CTH2_YEAST
ID CTH2_YEAST Reviewed; 285 AA.
AC P47977; D6VYD1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=mRNA decay factor CTH2;
DE AltName: Full=Cysteine-three-histidine protein 2;
DE AltName: Full=Protein TIS11 homolog;
DE AltName: Full=Protein YTIS11;
DE AltName: Full=TPA-induced sequence protein 11;
GN Name=TIS11; Synonyms=CTH2; OrderedLocusNames=YLR136C;
GN ORFNames=L3143, L9606.12;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7845673;
RA Ma Q., Herschman H.R.;
RT "The yeast homologue YTIS11, of the mammalian TIS11 gene family is a non-
RT essential, glucose repressible gene.";
RL Oncogene 10:487-494(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8890739; DOI=10.1016/0378-1119(96)00084-4;
RA Thompson M.J., Lai W.S., Taylor G.A., Blackshear P.J.;
RT "Cloning and characterization of two yeast genes encoding members of the
RT CCCH class of zinc finger proteins: zinc finger-mediated impairment of cell
RT growth.";
RL Gene 174:225-233(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP FUNCTION, INDUCTION, MUTAGENESIS OF CYS-190 AND CYS-213, AND MRNA-BINDING.
RX PubMed=15652485; DOI=10.1016/j.cell.2004.11.032;
RA Puig S., Askeland E., Thiele D.J.;
RT "Coordinated remodeling of cellular metabolism during iron deficiency
RT through targeted mRNA degradation.";
RL Cell 120:99-110(2005).
RN [8]
RP FUNCTION.
RX PubMed=18522836; DOI=10.1016/j.cmet.2008.04.010;
RA Puig S., Vergara S.V., Thiele D.J.;
RT "Cooperation of two mRNA-binding proteins drives metabolic adaptation to
RT iron deficiency.";
RL Cell Metab. 7:555-564(2008).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18923425; DOI=10.1038/emboj.2008.212;
RA Prouteau M., Daugeron M.-C., Seraphin B.;
RT "Regulation of ARE transcript 3' end processing by the yeast Cth2 mRNA
RT decay factor.";
RL EMBO J. 27:2966-2976(2008).
RN [10]
RP FUNCTION, INTERACTION WITH DHH1, AND SUBCELLULAR LOCATION.
RX PubMed=18715869; DOI=10.1074/jbc.m804910200;
RA Pedro-Segura E., Vergara S.V., Rodriguez-Navarro S., Parker R.,
RA Thiele D.J., Puig S.;
RT "The Cth2 ARE-binding protein recruits the Dhh1 helicase to promote the
RT decay of succinate dehydrogenase SDH4 mRNA in response to iron
RT deficiency.";
RL J. Biol. Chem. 283:28527-28535(2008).
CC -!- FUNCTION: Binds to specific AU-rich elements (ARE) in the 3'-
CC untranslated region of target mRNAs and promotes their degradation. In
CC response to iron deficiency, promotes the decay of many mRNAs encoding
CC proteins involved in iron-dependent pathways. Recruits the DHH1
CC helicase to the SDH4 mRNA and promotes SDH4 mRNA decay. Also
CC destabilizes target mRNA by modulating 3'-end processing, creating
CC extended transcripts that are prone for degradation.
CC {ECO:0000269|PubMed:15652485, ECO:0000269|PubMed:18522836,
CC ECO:0000269|PubMed:18715869, ECO:0000269|PubMed:18923425}.
CC -!- SUBUNIT: Interacts with DHH1. {ECO:0000269|PubMed:18715869}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18923425}. Cytoplasm,
CC P-body {ECO:0000269|PubMed:18715869}.
CC -!- INDUCTION: By transcription factors AFT1 and AFT2 in response to iron
CC deficiency. {ECO:0000269|PubMed:15652485}.
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DR EMBL; S76619; AAB33266.1; -; Genomic_DNA.
DR EMBL; L42134; AAB39898.1; -; Genomic_DNA.
DR EMBL; X91258; CAA62651.1; -; Genomic_DNA.
DR EMBL; Z73308; CAA97707.1; -; Genomic_DNA.
DR EMBL; U53881; AAB82400.1; -; Genomic_DNA.
DR EMBL; AY558210; AAS56536.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09447.1; -; Genomic_DNA.
DR PIR; S59328; S59328.
DR RefSeq; NP_013237.1; NM_001182023.1.
DR AlphaFoldDB; P47977; -.
DR SMR; P47977; -.
DR BioGRID; 31405; 62.
DR DIP; DIP-5614N; -.
DR IntAct; P47977; 2.
DR STRING; 4932.YLR136C; -.
DR PaxDb; P47977; -.
DR PRIDE; P47977; -.
DR EnsemblFungi; YLR136C_mRNA; YLR136C; YLR136C.
DR GeneID; 850827; -.
DR KEGG; sce:YLR136C; -.
DR SGD; S000004126; TIS11.
DR VEuPathDB; FungiDB:YLR136C; -.
DR eggNOG; KOG1677; Eukaryota.
DR GeneTree; ENSGT00940000170800; -.
DR HOGENOM; CLU_060370_0_0_1; -.
DR InParanoid; P47977; -.
DR OMA; TELCESX; -.
DR BioCyc; YEAST:G3O-32276-MON; -.
DR Reactome; R-SCE-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR PRO; PR:P47977; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P47977; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:SGD.
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; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat; RNA-binding;
KW Zinc; Zinc-finger.
FT CHAIN 1..285
FT /note="mRNA decay factor CTH2"
FT /id="PRO_0000089174"
FT ZN_FING 169..197
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 207..235
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 37..55
FT /note="Required for mRNA decay activity"
FT REGION 132..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 190
FT /note="C->A,R: Abolishes mRNA binding."
FT /evidence="ECO:0000269|PubMed:15652485"
FT MUTAGEN 213
FT /note="C->A,R: Abolishes mRNA binding."
FT /evidence="ECO:0000269|PubMed:15652485"
SQ SEQUENCE 285 AA; 32314 MW; 72E041AE31EC4099 CRC64;
MWAQLSYTRP ESQKTDLTSL FSTDQEQNPL NDYQYQINIR ELEEYYNKTI LNEDNIQETS
SEISSAVSFS PPKNTNAIQP GLLYDPQLMN PFLPSAHLNS TAPTTFKKKL EVQINPDYVP
KSSQLPLTSQ NLQQLSQQKP KNDASFSSEK ESSAQPKVKS QVQETPKQLY KTELCESFTL
KGSCPYGSKC QFAHGLGELK VKKSCKNFRT KPCVNWEKLG YCPYGRRCCF KHGDDNDIAV
YVKAGTYCNV SSTSKQSDEK RSNGRGSAKK KNLNVKVKAL QRMTW
