ID A0A0J9XVS1_BRUMA Unreviewed; 1338 AA.
AC A0A0J9XVS1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=Bm2256 {ECO:0000313|EMBL:CDP96229.1,
GN ECO:0000313|WormBase:Bm2256b}, BM_Bm2256
GN {ECO:0000313|EMBL:CDP96229.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CDP96229.1};
RN [1] {ECO:0000313|EMBL:CDP96229.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP96229.1};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CDP96229.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP96229.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN856957; CDP96229.1; -; Genomic_DNA.
DR WormBase; Bm2256b; BM43351; WBGene00222517; -.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF527; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ROS; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 813..838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 482..602
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 711..809
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 886..1158
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1195..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 921
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1338 AA; 149579 MW; 55F185752C47DFD0 CRC64;
MDLFWEEPTE WNGEALGYLV NCTVDGVSES VAEVPATIRF YSFSVKSGSV SCAVAAHNEP
KLETFSETVT IDSSELRPLV RLFAIDSNNN VFAITNWSPS SSQQSTRAKR QTSSLLAIME
QSIAYIGNDL YSIRKDFGST QPSLLRLDPN NVENILHKVS IGGEIGKVDA MTSDWVANRL
LFVSTARVMQ LPLDAIQSLS MITPRRIMNL SSGAGDAKQL LFDPFSNTAF LLTKNGSLFA
LDLNMGVEEN MALRLECLKS ETVSWMMADF AWNLASLPVI YVLTWNGMVR VDLTSSKCEE
IKFAWEKFGE KGLKSILSFA IADKLYIFVT SSALVVYELG SSTVTPIAVN GSPLKQILVA
TQSTQPFPER SCFVLPPASE IKFTVQNEER SGALISVNEP QLPNVCPGIT LPLTQYEIHF
QRRGSDKIRS IHSISNVLHV ENGVLDKEAD YDISVSWFNR YTPVSEASAT QMLRTGYGFP
SSPLDPLAFA LTPDIVLLYW KLPARPNAPI PEIKYMISQL SATQISPSAI GAQQFEGANY
AIMPTDVVSC LSNPCSAKIS NLRPSTEYKF WVRAIHESHL NMQFVDDAEG SSVEASVRTK
DIAGTLRLDN ITGTAVVLRW NSLDPECYPK RIYIQYRIVG TNTVWKSPYN ASFEGSAKSV
AVVVRALHSA TTYDYRFTAE YVDSYHYADH DYFYNETFLQ VSQQFRTKPG TPSAPASIRL
VQEHNEWVVR WDKPLSDGGS PITSYALEFR PNEDAEWEIA ERGLEGGCLW WKPLRINFLA
ECAEFRIRAA NSEGFGAYAY SKHHSGESHT HSLWIIIVTL LIAILLLTAV IAVLFIYYQR
IDGRHNNIRS QDISLHGYTN SMKRNIFPPQ LINDLKIISR VPKNNISLLR IIGKGGFGEV
YEGVANGLPQ SPTKTIRVAV KTLRNGFSES DRIKFLQEAV LMNSFDHPNI VKLLGVSLET
EPYFLIAELM EGGDLLGFLR SSRPSDCFPS QLSLYELIGM MVDVGRGAAY LEVKKRIHRD
LAARNCLISS RNSNTRITKI GDFGHARDIY TNDYYRVHGD DFLPLRWLSP ESINDGIFTS
KSDVWSFGIL LWEILTLGQQ PFSGKNNVQV MSFVKNGGRP EKPQFCPDEI FTIVERAWVY
DPEERPRFAD LLPELEALRG CPLYQEDIPY PPNCSSLITD SNFEFSFNSN ISRGESGHSG
SIRFDKSDNP SAKKQGRPSI LRSLRRERSR PFSNLADLEA GNRSRSVNSV TNDMNSSTRN
CDEGYDNSIF ISNCCYEVPK KSHTKKSQLN RSKQRASELP NRSPVSSSSS PLSSPRTPSS
GNSDIPSMYI RPARVSRV
//
