ID A0A0K0F496_STRVS Unreviewed; 1874 AA.
AC A0A0K0F496;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Strongyloides venezuelensis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_0363200.1};
RN [1] {ECO:0000313|Proteomes:UP000035680}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A, De Silva N.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SVE_0363200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the DUOXA family.
CC {ECO:0000256|ARBA:ARBA00009816}.
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DR STRING; 75913.A0A0K0F496; -.
DR WBParaSite; SVE_0363200.1; SVE_0363200.1; SVE_0363200.
DR Proteomes; UP000035680; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0098590; C:plasma membrane region; 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:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0000003; P:reproduction; IEA:UniProt.
DR CDD; cd00064; FU; 3.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR018469; Dual_oxidase_maturation_fac.
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; 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:SF566; EPIDERMAL GROWTH FACTOR RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF10204; DuoxA; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 6.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; 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 Reference proteome {ECO:0000313|Proteomes:UP000035680};
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 TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1346..1369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1410..1677
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1874 AA; 214681 MW; CFCDC4B0D4E896CA CRC64;
MISGWFDAFR ENGEPTWFNE IKSPLPTDIF IVAIFWLFLT PIAAFLIILP GVRNKKAISS
LSFLLAMSTG ATILVSIYYP GWHQSNGRIF SSYRSFSSGK IHAKIGVKIG LKHVNITLTS
LCENDLFENE TISQFSNQFL YNERFQFDEV STLSKELLIA TKKGLPYPIL KVVEYLSVNG
GGFPWGRQYR LAGYYASFCL WLAFGFWILK LTFLCFVPHH TFHISCIVGI SILAADIIYA
YNTPKPLIIR FEGPNKNVVD LVFSLSTCFY STLLVGTGSL LYGIVGWIMQ DFCGYQLKTF
FTGNIDDTVV PCREKIDLNW KMRYYAQNND KREMYRKQVS FQKNNNFSDC EKIRYKSENN
HSRPSLWDAY SSLSAIQHTL QNSNDNLKLK NDNLSPSLIN DPQYLGRLPV STIYSKEHQV
TINDSEIKED QITASIIIPD DNSESVMIIN NIKITRSSSL TNESSKESIW TEDDYSTSEF
TLTYSNSGQT NKMIRHLFIK DKIYILKLFL LLLTTVTSIS LDDGSVHASL HHHHHNHHHK
HSHYHNFLNG LKVCLGTSNG PSKLSNLSHY EMLKKQFSLC NRISGNLEIT HINGLEEIKD
GERPFGFLEN IEEIRGYLLI YQVENVPQII LPNLRVIWGD NLFDPTHREG KYSIYVGLTD
MEKLVFPNLT KIEKGFVEFN HFKKLCYLRE KIDWEQLLGS DYNNRVIFDD GSEYNTCNYD
NEIRECHPLC NGNCWGNSEN ECQIVFKNFC PISCHNHGCY KDHHGHYKCC DSMCTGGCFG
HGRSKCAACA NYIQDGECVQ SCRGLNYYNK ITGRLEDADD PRYTFKRYCV SECPSETLIE
KDYCVTRCKP KYFYNITLND RTCRECGSYC DKICEINQPL TKSNIKKLKN CEYVDGFIDI
SSEYFDRFNS ESLSISDLDY LKNVKLVTDY VIIKTGKSYI TNLNFLTNLE TIVGRKFYME
RVSLAIVHNN NLRELQLKNL KSINRGHVVI SNNENLCLAD TINWNITFPN TINKITRNGK
KEWCESNNIN YCGDQCDTSG CWGSGNKYCL SCKNVEYDGE CYGKCPPDTF RRNNSTKECV
KCHPECIGCN GETQYHCLEC LSLLVYQDDG NNYCSKTCPK THYLSNNNCI PCHKSCYDYG
CTGQSDILGE GGCNGCKFAK EDVNEMKEHL YTCLYYDGVA ENVCRDVGLT NYFTSTHKPK
NGMKVEYLVC QKCDDECESC SGIGKSVQMH DCKCTNKILI QNFNTTNIDE EEICVNECPI
NSFSMIEYGK PNICQSCHKL CDSHKSCYGP EFFQCESCEY AGFKKDDGTI ICTEECNSEF
PFINEYDRLC YSEDVVSLER HRRTKFIIIV GIILIIILII LIIAIWYCIN YRRKYRKEVE
LNMPSIPDYD LSKTQANMGR INLITIDQLE QTTQIIGQGA FGVVYAGKWK NPIKDCKNVP
VAIKVMKAIT SMDSKEILEE AGMMAQVSGG HKHLHPIIGI CLCDTVQIVT LLRPLGSLLH
FLKKHKDKLG ASKILLYCYQ ISSAMEYLAQ RGIVHRDLAA RNVLVKNINH VEVTDFGLAK
MLHGEECIKL SGKVAVKWLA IETLTQTIFN HATDVWAFAV TCWEILTFGQ APYQGISLSD
IKDHLLSGNR LEQPNNCSQE LYHTLLHCWM LNPEARPTFT LLTETFQNYC KAPHQYVTEY
HLHNKMEIIS NYEQFKMIAD LLNDEDIMDP LDYQDISQRS QNSYPNGNFF NDSLNSQTRP
LLPKYDAPCD NLTSSSLRYK EQSMDNKFEV VLGEEPENYL IPREIDEDAS SVYTDVVTMN
ECMAEYYNDP LKVQKLDNGN NLNHNYVNQD SIEMNVLKRQ DNVDDMDFYT TIDKDLEIIN
TPSSEVKIPS ETSV
//
