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Database: UniProt
Entry: A0A0N4VI05_ENTVE
LinkDB: A0A0N4VI05_ENTVE
Original site: A0A0N4VI05_ENTVE 
ID   A0A0N4VI05_ENTVE        Unreviewed;      1134 AA.
AC   A0A0N4VI05;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS   Enterobius vermicularis (Human pinworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX   NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0001045601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EVEC_0001045601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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   AlphaFoldDB; A0A0N4VI05; -.
DR   WBParaSite; EVEC_0001045601-mRNA-1; EVEC_0001045601-mRNA-1; EVEC_0001045601.
DR   Proteomes; UP000038041; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00064; FU; 3.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR032778; GF_recep_IV.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-dom_sf.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   SMART; SM00261; FU; 6.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   SUPFAM; SSF52058; L domain-like; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1134
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005887572"
FT   TRANSMEM        837..861
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          39..154
FT                   /note="Receptor L-domain"
FT                   /evidence="ECO:0000259|Pfam:PF01030"
FT   DOMAIN          170..328
FT                   /note="Furin-like cysteine-rich"
FT                   /evidence="ECO:0000259|Pfam:PF00757"
FT   DOMAIN          399..489
FT                   /note="Receptor L-domain"
FT                   /evidence="ECO:0000259|Pfam:PF01030"
FT   DOMAIN          534..637
FT                   /note="Growth factor receptor"
FT                   /evidence="ECO:0000259|Pfam:PF14843"
FT   REGION          996..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1017
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1134 AA;  127877 MW;  5DC7974C6E7AC1F1 CRC64;
     LSTILLLGTI FTDCVGSIDG VTRAGYSDNI DILRKQYSGC TIVFGNVVIA HLQQKAIGNQ
     TMEEMEKKLD FLNHIEQITG SLIIFATHLK SISFKRLKII WGDELHDGMA MLIEGNEELR
     HLKLPSLRSV ERGNITLNSN PYLCYLEKKV SFHEIVGEGA SERIWRKNES TLCSKESEPE
     CDRKCGQYCW GPGAENCQII YRQNCTDCHS GMCHFDNPSL PICCDDACAA GCTGQGSDHC
     VACKRLSQDG QCVERCNGLT SYDIVKMMTV PHEKPRYTHN RFCVPECPPT TIIENENCVH
     RCSKGYSYDA DSRPYVCKPC ENGICPKCTF ERLSCLLEEP LDSRNIERLK DCIIIEGYIF
     LSPYAFVEHL YIPPDLSQLT FEKSSDMDRF DFMNTTVPAI KEEQLEILST VRMVTQYVEI
     SLFDYSPTNL SFLRNLETIV GRKQRARQSL KIFSNSNLKY LGLKSLKKIL GGRVFITDNK
     ALCYANTQSR TWDDIIEEVP EAGHRKFRIE RNRNPSICGN AVIYICYYLQ GRRCSDSCDE
     DYGCWGPGSD QCVKCKYYYD GEQCLYSCSP IGNYVDGKNC LRCDEECVKC HGPSNEDCDK
     CKHVSLQRGL RKQCLRECPN THYENNGTCV PCHPACYAYG PMFFSCTGGS DIAGLGGCNK
     CEYGVELDGS IKCLSSENNS YSVCKENHLD NYFVHLETTD KIASYKCNKC PDECFSCTGF
     GTDTAKHECV CAAYVTHSPG NRSYCTAKCE TGSYLIKEKT ANNTGHCQIC HELCDHSYGC
     VGNKPSECER CKFAAVEKDG IQTCLDECPL GLHKYDDVNN VCHDIDPAAV VRRKKRIAAF
     SFVLCVVFAV VIAAVFGVNC WKYRNRYKKE LQLNPPALPE YKPMDPDDKP NMNQLRLISS
     EQLTKTSRPL GKGAFGIVYA VSWLENPDSR PTFVVLKTYF DSFCRVPNRY LVLKKRNPPL
     PMESMNNENQ RDLINEMMQD NDFMDPLTYF DEHDGPTTES TIIPPTPTTP AWSSNNETSG
     NSCNAILMSC QGRRLTNSDS TRYQSDPVHG DGSNIELSTD EGNYLVPNTK QSAVLYTPVV
     VHENSETDLL SPTHYYNENG TPEYYNELKP ADDKIPMIRS LANRDYFAEA ETAL
//
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