ID PTKL_PLAF7 Reviewed; 1501 AA. AC Q8IIT5; DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 2. DT 27-NOV-2024, entry version 136. DE RecName: Full=Inactive protein tyrosine kinase pTKL {ECO:0000305}; DE AltName: Full=PfpTKL {ECO:0000303|PubMed:31148576}; DE AltName: Full=Pseudo-tyrosine kinase-like protein {ECO:0000303|PubMed:31148576}; GN Name=pTKL {ECO:0000303|PubMed:31148576}; GN ORFNames=PF3D7_1106800 {ECO:0000312|EMBL:CZT98734.1}; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450}; RN [1] {ECO:0000312|Proteomes:UP000001450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450}; RX PubMed=12368864; DOI=10.1038/nature01097; RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D., RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S., RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M., RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A., RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I., RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J., RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.; RT "Genome sequence of the human malaria parasite Plasmodium falciparum."; RL Nature 419:498-511(2002). RN [2] {ECO:0000305} RP LACK OF CATALYTIC ACTIVITY, INTERACTION WITH SERA5 AND PP1C, AND DOMAIN. RX PubMed=31148576; DOI=10.1038/s41598-019-44542-3; RA Gnangnon B., Freville A., Cailliau K., Leroy C., De Witte C., Tulasne D., RA Martoriarti A., Jung V., Guerrera I.C., Marion S., Khalife J., Pierrot C.; RT "Plasmodium pseudo-Tyrosine Kinase-like binds PP1 and SERA5 and is exported RT to host erythrocytes."; RL Sci. Rep. 9:8120-8120(2019). CC -!- SUBUNIT: Interacts (via RVxF motif 1 and/or 2) with phosphatase PP1C CC (PubMed:31148576). May interact (via SAM domain) with SERA5 (via C- CC terminus) (PubMed:31148576). {ECO:0000269|PubMed:31148576}. CC -!- SUBCELLULAR LOCATION: Parasitophorous vacuole CC {ECO:0000250|UniProtKB:A0A509AIU5}. Host cell membrane CC {ECO:0000250|UniProtKB:A0A509AIU5}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:A0A509AIU5}. Host cytoplasm, host cytoskeleton CC {ECO:0000250|UniProtKB:A0A509AIU5}. Host cytoplasm CC {ECO:0000250|UniProtKB:A0A509AIU5}. Note=During the trophozoite stages, CC secreted into the parasitophorous vacuole and into the host erythrocyte CC cytoplasm. At the schizont stage, localizes to the parasitophorous CC vacuole but not to the host erythrocyte cytoplasm. CC {ECO:0000250|UniProtKB:A0A509AIU5}. CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically CC inactive (By similarity). There is a second N-terminal lobe-like kinase CC domain at residues 830-1095 that contains functional ATP binding sites CC (PubMed:31148576). {ECO:0000255|PROSITE-ProRule:PRU00159, CC ECO:0000269|PubMed:31148576}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- CAUTION: Although it belongs to the kinase superfamily, contains an CC asparagine residue at the position of the canonical catalytic aspartic CC acid and does not have kinase activity (PubMed:31148576). However, can CC bind ATP (PubMed:31148576). {ECO:0000269|PubMed:31148576}. 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; LN999945; CZT98734.1; -; Genomic_DNA. DR RefSeq; XP_001347755.2; XM_001347719.2. DR AlphaFoldDB; Q8IIT5; -. DR STRING; 36329.Q8IIT5; -. DR GlyCosmos; Q8IIT5; 22 sites, No reported glycans. DR PaxDb; 5833-PF11_0079; -. DR EnsemblProtists; CZT98734; CZT98734; PF3D7_1106800. DR GeneID; 810631; -. DR KEGG; pfa:PF3D7_1106800; -. DR VEuPathDB; PlasmoDB:PF3D7_1106800; -. DR HOGENOM; CLU_248690_0_0_1; -. DR InParanoid; Q8IIT5; -. DR OMA; HIYCNNI; -. DR OrthoDB; 241850at2759; -. DR PhylomeDB; Q8IIT5; -. DR Reactome; R-PFA-430116; GP1b-IX-V activation signalling. DR Reactome; R-PFA-5673000; RAF activation. DR Reactome; R-PFA-5674499; Negative feedback regulation of MAPK pathway. DR Reactome; R-PFA-5675221; Negative regulation of MAPK pathway. DR Reactome; R-PFA-5689880; Ub-specific processing proteases. DR Proteomes; UP000001450; Chromosome 11. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0020003; C:symbiont-containing vacuole; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR050167; Ser_Thr_protein_kinase. DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2. DR Pfam; PF07647; SAM_2; 1. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. PE 1: Evidence at protein level; KW ATP-binding; Coiled coil; Glycoprotein; Host cell membrane; Host cytoplasm; KW Host cytoskeleton; Host membrane; Membrane; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..1501 FT /note="Inactive protein tyrosine kinase pTKL" FT /id="PRO_0000450198" FT DOMAIN 301..366 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT DOMAIN 1088..1483 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 204..223 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 257..276 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 392..425 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 543..607 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 659..678 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 399..433 FT /evidence="ECO:0000255" FT MOTIF 483..486 FT /note="RVxF motif 1" FT /evidence="ECO:0000305|PubMed:31148576" FT MOTIF 1238..1241 FT /note="RVxF motif 2" FT /evidence="ECO:0000305|PubMed:31148576" FT COMPBIAS 204..221 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 257..272 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 398..425 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 543..575 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 662..677 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 836..844 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 864 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT CARBOHYD 64 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 128 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 133 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 239 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 242 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 258 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 327 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 448 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 463 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 471 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 506 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 652 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 681 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 712 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 737 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 811 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 819 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1024 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1031 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1074 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1157 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1382 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" SQ SEQUENCE 1501 AA; 176120 MW; E517CBE251A2999F CRC64; MGNTLDSNKP KNFVTYADYK YIGKLNNKNE HHGIGIILYN SGESFYGSFI NGKKEGKGIY IDKNLTRYIN TWVDNKVFGK VKVVPYNSNR VYYFYYKNYM IEKCIYFDNN INNKESHHKN NIYNNYDNNS YNNNSCDDEE KRKYPIGVTK FKEDLSNYIH STHIMKKNNK LFNKNDNEYN IFSSSLSYSS DSENINLLDI LKKKKNKKNK KNKKKKNKKT KNTQILSCTQ HKMYEHNMNE SNFTKKDNVN CEHTDKMNIS LHEKNDKKNE KKNEKKNKKK KLFKYFSNNI ENLIIENYQT WSLREVIQWL MLCNVPVKWL ISFYKNNITG DKLKYININT IRNELGIIAY GHAIKILQLI KNLQVMAYNK KFNNLIQIEE YKNYIRQKEN TNKNIKKGKN IKKEKKKKKE KNIKKEKKKK KKETKKFNNM DKKYIDLAIH KNVKNIQNDT FYNKHENIYN CKNQTNFIYQ NDSEIKKIMN KKKVSFEYDN NEEKKKKNII KFIKNNKSLQ NSNGEYYLIN HLSKGICSDS IFYKSSQSKS SSQLSSPLSS PLSSPSPSSS PSSSPSSSPS SSPSSSPSPS SSPSPSSSPS SSPSSSPSSP PSPLSYKDNF PISSSCSSLE RLPSYEKKLL SSSQSNIEHI KNLPLDVLSN NNSSANIKIK KSKSKYNNDK KEQKKLPLIL NKSSSEFSPS HSYTSKSYHY NIKPSLQSSS NNSSDSSYSI SSTCSSSSSY VSSLYSNRSN DILNFYRNKI IKYCNNIYMN TKLAYSYMNG FIIPHEDLIF IHPIENYYMD NTNEKNNINN PYTKEKIMNH NFSFNTKNNT SFIDINTNIF SSNKQQNINN FGKYKKMKSR MFKGKYMGKE VAIKILVGKI KNFKKLHQIL YNLYNLRHSN LVLIMGVSIH YPFVFIIYEY MKNKCLFSYL HCIKYKHVYI STFLQRYKTL LHITQQEKIK KTNNINNNNN INHNNINNNN INHNNINHNN INNNNINNNN INYNKDYNNK KKKEDEQHNI EHQDTFIDLP EKSNISSDDN NSTDISQIQK ENFHFLNKKI EENKNIIYDD HTSTLSDHSI HNINKSYDNV YKNKMNIFHY QHNVLCGAYD NNDNNINDND IYCNNIYDNN INDNHIYCNN INDNHIYCNN INDNHIYCNN IYDHHKNTSL NSKEQNTDHN IEQINECNKY ASETKYNIKK SNLKNNIISH KNFQKCNQIQ MNQPYTFPPY QKELSSYLKN EKIKRKRKVL FSYLKTHIHF NSQQINDQHN RLSVQKIMKI ITDVTLACTY LEKEKMSPIN LKPTNILLDE SLNAKISDFG ISKIENCLDM NIDYSYKISS NSVIKINKKE YEQKKAKKIK IVNKNNNDLL YLYDHNNNVY KYNTQYIDVT YNNSYPSIFY WTPPEILRGK KNKKFYSDIY AFGIILWEML SNDIPYNYPF ASHIMAVVGY ANEELSFNNI PVSIQSLIKA CVNRNKYKRP TFEHILKTIS TLYQKANTKV EDALISFMDG T //