CTU1_MOUSE
ID CTU1_MOUSE Reviewed; 420 AA.
AC Q99J10;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 1 {ECO:0000255|HAMAP-Rule:MF_03053};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_03053};
DE AltName: Full=ATP-binding domain-containing protein 3 {ECO:0000255|HAMAP-Rule:MF_03053};
DE AltName: Full=Cytoplasmic tRNA adenylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN Name=Ctu1; Synonyms=Atpbd3, Ncs6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds
CC tRNAs and probably acts by catalyzing adenylation of tRNAs, an
CC intermediate required for 2-thiolation. It is unclear whether it acts
CC as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1
CC onto the uridine of tRNAs at wobble position. {ECO:0000255|HAMAP-
CC Rule:MF_03053}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03053}.
CC -!- SUBUNIT: Component of a complex at least composed of URM1, CTU2/NCS2
CC and CTU1/ATPBD3. May form a heterodimer with CTU2/NCS2.
CC {ECO:0000255|HAMAP-Rule:MF_03053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053}.
CC -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03053}.
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DR EMBL; AK155284; BAE33164.1; -; mRNA.
DR EMBL; BC005752; AAH05752.1; -; mRNA.
DR CCDS; CCDS21179.1; -.
DR RefSeq; NP_663557.1; NM_145582.1.
DR AlphaFoldDB; Q99J10; -.
DR SMR; Q99J10; -.
DR BioGRID; 231384; 3.
DR STRING; 10090.ENSMUSP00000036770; -.
DR iPTMnet; Q99J10; -.
DR PhosphoSitePlus; Q99J10; -.
DR EPD; Q99J10; -.
DR MaxQB; Q99J10; -.
DR PaxDb; Q99J10; -.
DR PeptideAtlas; Q99J10; -.
DR PRIDE; Q99J10; -.
DR ProteomicsDB; 279296; -.
DR Antibodypedia; 52772; 119 antibodies from 22 providers.
DR DNASU; 233189; -.
DR Ensembl; ENSMUST00000038332; ENSMUSP00000036770; ENSMUSG00000038888.
DR GeneID; 233189; -.
DR KEGG; mmu:233189; -.
DR UCSC; uc009gnh.1; mouse.
DR CTD; 90353; -.
DR MGI; MGI:2385277; Ctu1.
DR VEuPathDB; HostDB:ENSMUSG00000038888; -.
DR eggNOG; KOG2840; Eukaryota.
DR GeneTree; ENSGT00390000001041; -.
DR HOGENOM; CLU_026481_1_0_1; -.
DR InParanoid; Q99J10; -.
DR OMA; MNLDQKQ; -.
DR OrthoDB; 860739at2759; -.
DR PhylomeDB; Q99J10; -.
DR TreeFam; TF352405; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 233189; 11 hits in 73 CRISPR screens.
DR ChiTaRS; Ctu1; mouse.
DR PRO; PR:Q99J10; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q99J10; protein.
DR Bgee; ENSMUSG00000038888; Expressed in dorsal pancreas and 240 other tissues.
DR Genevisible; Q99J10; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_03053; CTU1; 1.
DR InterPro; IPR032442; CTU1_C.
DR InterPro; IPR000541; Ncs6/Tuc1/Ctu1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR PANTHER; PTHR11807:SF12; PTHR11807:SF12; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR Pfam; PF16503; zn-ribbon_14; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..420
FT /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT /id="PRO_0000282392"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7A3"
SQ SEQUENCE 420 AA; 43823 MW; 3DDCEDBE70D196B1 CRC64;
MPAPTCFSCH KTRAALRRPR SGQALCGSCF CAAFEAEVLH TVLAGHLLPP GAVVAVGASG
GKDSTVLAHV LRELAPRLGI TLHLVAVDEG IGGYRDAALE AVRSQAARWE LPLTIVAYED
LFGGWTMDAV ARSTAGSGRS RSCCTFCGVL RRRALEEGAR LVGATHIVTG HNADDMAETV
LMNFLRGDAG RLARGGVLGS TGEGCALPRC RPLQFASQKE VVLYAHFRHL RYFSEECVYA
PEAFRGHARD LLKLLEAARP SAVLDLVHSA ERLALAPAAK PPPPGTCSRC GALASHKLCQ
ACALLDGLNR GLPRLAIGKG RRVLQVEPPQ PGNPSLVTSD PVAPAGPCTC KQPKDKANPC
GNGGDRAGAT CVSQCDLSPG NGEDRAGATC VSQRDLSLGN GGDRAGATCV SQCDLSPVAE
