TRNT1_MOUSE
ID TRNT1_MOUSE Reviewed; 434 AA.
AC Q8K1J6; Q3TKW1; Q3UX99; Q920N6; Q9CSX0;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=CCA tRNA nucleotidyltransferase 1, mitochondrial;
DE EC=2.7.7.72 {ECO:0000250|UniProtKB:Q96Q11};
DE AltName: Full=mitochondrial tRNA nucleotidyl transferase, CCA-adding;
DE Short=mt CCA-adding enzyme;
DE Short=mt tRNA CCA-diphosphorylase;
DE Short=mt tRNA CCA-pyrophosphorylase;
DE Short=mt tRNA adenylyltransferase;
DE Flags: Precursor;
GN Name=Trnt1;
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 [MRNA] (ISOFORM 1).
RX PubMed=11504732; DOI=10.1074/jbc.m106202200;
RA Nagaike T., Suzuki T., Tomari Y., Takemoto-Hori C., Negayama F.,
RA Watanabe K., Ueda T.;
RT "Identification and characterization of mammalian mitochondrial tRNA
RT nucleotidyltransferases.";
RL J. Biol. Chem. 276:40041-40049(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Blastocyst, Bone marrow macrophage, Egg, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-402, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Adds and repairs the conserved 3'-CCA sequence necessary for
CC the attachment of amino acids to the 3' terminus of tRNA molecules,
CC using CTP and ATP as substrates. {ECO:0000250|UniProtKB:Q96Q11}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3
CC diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-
CC COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72;
CC Evidence={ECO:0000250|UniProtKB:Q96Q11};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K1J6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K1J6-2; Sequence=VSP_018616, VSP_018617;
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
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DR EMBL; AB063106; BAB70663.1; -; mRNA.
DR EMBL; AK011764; BAB27827.3; -; mRNA.
DR EMBL; AK135791; BAE22664.1; -; mRNA.
DR EMBL; AK152739; BAE31459.1; -; mRNA.
DR EMBL; AK166804; BAE39032.1; -; mRNA.
DR EMBL; BC031764; AAH31764.1; -; mRNA.
DR CCDS; CCDS20397.1; -. [Q8K1J6-1]
DR CCDS; CCDS57443.1; -. [Q8K1J6-2]
DR RefSeq; NP_001229287.1; NM_001242358.1. [Q8K1J6-1]
DR RefSeq; NP_001229289.1; NM_001242360.1. [Q8K1J6-2]
DR RefSeq; NP_081572.1; NM_027296.3. [Q8K1J6-1]
DR RefSeq; XP_006506644.1; XM_006506581.3. [Q8K1J6-1]
DR AlphaFoldDB; Q8K1J6; -.
DR SMR; Q8K1J6; -.
DR BioGRID; 213836; 1.
DR STRING; 10090.ENSMUSP00000060900; -.
DR iPTMnet; Q8K1J6; -.
DR PhosphoSitePlus; Q8K1J6; -.
DR EPD; Q8K1J6; -.
DR MaxQB; Q8K1J6; -.
DR PaxDb; Q8K1J6; -.
DR PeptideAtlas; Q8K1J6; -.
DR PRIDE; Q8K1J6; -.
DR ProteomicsDB; 298136; -. [Q8K1J6-1]
DR ProteomicsDB; 298137; -. [Q8K1J6-2]
DR Antibodypedia; 25074; 59 antibodies from 18 providers.
DR DNASU; 70047; -.
DR Ensembl; ENSMUST00000057578; ENSMUSP00000060900; ENSMUSG00000013736. [Q8K1J6-1]
DR Ensembl; ENSMUST00000113247; ENSMUSP00000108873; ENSMUSG00000013736. [Q8K1J6-2]
DR Ensembl; ENSMUST00000113248; ENSMUSP00000108874; ENSMUSG00000013736. [Q8K1J6-1]
DR Ensembl; ENSMUST00000113249; ENSMUSP00000108875; ENSMUSG00000013736. [Q8K1J6-1]
DR GeneID; 70047; -.
DR KEGG; mmu:70047; -.
DR UCSC; uc009dcy.2; mouse. [Q8K1J6-1]
DR UCSC; uc029vxx.1; mouse. [Q8K1J6-2]
DR CTD; 51095; -.
DR MGI; MGI:1917297; Trnt1.
DR VEuPathDB; HostDB:ENSMUSG00000013736; -.
DR eggNOG; KOG2159; Eukaryota.
DR GeneTree; ENSGT00390000009678; -.
DR HOGENOM; CLU_015961_2_1_1; -.
DR InParanoid; Q8K1J6; -.
DR OMA; YNYELRI; -.
DR OrthoDB; 730946at2759; -.
DR PhylomeDB; Q8K1J6; -.
DR TreeFam; TF313253; -.
DR BioGRID-ORCS; 70047; 25 hits in 76 CRISPR screens.
DR ChiTaRS; Trnt1; mouse.
DR PRO; PR:Q8K1J6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8K1J6; protein.
DR Bgee; ENSMUSG00000013736; Expressed in spermatocyte and 243 other tissues.
DR ExpressionAtlas; Q8K1J6; baseline and differential.
DR Genevisible; Q8K1J6; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009022; F:tRNA nucleotidyltransferase activity; ISO:MGI.
DR GO; GO:1990180; P:mitochondrial tRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; ISO:MGI.
DR GO; GO:0008033; P:tRNA processing; ISO:MGI.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Magnesium; Mitochondrion;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Reference proteome; RNA-binding; Transferase; Transit peptide;
KW tRNA processing.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..434
FT /note="CCA tRNA nucleotidyltransferase 1, mitochondrial"
FT /id="PRO_0000004783"
FT ACT_SITE 77
FT /evidence="ECO:0000250"
FT ACT_SITE 79
FT /evidence="ECO:0000250"
FT ACT_SITE 121
FT /evidence="ECO:0000250"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q11"
FT MOD_RES 402
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 204..215
FT /note="FYGRIVDRPGDH -> PGIVLGDLTTEK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018616"
FT VAR_SEQ 216..434
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018617"
FT CONFLICT 202
FT /note="F -> I (in Ref. 1; BAB70663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 49895 MW; 0578FB438165838B CRC64;
MQSVLYPWHR QVLRCSWSRL CLLKRYLFTM KLQSPEFQSL FTEGLKSLTE LFAKENHELR
IAGGAVRDLL NGVKPQDVDF ATTATPTQMK EMFQSAGIRM INNKGEKHGT ITARLHEENF
EVTTLRIDVT TDGRHAEVEF TTDWQKDAER RDLTINSMFL GFDGTLFDYF NGYADLKNKK
VRFVGHAKQR IQEDYLRILR YFRFYGRIVD RPGDHDHETL EAIAENAKGL AGISGERIWV
ELKKILTGDH VNHLIHLIYD LGVAPHIGLP ANANLEEFNK VSKNVEGFSP KPMTLLASLF
KVQDDVTKLD LRLKISKEEK NLGLFIVKNR KDLIKATDSS EPLKPYQDFV IDSREPDATA
RVCELLKYQG EHGLLKEMQQ WSVPPFPVSG HDIRKVGISS GKEIGALLQQ LREQWKKSGY
RMEKDELLSY IKKT
