ZC311_TRYB2
ID ZC311_TRYB2 Reviewed; 364 AA.
AC Q57W26; D6XG19;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=RNA-binding protein ZC3H11 {ECO:0000305};
DE AltName: Full=CCCH zinc finger protein ZC3H11 {ECO:0000303|PubMed:23592996};
GN Name=ZC3H11 {ECO:0000303|PubMed:23592996};
GN ORFNames=Tb927.5.810 {ECO:0000312|EMBL:AAX70193.1};
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:AAZ11196.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|EMBL:AAZ11196.1};
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 MKT1 AND PBP1, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, INDUCTION, DOMAIN, PHOSPHORYLATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=427 {ECO:0000303|PubMed:23592996};
RX PubMed=23592996; DOI=10.1371/journal.ppat.1003286;
RA Droll D., Minia I., Fadda A., Singh A., Stewart M., Queiroz R., Clayton C.;
RT "Post-transcriptional regulation of the trypanosome heat shock response by
RT a zinc finger protein.";
RL PLoS Pathog. 9:e1003286-e1003286(2013).
RN [4] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MKT1 AND
RP PBP1, MOTIF, AND MUTAGENESIS OF 198-PRO-TYR-199.
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 [5] {ECO:0000305}
RP FUNCTION, INDUCTION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27002830; DOI=10.1371/journal.ppat.1005514;
RA Minia I., Clayton C.;
RT "Regulating a Post-Transcriptional Regulator: Protein Phosphorylation,
RT Degradation and Translational Blockage in Control of the Trypanosome
RT Stress-Response RNA-Binding Protein ZC3H11.";
RL PLoS Pathog. 12:e1005514-e1005514(2016).
CC -!- FUNCTION: RNA-binding protein involved in regulation of mRNA stability
CC (PubMed:23592996). Binds AU-rich regions in the 3'-UTR of mRNAs and
CC promotes their stabilization by recruiting a MKT1-containing complex
CC (PubMed:23592996, PubMed:24470144). Stabilizes chaperone mRNAs during
CC stress that causes an accumulation of misfolded or unfolded proteins in
CC the cytoplasm (PubMed:23592996, PubMed:24470144, PubMed:27002830).
CC {ECO:0000269|PubMed:23592996, ECO:0000269|PubMed:24470144,
CC ECO:0000269|PubMed:27002830}.
CC -!- SUBUNIT: Interacts (via MKT1-binding motif) with MKT1 (PubMed:23592996,
CC PubMed:24470144). Interacts with PBP1 (via C-terminus); the interaction
CC is direct (PubMed:23592996, PubMed:24470144).
CC {ECO:0000269|PubMed:23592996, ECO:0000269|PubMed:24470144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23592996}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the procyclic form and the
CC bloodstream form at low levels. {ECO:0000269|PubMed:23592996}.
CC -!- INDUCTION: Induced during the response to misfolded or unfolded
CC cytoplasmic proteins; including during thermal stress, sodium arsenite,
CC or acidic pH (at protein level) (PubMed:23592996, PubMed:27002830). Not
CC induced by endoplasmic reticulum stress (PubMed:27002830).
CC {ECO:0000269|PubMed:23592996, ECO:0000269|PubMed:27002830}.
CC -!- DOMAIN: The zinc finger domain binds AU-rich regions in the 3'-UTR of
CC mRNAs. {ECO:0000269|PubMed:23592996}.
CC -!- PTM: Phosphorylated at the N-terminus (PubMed:23592996,
CC PubMed:27002830). CK1.2-dependent phosphorylation may lead to
CC proteasome-dependent degradation of ZC3H11 in absence of stress
CC (PubMed:27002830). {ECO:0000269|PubMed:23592996,
CC ECO:0000269|PubMed:27002830}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the bloodstream form
CC is lethal and causes a reduction in chaperone mRNA levels in response
CC to heat-induced stress (PubMed:23592996). RNAi-mediated knockdown in
CC the procyclic form causes sensitivity to cytoplasmic protein folding
CC stress (induced by high temperature, puromycin, arsenite, MG132 or
CC ethanol), characterized by a reduction in chaperone mRNA levels
CC (PubMed:23592996, PubMed:27002830). {ECO:0000269|PubMed:23592996,
CC ECO:0000269|PubMed:27002830}.
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DR EMBL; AC159432; AAX70193.1; -; Genomic_DNA.
DR EMBL; CP000068; AAZ11196.1; -; Genomic_DNA.
DR RefSeq; XP_844755.1; XM_839662.1.
DR AlphaFoldDB; Q57W26; -.
DR PaxDb; Q57W26; -.
DR GeneID; 3657190; -.
DR KEGG; tbr:Tb927.5.810; -.
DR VEuPathDB; TriTrypDB:Tb927.5.810; -.
DR eggNOG; ENOG502S8CS; Eukaryota.
DR InParanoid; Q57W26; -.
DR Proteomes; UP000008524; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:GeneDB.
DR GO; GO:0140517; F:protein-RNA adaptor activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISM:GeneDB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IEP:GeneDB.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
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 GO; GO:0009408; P:response to heat; IMP:GeneDB.
DR InterPro; IPR045877; ZFP36-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12547; PTHR12547; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome; RNA-binding;
KW Stress response; Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..364
FT /note="RNA-binding protein ZC3H11"
FT /id="PRO_0000451929"
FT ZN_FING 64..92
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 340..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 194..199
FT /note="MKT1-binding motif"
FT /evidence="ECO:0000269|PubMed:24470144"
FT MUTAGEN 198..199
FT /note="PY->AA: Abolishes MKT1 protein binding."
FT /evidence="ECO:0000269|PubMed:24470144"
SQ SEQUENCE 364 AA; 39555 MW; EBCD719EB8603338 CRC64;
MSTATSAPVV ESMSDTVVCP QLSRHSTSLE ELYTIGYNRS HSPSCFSSAG CEEEEGQKNV
LAERYKTKLC KNFVQYGTCP YDIRCMFAHG EEELRTAEMN IMDGLVTKDA ITSFQKLWHR
AVSASSGSKH HSSHVANRRG VMTTATTTTT AGGSTDAAMH ICRRMQRVVA AAAAAVPCGG
RRVVSGSIRI RGCVRHNPYC HNILPTVSRY YSTMPDVFTR PYSKSDSCGN EAITEGNAWT
YANEEGNEKE TPAMISSGVP ELTAWKRFNY VAERSQCTSV PEQNLPCADF AAIKESNNTG
GNASGVDVEN VDDAEHSTCS SVGNESGYFC RASRSASCGE QSQSHLKREG NEGRGEGLHM
FLSL
