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CTH1_YEAST
ID   CTH1_YEAST              Reviewed;         325 AA.
AC   P47976; D6VSD3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=mRNA decay factor CTH1;
DE   AltName: Full=Cysteine-three-histidine protein 1;
GN   Name=CTH1; OrderedLocusNames=YDR151C; ORFNames=YD8358.07C;
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=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
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   [4]
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   [5]
RP   FUNCTION, INDUCTION, MUTAGENESIS OF CYS-225, AND MRNA-BINDING.
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).
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. Negatively regulates
CC       primarily iron-dependent mitochondrial processes including respiration
CC       and amino acid biosynthesis. {ECO:0000269|PubMed:18522836}.
CC   -!- INDUCTION: By transcription factors AFT1 and AFT2 in response to iron
CC       deficiency. {ECO:0000269|PubMed:18522836}.
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DR   EMBL; L42133; AAB39897.1; -; Genomic_DNA.
DR   EMBL; Z50046; CAA90373.1; -; Genomic_DNA.
DR   EMBL; AY557690; AAS56016.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11993.1; -; Genomic_DNA.
DR   PIR; S57977; S57977.
DR   RefSeq; NP_010435.1; NM_001180458.1.
DR   AlphaFoldDB; P47976; -.
DR   SMR; P47976; -.
DR   BioGRID; 32204; 60.
DR   DIP; DIP-1784N; -.
DR   IntAct; P47976; 5.
DR   MINT; P47976; -.
DR   STRING; 4932.YDR151C; -.
DR   iPTMnet; P47976; -.
DR   PaxDb; P47976; -.
DR   PRIDE; P47976; -.
DR   EnsemblFungi; YDR151C_mRNA; YDR151C; YDR151C.
DR   GeneID; 851729; -.
DR   KEGG; sce:YDR151C; -.
DR   SGD; S000002558; CTH1.
DR   VEuPathDB; FungiDB:YDR151C; -.
DR   eggNOG; KOG1677; Eukaryota.
DR   GeneTree; ENSGT00940000170800; -.
DR   HOGENOM; CLU_060370_0_0_1; -.
DR   InParanoid; P47976; -.
DR   OMA; KPCINWS; -.
DR   BioCyc; YEAST:G3O-29745-MON; -.
DR   Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR   Reactome; R-SCE-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR   ChiTaRS; CTL1; yeast.
DR   PRO; PR:P47976; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P47976; protein.
DR   GO; GO:0005634; C:nucleus; IC:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; ISS:SGD.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IGI:SGD.
DR   GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IGI: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   Metal-binding; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..325
FT                   /note="mRNA decay factor CTH1"
FT                   /id="PRO_0000089173"
FT   ZN_FING         204..232
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         242..270
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          284..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         225
FT                   /note="C->R: Abolishes mRNA binding."
FT                   /evidence="ECO:0000269|PubMed:18522836"
FT   CONFLICT        142..143
FT                   /note="EI -> RV (in Ref. 1; AAB39897)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   325 AA;  36772 MW;  8B5966F88CE096DE CRC64;
     MMPNVAPNSY YLNIPNANST STTTSSIFSD LNKEYESKIK EIEEYYIKTL LNENTDNDDS
     SSSEGHNINE TDILSEYSPR PSPWLPSKPN CYHPLGDFKD LIISDSRPTN TLPINNPFAG
     NNNISTLATT EKKRKKRSLE VEINPTYTTS AFSLPLTAEN LQKLSQVDSQ STGLPYTLPI
     QKTTKLEPCR RAPLQLPQLV NKTLYKTELC ESFTIKGYCK YGNKCQFAHG LNELKFKKKS
     NNYRTKPCIN WSKLGYCPYG KRCCFKHGDD KDVEIYQNAN DGRSKDTALT PLPTSLAPSN
     NDNITNLSKP RNLHTSVKAL QRMTW
 
 
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