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Database: UniProt
Entry: E0VZ21_PEDHC
LinkDB: E0VZ21_PEDHC
Original site: E0VZ21_PEDHC 
ID   E0VZ21_PEDHC            Unreviewed;       656 AA.
AC   E0VZ21;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=8235006 {ECO:0000313|EnsemblMetazoa:PHUM523320-PA};
GN   ORFNames=Phum_PHUM523320 {ECO:0000313|EMBL:EEB18627.1};
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:EEB18627.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB18627.1};
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:EEB18627.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB18627.1};
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:PHUM523320-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM523320-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};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR   EMBL; AAZO01006351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS235849; EEB18627.1; -; Genomic_DNA.
DR   RefSeq; XP_002431365.1; XM_002431320.1.
DR   AlphaFoldDB; E0VZ21; -.
DR   STRING; 121224.E0VZ21; -.
DR   EnsemblMetazoa; PHUM523320-RA; PHUM523320-PA; PHUM523320.
DR   GeneID; 8235006; -.
DR   KEGG; phu:Phum_PHUM523320; -.
DR   CTD; 8235006; -.
DR   VEuPathDB; VectorBase:PHUM523320; -.
DR   eggNOG; KOG1026; Eukaryota.
DR   HOGENOM; CLU_000288_30_4_1; -.
DR   InParanoid; E0VZ21; -.
DR   OMA; SECKAML; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000009046; 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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07469; CRD_TK_ROR_related; 1.
DR   CDD; cd00108; KR; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_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:SF317; MUSCLE, SKELETAL RECEPTOR TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF01392; Fz; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00018; KRINGLE.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_2; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:EEB18627.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEB18627.1};
KW   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121};
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:EEB18627.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEB18627.1};
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   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..656
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011412778"
FT   TRANSMEM        289..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..172
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          185..264
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          362..641
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   656 AA;  75279 MW;  BB2F0455BDE6813B CRC64;
     MTKLIFELVF LLFLYNQKKC FAQEKEDQTL SSSAGYCALY RGEICKDYLV GSGYVWFNKS
     HDGGWLNEQI TTNLWKEIIV SLKEPCLSAA KKLLCAYAFP QCSLQDNNAI GLPLCAEDCT
     AVKHLFCHND WALIDYNKRR GIYLKSKGHF TLPNCENLPS FKNAKKPICS HAKLTEMPKE
     EITYDCIKGR GRFYQGNINH TQDGILCQRW DSQEPHIHLR PPNVFPEIEN AENFCRNAGG
     EEPTPWCYTV NSSIRWQHCS IPVCENSTGF KVNSENNFFS PFLLTPYNIL IFGAVGCAFL
     IVILLICVLF RKIRKYQSGY NNPNLRDINI DLEELPSNQA YHKTGAQLNP KLEKLEFPRN
     DIIFIRDLGQ GAFGRVFQAK APGLVKGEEF TLVAVKMLKD EASPDLQVDF EREACLLAEF
     DHPNIVKLLG VCAIGKPMCL LFEYMGRGDL NEFLRSCSPS NYIVRSVDDS GDFFKDVRLQ
     TLDLLSIAKQ VASGMVYLSD RKFVHRDLAT RNCLVDDNMS VKIADFGLSQ KIYLQDYYKG
     DEHDAIPVRW MPLESILFNK YTVETDVWAY GVCLWEIFSF ALQPYYGMNH EEVVKYIKEG
     KMLSCPDNTP WQVYELMKQC WNRKPQGRPS FRMICQTLDS IKDELTKGMN SLYISR
//
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