ZC320_TRYB2
ID ZC320_TRYB2 Reviewed; 405 AA.
AC Q57XK8; D6XKI3;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=RNA-binding protein ZC3H20 {ECO:0000305};
DE AltName: Full=CCCH zinc finger protein ZC3H20 {ECO:0000305};
GN Name=ZC3H20 {ECO:0000303|PubMed:31743541};
GN ORFNames=Tb927.7.2660 {ECO:0000312|EMBL:AAX69661.1};
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:AAZ12330.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|EMBL:AAZ12330.1};
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, DEVELOPMENTAL STAGE, INDUCTION, DISRUPTION PHENOTYPE, MOTIF, AND
RP MUTAGENESIS OF 386-PRO-TYR-387.
RC STRAIN=427 {ECO:0000303|PubMed:31743541};
RX PubMed=31743541; DOI=10.1111/mmi.14429;
RA Liu B., Kamanyi Marucha K., Clayton C.;
RT "The zinc finger proteins ZC3H20 and ZC3H21 stabilise mRNAs encoding
RT membrane proteins and mitochondrial proteins in insect-form Trypanosoma
RT brucei.";
RL Mol. Microbiol. 113:430-451(2020).
RN [4] {ECO:0000305}
RP INTERACTION WITH MKT1, MOTIF, AND MUTAGENESIS OF 386-PRO-TYR-387.
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: RNA-binding protein involved in regulation of mRNA stability
CC (PubMed:31743541). Promotes mRNA stabilization by recruiting MKT1 and
CC PBP1 (By similarity). Stabilizes mRNA required for differentiation from
CC the bloodstream form to the procyclic form, and maintenance of the
CC procyclic form (PubMed:31743541). Stabilizes transcripts encoding
CC membrane and mitochondrial proteins, including AQP1 and GPEET2
CC procyclin (PubMed:31743541). {ECO:0000250|UniProtKB:Q57W26,
CC ECO:0000269|PubMed:31743541}.
CC -!- SUBUNIT: Interacts (via MKT1-binding motif) with MKT1.
CC {ECO:0000269|PubMed:32532821}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in the bloodstream form
CC (at protein level) (PubMed:31743541, PubMed:32532821). Expressed in the
CC procyclic form (PubMed:31743541). {ECO:0000269|PubMed:31743541,
CC ECO:0000269|PubMed:32532821}.
CC -!- INDUCTION: Induced during differentiation of bloodstream form to
CC procyclic form. {ECO:0000269|PubMed:31743541}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes abnormal
CC differentiation of the bloodstream form into the procyclic form, a
CC reduction in the expression of several mRNA including differentiation
CC protein PAD1, and premature death (PubMed:31743541). RNAi-mediated
CC knockdown at the procyclic stage causes a decrease in growth rate
CC (PubMed:31743541). Simultaneous RNAi-mediated knockdown of ZC3H20 and
CC ZC3H21 at the bloodstream stage is lethal (PubMed:31743541).
CC Simultaneous RNAi-mediated knockdown of ZC3H20 and ZC3H21 at the
CC procyclic stage causes a severe growth defect and a shift towards a
CC bloodstream form (PubMed:31743541). {ECO:0000269|PubMed:31743541}.
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DR EMBL; AC159413; AAX69661.1; -; Genomic_DNA.
DR EMBL; CP000070; AAZ12330.1; -; Genomic_DNA.
DR RefSeq; XP_845889.1; XM_840796.1.
DR AlphaFoldDB; Q57XK8; -.
DR PaxDb; Q57XK8; -.
DR GeneID; 3658475; -.
DR KEGG; tbr:Tb927.7.2660; -.
DR VEuPathDB; TriTrypDB:Tb927.7.2660; -.
DR eggNOG; ENOG502RZ2R; Eukaryota.
DR InParanoid; Q57XK8; -.
DR Proteomes; UP000008524; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005634; C:nucleus; IDA:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISM:GeneDB.
DR GO; GO:0048255; P:mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:GeneDB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP: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; IPR000571; Znf_CCCH.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Repeat; RNA-binding;
KW Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..405
FT /note="RNA-binding protein ZC3H20"
FT /id="PRO_0000451930"
FT ZN_FING 55..77
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 178..205
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 381..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 382..387
FT /note="MKT1-binding motif"
FT /evidence="ECO:0000305|PubMed:31743541,
FT ECO:0000305|PubMed:32532821"
FT MUTAGEN 386..387
FT /note="PY->AA: Abolishes MKT1 binding. Abolishes positive
FT regulation of protein expression."
FT /evidence="ECO:0000269|PubMed:31743541,
FT ECO:0000269|PubMed:32532821"
SQ SEQUENCE 405 AA; 43758 MW; 460347E6086946EF CRC64;
MQLVASPLET RRDIMCFEKG VECMVVVDPA TRKLRIPLSC VYPTRAHQRT TIPSLCLLFL
DGRCRQGTQC HQVHAALNVV AALRSQVDYL PICCALHGDR DYVNALDNRS WMSRVVVHVP
DATYGGGYIP LARFSYTTPI SRLLDALFHS TPQAEGQDGA QWESRAFGTP PSCLVLEAGD
ITLCRLHVQD RCRYAEECNY LHICKEVARC DRGLTLGQRP RSWKKPPSSS PSGGCFVVTA
SGTSMPPPPA AAAACDAPTP VSGGWTCPGS PTGSLFGANR SVTLGDASVT TQPAVVRCCD
PSSCTEAHSV VDCGQAHIPF SLSRQVSDIH MRQVSSTFFP SDNLSLDVDP STSGDCLAEQ
GCGMTPNIVV VTRNGKGGRE RWHYNPYGTN GTDRGIEKGE GRGRN
