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Database: UniProt/TrEMBL
Entry: E0VXW7_PEDHC
LinkDB: E0VXW7_PEDHC
Original site: E0VXW7_PEDHC 
ID   E0VXW7_PEDHC            Unreviewed;      1289 AA.
AC   E0VXW7;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-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};
GN   Name=8232943 {ECO:0000313|EnsemblMetazoa:PHUM506080-PA};
GN   ORFNames=Phum_PHUM506080 {ECO:0000313|EMBL:EEB18223.1};
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC   Pediculus.
OX   NCBI_TaxID=121224;
RN   [1] {ECO:0000313|EMBL:EEB18223.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB18223.1};
RA   Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA   Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA   Amedeo P., Strausberg R.;
RT   "Annotation of Pediculus humanus corporis strain USDA.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB18223.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB18223.1};
RG   The Human Body Louse Genome Consortium;
RA   Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT   "The genome of the human body louse.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:PHUM506080-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM506080-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; AAZO01006149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS235841; EEB18223.1; -; Genomic_DNA.
DR   RefSeq; XP_002430961.1; XM_002430916.1.
DR   STRING; 121224.E0VXW7; -.
DR   EnsemblMetazoa; PHUM506080-RA; PHUM506080-PA; PHUM506080.
DR   GeneID; 8232943; -.
DR   KEGG; phu:Phum_PHUM506080; -.
DR   CTD; 8232943; -.
DR   VEuPathDB; VectorBase:PHUM506080; -.
DR   eggNOG; KOG4258; Eukaryota.
DR   HOGENOM; CLU_000288_166_0_1; -.
DR   InParanoid; E0VXW7; -.
DR   OMA; HRCWHHR; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000009046; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0000003; P:reproduction; IEA:UniProt.
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   PANTHER; PTHR24416:SF525; INSULIN-LIKE RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00041; fn3; 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; 2.
DR   SMART; SM00261; FU; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:EEB18223.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW   Transferase {ECO:0000313|EMBL:EEB18223.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        879..900
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1228..1255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          771..871
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          937..1212
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1265..1289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         971
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1289 AA;  147281 MW;  DD6F34E0C7F91DE3 CRC64;
     MTNRACKSCN ELINNITFPE LREVTGYVIF WRVQGLRSFG TLFPNLSVIR GKTLFHNYAL
     VIYESKALQE IGLYSLTHIL RGSVRFDENS NLCFVDTIDW DWIAPQGAKE HFIGDNRPIE
     ECLKCPISVN NEKCPLSSSG EPLCWNKEHC QKDFRDCVKD ENGECCHESC LGGCSGKLSK
     DCYVCKNVVF KNDCTQECPE NMYKYLDRRC VTESECFNMT KPLDVEKRDI ASPFPFRPIL
     DMCTLECPAN FSEYEKETEY GLRFQCRPCD GPCKKECPGG SINSISSAQK FAGCTHIKGS
     LEIHLRFAGN IVTELQESLR SVEEISGYLK VARSLPLLSL DFLKNLKVIR GEELHNNKSA
     FVLLDNERLE ELWDWDAREK DLRILNGRLA IHFNPKLCFY KIEKFVEIVK IKGFTEDEVP
     RGTNGDKEAC ELSVVGCCRL FSFPNKVVIR FEKFQHYDQR TLLGYVLYFK KAPNKNVTLY
     YGRNACGGDG WMDKDVPAPK QDNHQNEISY DLIGLKPFTQ YAYFIKTYAI SSERSGARSG
     IQYFITNPGT PTSPRSLFAF SNSTSEVVIS WEPPAEMNGN FTHYFVEAEA MEDHPKSRDF
     CSEPLVIATK KLEIPTSPPP AVKTSSDSCA CEAPRKVDLK VSEAVRDSEI YFENALQNSF
     IVRSCYHHYH YFLSFFRTDN KRTKREMNYA EGSHPQILQK NHFFNEGVGG KSFGNTKKEK
     VSFTFEVRTN KLVVRNLNYF TNYKIQVQAC RAVVEGENGV HSPCKTADKI PVITLIPLTS
     NGTVEETNLR WEEPPNPNGL ILSYQIEYRR VDNDKYKSVV ECIVREKFLE QKKEYVLKHL
     PPGNYSVRVL ASSLAGDGPY SSPLTFYIRQ PPHPSTIDIL GIGLGAICGI AFIFILYMFW
     KRKTSGVPKL FANVNPEYVS AATIYVPDEW EVPRENIELI RELGQGSFGM VYEGIARDIV
     QGEPEVRCAV KTVNEVSTDR DRMEFLNEAS VMKAFNTHHV VQLLGVVSEG QPTLVVMELM
     VNGDLKTYLR SHRPEFCEDK KKQPPTLRRI IRMAMEIADG MAYLAAKKFV HRDLAARNCM
     VAEDLTVKIG DFGMTRDIYE TDYYKKGTKG LLPVRWMAPE SLKDGVFTTH SDVWSYGIVL
     WEMVTLASQP YQGLSNDQVL RYVIEGGVME RPENCPNKLY DLMKLCWQHK PSSRPHFMSF
     VTKLLPDASP EFCEKSYYHS REGQELRWFI IFSLSLSLSF SFVLYRLIFF CFWNVQSAFR
     SSGKFENESI SNDGGDDSDD DDRDSITIS
//
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