MKT1_TRYB2
ID MKT1_TRYB2 Reviewed; 735 AA.
AC Q587E3; D6XH60;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Post-transcriptional regulator MKT1 {ECO:0000305};
DE AltName: Full=Inactive endonuclease MKT1 {ECO:0000305};
GN Name=MKT1 {ECO:0000303|PubMed:24470144};
GN ORFNames=Tb927.6.4770 {ECO:0000312|EMBL:AAX79234.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000312|Proteomes:UP000008524};
RN [1] {ECO:0000312|EMBL:AAZ12035.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|EMBL:AAZ12035.1};
RX PubMed=16020724; DOI=10.1126/science.1112181;
RA El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT "Comparative genomics of trypanosomatid parasitic protozoa.";
RL Science 309:404-409(2005).
RN [2] {ECO:0000312|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PBP1 AND ZC3H11, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=427 {ECO:0000303|PubMed:24470144};
RX PubMed=24470144; DOI=10.1093/nar/gkt1416;
RA Singh A., Minia I., Droll D., Fadda A., Clayton C., Erben E.;
RT "Trypanosome MKT1 and the RNA-binding protein ZC3H11: interactions and
RT potential roles in post-transcriptional regulatory networks.";
RL Nucleic Acids Res. 42:4652-4668(2014).
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH PBP1; LSM12 AND XAC1,
RP INTERACTION WITH ZC3H11; CFB1; CFB2; PBP1 AND EIF4G5, DEVELOPMENTAL STAGE,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=427 {ECO:0000303|PubMed:32532821};
RX PubMed=32532821; DOI=10.1074/jbc.ra120.013306;
RA Melo do Nascimento L., Terrao M., Marucha K.K., Liu B., Egler F.,
RA Clayton C.;
RT "The RNA-associated proteins MKT1 and MKT1L form alternative PBP1-
RT containing complexes in Trypanosoma brucei.";
RL J. Biol. Chem. 295:10940-10955(2020).
CC -!- FUNCTION: Involved in post-transcriptional regulation of gene
CC expression (PubMed:24470144). Promotes mRNA stabilization by recruiting
CC a complex containing PBP1, LSM12 and XAC1 to mRNAs (PubMed:24470144,
CC PubMed:32532821). Recruited to mRNAs by sequence-specific RNA binding
CC proteins (PubMed:24470144). May regulate translation through
CC interactions with the EIF4E6-EIF4G5 translation initiation complex
CC (PubMed:32532821). {ECO:0000269|PubMed:24470144,
CC ECO:0000269|PubMed:32532821}.
CC -!- SUBUNIT: Forms a complex composed of at least MKT1, PBP1, XAC1 and
CC LSM12 (PubMed:32532821). Within the complex, interacts (via C-terminus)
CC with PBP1; the interaction is direct (PubMed:32532821,
CC PubMed:24470144). Interacts with RNA-binding protein ZC3H11 (via MKT1-
CC binding motif); the interaction is direct (PubMed:32532821,
CC PubMed:24470144). May interact with RNA-binding proteins CFB1 and CFB2
CC (PubMed:32532821). Interacts with the EIF4E6-EIF4G5 translation
CC initiation complex via EIF4G5; the interaction with EIF4G5 is direct
CC (PubMed:32532821). {ECO:0000269|PubMed:24470144,
CC ECO:0000269|PubMed:32532821}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24470144}.
CC Cytoplasm, Stress granule {ECO:0000269|PubMed:24470144}. Note=Localizes
CC to polysomes (PubMed:24470144). Partially localizes to starvation-
CC induced stress granules but not to heat shock-induced stress granules
CC (PubMed:24470144). {ECO:0000269|PubMed:24470144}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the procyclic and bloodstream forms
CC (at protein level). {ECO:0000269|PubMed:24470144,
CC ECO:0000269|PubMed:32532821}.
CC -!- DISRUPTION PHENOTYPE: RNAI-mediated knockdown in the bloodstream form
CC is lethal (PubMed:24470144). RNAi-mediated knockdown in the procyclic
CC form has no effect on viability (PubMed:24470144).
CC {ECO:0000269|PubMed:24470144}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the XPG/RAD2 endonuclease family, only
CC two of the seven Asp residues involved in Mg(2+) binding are conserved
CC suggesting that it has no nuclease activity. {ECO:0000305}.
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DR EMBL; AC007863; AAX79234.1; -; Genomic_DNA.
DR EMBL; CP000069; AAZ12035.1; -; Genomic_DNA.
DR RefSeq; XP_845594.1; XM_840501.1.
DR AlphaFoldDB; Q587E3; -.
DR STRING; 5691.AAZ12035; -.
DR PaxDb; Q587E3; -.
DR GeneID; 3658115; -.
DR KEGG; tbr:Tb927.6.4770; -.
DR VEuPathDB; TriTrypDB:Tb927.6.4770; -.
DR eggNOG; ENOG502QVHA; Eukaryota.
DR InParanoid; Q587E3; -.
DR OMA; FYQTKVI; -.
DR Proteomes; UP000008524; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:GeneDB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:GeneDB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR022039; MKT1_C.
DR InterPro; IPR022040; MKT1_N.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006084; XPG/Rad2.
DR PANTHER; PTHR11081; PTHR11081; 1.
DR Pfam; PF12246; MKT1_C; 1.
DR Pfam; PF12247; MKT1_N; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Translation regulation.
FT CHAIN 1..735
FT /note="Post-transcriptional regulator MKT1"
FT /id="PRO_0000451923"
FT REGION 475..722
FT /note="Interaction with PBP1"
FT /evidence="ECO:0000269|PubMed:24470144"
SQ SEQUENCE 735 AA; 83307 MW; C49FE3E218D4C0A3 CRC64;
MYPRHDDVSL FQRFVNDHKL EEKGLPLYQL AQLEGTDQVM LGVDGTKIID MITQAVRERE
KMAIYTYTTP YTVYEKINEF RTMFQSIKNC TPVFVFNGIQ YSPDSAEEFG REKNVVPSEV
AALTGTDSSR LSNTTNVRFA EIHKKTANRF VVEEDVEGQI IRIFRSEFKN TIRAPYLAWA
QLSSFRHCNH RHISEVYGCL ELLAFPGIDR VVTNINPTRG TFDVVYKARV LEAARLSEED
LSSLILVESR SRVMRTVTLK FSSLEDMIKK VVRYKGSTIG ASFAQQLHEE AIRASEANRM
RASNQRGAAF RNLSAFASPV LTLTPPHCLP LHFLYGIPGF PHADAESFVG LPLPPVLYYI
MSAGLLSPSL FAAVSQETVV DDWPLVDSIK YRDVAETVLP LRVQTIYQLA WTMSRGLGSI
SWFRRYNVLP ARVSKLHVPP AIQLDGWALH SVTVPRGLHL VDVMEFAHLA CSVDQVIYNT
MEETYAAILL QSLDLLGYLT HETQDLHEEG QSSEPSTFGR ALQLCSVPTL SEYTVLLIEL
ARTNAISTEP FRITTEEVSP RDTPRDIVFA SRVLSIIPLN VSGPWTAPID AELAAFSMLS
RMISRSIRQL LEAITTLMFS KGRTHVPLHR IGEIQRLLPF STPVEFGCGV LVEYMLMKDK
CTLKDLEEAF PECTYLRHDL ATLFYFWDLA VQVLQRIETK ENFCVDQHCL SSANERMKRA
QKNLNILTGV RETYY
