTOR HOMOLOG 1-RELATED; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 3.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
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|PROSITE-ProRule:PRU10141};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:EDS27231.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW   Signal {ECO:0000256|SAM:SignalP};
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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..749
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011409378"
FT   TRANSMEM        335..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          125..215
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          217..317
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          433..710
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        574
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         467
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         579
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         592
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ   SEQUENCE   749 AA;  85220 MW;  0ADC5DF1F0B034E1 CRC64;
     MAILLGVTLV LLITLVITQQ PATFRINLVR RQILNRTVPL HSNVTIRCDL DDPQWFRNAS
     YVIPQDARVI PLYGIESDDA GFYSCRSSRG EWAHLGLLVE DRLTGRVGDG LERVSKDLEW
     AASVPFFVDE SQLITKRTQL VGSTVLMKCT GDGNPKPGIV WTKDGRKIVR KAGRVEDMQW
     AIVLEKLDVN DSGSYRCNVC NRVGCISFTT ELEVKEPSRQ AAIVYTYLQN TTLEVGCEAR
     FECSKEPDLE QRVEWIRFHM VDKTKPEIPE NVTKPRGSSN DGEEVLLLRN VTHDDEGWYT
     CVATSARGVF YQSAYLRVVD ELENVELIID QYTSAMILVI SLSVAFCVIA SMVVFICIKL
     RINQKKYFNY WIKTVTVSHM PAVGGTVKSF QLPVVHIETH RMAVAKNEYY EAADVSEYEF
     PIDWSWEFSR DKLTLGDTLG EGAFGRVVMA EAHGLLEKDQ TSKVAVKMLK KGHTDVDVKN
     LVCEMEVMKL IGKHFNIINL LGCCCKDGPL FVIVEYAAHG NLKEFLRSHR LQTTVNSPID
     GDQRILTPKQ QISFAFQIAR GMEHLSSMQC IHRDLAARNV LVTEGLVMKI ADFGFARDIH
     DREYYRRKSD SKLPVRWMAP ESLEERFYDT RSDVWSFGVV MWEIMTFGSH PYPSIPAWDD
     LLEFLKQGKR LEQPQHCSDE VYALMNKCWE FKPGERPPFS EIVWGLDQLI SAITSEEYLD
     LGVPESQAST ASLHDDEEKK VYISAEEIV
//
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