ID   CTU2_MOUSE              Reviewed;         514 AA.
AC   Q3U308; Q8BTG9; Q8CI68;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=Ctu2; Synonyms=Ncs2;
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=C57BL/6J, and NOD; TISSUE=Diencephalon;
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=FVB/N; 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).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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). May act by
CC       forming a heterodimer with CTU1/ATPBD3 that ligates sulfur from
CC       thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
CC       {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SUBUNIT: Component of a complex at least composed of URM1, CTU2/NCS2
CC       and CTU1/ATPBD3. {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03054}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH36332.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC41181.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK090349; BAC41181.1; ALT_FRAME; mRNA.
DR   EMBL; AK154995; BAE32982.1; -; mRNA.
DR   EMBL; BC036332; AAH36332.1; ALT_INIT; mRNA.
DR   CCDS; CCDS52694.1; -.
DR   RefSeq; NP_722470.2; NM_153775.2.
DR   AlphaFoldDB; Q3U308; -.
DR   BioGRID; 426341; 1.
DR   STRING; 10090.ENSMUSP00000112113; -.
DR   GlyGen; Q3U308; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3U308; -.
DR   PhosphoSitePlus; Q3U308; -.
DR   SwissPalm; Q3U308; -.
DR   EPD; Q3U308; -.
DR   MaxQB; Q3U308; -.
DR   PaxDb; 10090-ENSMUSP00000112113; -.
DR   PeptideAtlas; Q3U308; -.
DR   ProteomicsDB; 285353; -.
DR   Pumba; Q3U308; -.
DR   Antibodypedia; 49625; 57 antibodies from 13 providers.
DR   Ensembl; ENSMUST00000116412.8; ENSMUSP00000112113.2; ENSMUSG00000049482.17.
DR   GeneID; 66965; -.
DR   KEGG; mmu:66965; -.
DR   UCSC; uc009nsz.2; mouse.
DR   AGR; MGI:1914215; -.
DR   CTD; 348180; -.
DR   MGI; MGI:1914215; Ctu2.
DR   VEuPathDB; HostDB:ENSMUSG00000049482; -.
DR   eggNOG; KOG2594; Eukaryota.
DR   GeneTree; ENSGT00390000008797; -.
DR   InParanoid; Q3U308; -.
DR   OMA; AFYNRMF; -.
DR   OrthoDB; 8183at2759; -.
DR   PhylomeDB; Q3U308; -.
DR   TreeFam; TF313203; -.
DR   UniPathway; UPA00988; -.
DR   BioGRID-ORCS; 66965; 23 hits in 82 CRISPR screens.
DR   ChiTaRS; Ctu2; mouse.
DR   PRO; PR:Q3U308; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q3U308; Protein.
DR   Bgee; ENSMUSG00000049482; Expressed in ear vesicle and 222 other cell types or tissues.
DR   ExpressionAtlas; Q3U308; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
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; HUPs; 1.
DR   HAMAP; MF_03054; CTU2; 1.
DR   InterPro; IPR019407; CTU2.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR20882; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 2; 1.
DR   PANTHER; PTHR20882:SF14; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 2; 1.
DR   Pfam; PF10288; CTU2; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   Genevisible; Q3U308; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Reference proteome;
KW   tRNA processing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q2VPK5"
FT   CHAIN           2..514
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000289176"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylcysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2VPK5"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2VPK5"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2VPK5"
SQ   SEQUENCE   514 AA;  56105 MW;  88A531D4F3BD3532 CRC64;
     MCQAGEDYAG PARREPPPVP RPSREQKCVK CAEGLPVVVI RAGDAFCRVC FKAFYVHKFR
     AMLGKNRVIF PGEKVLLSWS GGPSSSSMVW QVLEGLSQDS AKRLRFVPGV IYVDEGAACG
     QSLEDRQKTV AEVKRILENT GFPWHVVALE EVFSLPPSVL CCTSQESAGT EEAYKAAVDR
     FLQQQQQQQQ RVLGAEAGAS PAQGEARLHP SHGREPSGTA GYPTAAQTEA LSRLFSSIKT
     LTAKEELLQT LRTHLIVHIA RVHGYCKVMT GETCTRLAIK LMTNLALGRG AFLAWDTGFS
     DERHGDVVLV RPMRDHTLKE VAFYNHLFRV PSVFTPAIDT KAPEKASIHR LMEAFILRLQ
     TLFPSTVSTV YRTSEKLVKA PREGCAAGPS GPSCLLCMCA LDIDTADSAT AFGAQSSSHL
     SQMPSAEAGM PTQPCCAAGE GQAQSCHREV GKRGDARACI TEQLCYSCRV NMKDLPSLDP
     LPPYVLAEAQ LRSQRGSVSE EIQEYLITDE EEDS
//