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mRNA decay factor CTH2 (Cysteine-three-histidine protein 2) (Protein TIS11 homolog) (Protein YTIS11) (TPA-induced sequence protein 11)

 CTH2_YEAST              Reviewed;         285 AA.
P47977; D6VYD1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=mRNA decay factor CTH2;
AltName: Full=Cysteine-three-histidine protein 2;
AltName: Full=Protein TIS11 homolog;
AltName: Full=Protein YTIS11;
AltName: Full=TPA-induced sequence protein 11;
Name=TIS11; Synonyms=CTH2; OrderedLocusNames=YLR136C;
ORFNames=L3143, L9606.12;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7845673;
Ma Q., Herschman H.R.;
"The yeast homologue YTIS11, of the mammalian TIS11 gene family is a
non-essential, glucose repressible gene.";
Oncogene 10:487-494(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8890739; DOI=10.1016/0378-1119(96)00084-4;
Thompson M.J., Lai W.S., Taylor G.A., Blackshear P.J.;
"Cloning and characterization of two yeast genes encoding members of
the CCCH class of zinc finger proteins: zinc finger-mediated
impairment of cell growth.";
Gene 174:225-233(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
FUNCTION, INDUCTION, MUTAGENESIS OF CYS-190 AND CYS-213, AND
MRNA-BINDING.
PubMed=15652485; DOI=10.1016/j.cell.2004.11.032;
Puig S., Askeland E., Thiele D.J.;
"Coordinated remodeling of cellular metabolism during iron deficiency
through targeted mRNA degradation.";
Cell 120:99-110(2005).
[8]
FUNCTION.
PubMed=18522836; DOI=10.1016/j.cmet.2008.04.010;
Puig S., Vergara S.V., Thiele D.J.;
"Cooperation of two mRNA-binding proteins drives metabolic adaptation
to iron deficiency.";
Cell Metab. 7:555-564(2008).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18923425; DOI=10.1038/emboj.2008.212;
Prouteau M., Daugeron M.-C., Seraphin B.;
"Regulation of ARE transcript 3' end processing by the yeast Cth2 mRNA
decay factor.";
EMBO J. 27:2966-2976(2008).
[10]
FUNCTION, INTERACTION WITH DHH1, AND SUBCELLULAR LOCATION.
PubMed=18715869; DOI=10.1074/jbc.M804910200;
Pedro-Segura E., Vergara S.V., Rodriguez-Navarro S., Parker R.,
Thiele D.J., Puig S.;
"The Cth2 ARE-binding protein recruits the Dhh1 helicase to promote
the decay of succinate dehydrogenase SDH4 mRNA in response to iron
deficiency.";
J. Biol. Chem. 283:28527-28535(2008).
-!- FUNCTION: Binds to specific AU-rich elements (ARE) in the 3'-
untranslated region of target mRNAs and promotes their
degradation. In response to iron deficiency, promotes the decay of
many mRNAs encoding proteins involved in iron-dependent pathways.
Recruits the DHH1 helicase to the SDH4 mRNA and promotes SDH4 mRNA
decay. Also destabilizes target mRNA by modulating 3'-end
processing, creating extended transcripts that are prone for
degradation. {ECO:0000269|PubMed:15652485,
ECO:0000269|PubMed:18522836, ECO:0000269|PubMed:18715869,
ECO:0000269|PubMed:18923425}.
-!- SUBUNIT: Interacts with DHH1. {ECO:0000269|PubMed:18715869}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18923425}.
Cytoplasm, P-body {ECO:0000269|PubMed:18715869}.
-!- INDUCTION: By transcription factors AFT1 and AFT2 in response to
iron deficiency. {ECO:0000269|PubMed:15652485}.
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EMBL; S76619; AAB33266.1; -; Genomic_DNA.
EMBL; L42134; AAB39898.1; -; Genomic_DNA.
EMBL; X91258; CAA62651.1; -; Genomic_DNA.
EMBL; Z73308; CAA97707.1; -; Genomic_DNA.
EMBL; U53881; AAB82400.1; -; Genomic_DNA.
EMBL; AY558210; AAS56536.1; -; Genomic_DNA.
EMBL; BK006945; DAA09447.1; -; Genomic_DNA.
PIR; S59328; S59328.
RefSeq; NP_013237.1; NM_001182023.1.
ProteinModelPortal; P47977; -.
SMR; P47977; -.
BioGrid; 31405; 58.
DIP; DIP-5614N; -.
IntAct; P47977; 2.
MINT; MINT-504800; -.
STRING; 4932.YLR136C; -.
PRIDE; P47977; -.
EnsemblFungi; YLR136C; YLR136C; YLR136C.
GeneID; 850827; -.
KEGG; sce:YLR136C; -.
EuPathDB; FungiDB:YLR136C; -.
SGD; S000004126; TIS11.
GeneTree; ENSGT00530000063262; -.
HOGENOM; HOG000001038; -.
InParanoid; P47977; -.
OrthoDB; EOG092C4AZJ; -.
BioCyc; YEAST:G3O-32276-MONOMER; -.
Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
PRO; PR:P47977; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
GO; GO:0003729; F:mRNA binding; IDA:SGD.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IBA:GO_Central.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:SGD.
Gene3D; 4.10.1000.10; -; 2.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
Pfam; PF00642; zf-CCCH; 2.
SMART; SM00356; ZnF_C3H1; 2.
SUPFAM; SSF90229; SSF90229; 2.
PROSITE; PS50103; ZF_C3H1; 2.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Metal-binding; Nucleus;
Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
CHAIN 1 285 mRNA decay factor CTH2.
/FTId=PRO_0000089174.
ZN_FING 169 197 C3H1-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 207 235 C3H1-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
REGION 37 55 Required for mRNA decay activity.
MUTAGEN 190 190 C->A,R: Abolishes mRNA binding.
{ECO:0000269|PubMed:15652485}.
MUTAGEN 213 213 C->A,R: Abolishes mRNA binding.
{ECO:0000269|PubMed:15652485}.
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


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