TRNT1_HUMAN
ID TRNT1_HUMAN Reviewed; 434 AA.
AC Q96Q11; A8K2Z6; B7WP13; C9JKA2; Q8ND57; Q9BS97; Q9Y362;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=CCA tRNA nucleotidyltransferase 1, mitochondrial;
DE EC=2.7.7.72 {ECO:0000269|PubMed:11504732};
DE AltName: Full=Mitochondrial tRNA nucleotidyl transferase, CCA-adding;
DE AltName: Full=mt CCA-adding enzyme;
DE AltName: Full=mt tRNA CCA-diphosphorylase;
DE AltName: Full=mt tRNA CCA-pyrophosphorylase;
DE AltName: Full=mt tRNA adenylyltransferase;
DE Flags: Precursor;
GN Name=TRNT1; ORFNames=CGI-47;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP VARIANT LEU-23.
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] (ISOFORM 1), AND VARIANT LEU-23.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-23.
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LEU-23.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-23.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP LEU-23.
RC TISSUE=Bone marrow;
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11256614; DOI=10.1093/embo-reports/kvd058;
RA Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.;
RT "Systematic subcellular localization of novel proteins identified by large-
RT scale cDNA sequencing.";
RL EMBO Rep. 1:287-292(2000).
RN [9]
RP FUNCTION (ISOFORM 2).
RX PubMed=17204286; DOI=10.1016/j.jmb.2006.12.016;
RA Lizano E., Schuster J., Muller M., Kelso J., Morl M.;
RT "A splice variant of the human CCA-adding enzyme with modified activity.";
RL J. Mol. Biol. 366:1258-1265(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-402, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP INVOLVEMENT IN SIFD, VARIANTS SIFD ILE-154; VAL-158; SER-166; ILE-190;
RP THR-223; THR-326 AND GLU-416, AND CHARACTERIZATION OF VARIANTS SIFD
RP ILE-154; VAL-158; SER-166; ILE-190; THR-223 AND THR-326.
RX PubMed=25193871; DOI=10.1182/blood-2014-08-591370;
RA Chakraborty P.K., Schmitz-Abe K., Kennedy E.K., Mamady H., Naas T.,
RA Durie D., Campagna D.R., Lau A., Sendamarai A.K., Wiseman D.H., May A.,
RA Jolles S., Connor P., Powell C., Heeney M.M., Giardina P.J., Klaassen R.J.,
RA Kannengiesser C., Thuret I., Thompson A.A., Marques L., Hughes S.,
RA Bonney D.K., Bottomley S.S., Wynn R.F., Laxer R.M., Minniti C.P.,
RA Moppett J., Bordon V., Geraghty M., Joyce P.B., Markianos K., Rudner A.D.,
RA Holcik M., Fleming M.D.;
RT "Mutations in TRNT1 cause congenital sideroblastic anemia with
RT immunodeficiency, fevers, and developmental delay (SIFD).";
RL Blood 124:2867-2871(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP INVOLVEMENT IN RPEM, AND VARIANT RPEM GLU-43 DEL.
RX PubMed=26494905; DOI=10.1093/hmg/ddv446;
RA DeLuca A.P., Whitmore S.S., Barnes J., Sharma T.P., Westfall T.A.,
RA Scott C.A., Weed M.C., Wiley J.S., Wiley L.A., Johnston R.M.,
RA Schnieders M.J., Lentz S.R., Tucker B.A., Mullins R.F., Scheetz T.E.,
RA Stone E.M., Slusarski D.C.;
RT "Hypomorphic mutations in TRNT1 cause retinitis pigmentosa with
RT erythrocytic microcytosis.";
RL Hum. Mol. Genet. 25:44-56(2016).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 30-434, AND DIMERIZATION.
RX PubMed=12729736; DOI=10.1016/s0022-2836(03)00381-4;
RA Augustin M.A., Reichert A.S., Betat H., Huber R., Moerl M., Steegborn C.;
RT "Crystal structure of the human CCA-adding enzyme: insights into template-
RT independent polymerization.";
RL J. Mol. Biol. 328:985-994(2003).
CC -!- FUNCTION: [Isoform 1]: Adds and repairs the conserved 3'-CCA sequence
CC necessary for the attachment of amino acids to the 3' terminus of tRNA
CC molecules, using CTP and ATP as substrates.
CC {ECO:0000269|PubMed:11504732}.
CC -!- FUNCTION: [Isoform 2]: Adds 2 C residues (CC-) to the 3' terminus of
CC tRNA molecules instead of a complete CCA end as isoform 1 does (in
CC vitro). {ECO:0000269|PubMed:17204286}.
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:0000269|PubMed:11504732};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Monomer, and homodimer; disulfide-linked.
CC -!- INTERACTION:
CC Q96Q11-3; P28799: GRN; NbExp=3; IntAct=EBI-25861172, EBI-747754;
CC Q96Q11-3; O76024: WFS1; NbExp=3; IntAct=EBI-25861172, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11256614}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96Q11-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96Q11-2; Sequence=VSP_008442;
CC Name=3;
CC IsoId=Q96Q11-3; Sequence=VSP_008440, VSP_008441;
CC -!- DISEASE: Sideroblastic anemia with B-cell immunodeficiency, periodic
CC fevers, and developmental delay (SIFD) [MIM:616084]: An autosomal
CC recessive disease characterized by severe sideroblastic anemia with
CC onset in the neonatal period or infancy, recurrent periodic fevers
CC without an infectious etiology, B-cell lymphopenia and
CC hypogammaglobulinemia. Affected individuals show delayed psychomotor
CC development with variable neurodegeneration. Additional variable
CC features include sensorineural hearing loss, retinitis pigmentosa,
CC nephrocalcinosis, and cardiomyopathy. {ECO:0000269|PubMed:25193871}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Retinitis pigmentosa and erythrocytic microcytosis (RPEM)
CC [MIM:616959]: An autosomal recessive disease characterized by retinitis
CC pigmentosa, red blood cell microcytosis and anisocytosis with mild
CC anemia. {ECO:0000269|PubMed:26494905}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34042.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH12537.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB063105; BAB70662.1; -; mRNA.
DR EMBL; AF151805; AAD34042.1; ALT_FRAME; mRNA.
DR EMBL; AK290411; BAF83100.1; -; mRNA.
DR EMBL; AL834397; CAD39059.1; -; mRNA.
DR EMBL; AC024060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW63886.1; -; Genomic_DNA.
DR EMBL; BC005184; AAH05184.1; -; mRNA.
DR EMBL; BC012537; AAH12537.1; ALT_INIT; mRNA.
DR CCDS; CCDS2561.2; -. [Q96Q11-1]
DR CCDS; CCDS77691.1; -. [Q96Q11-2]
DR RefSeq; NP_001289875.1; NM_001302946.1. [Q96Q11-2]
DR RefSeq; NP_886552.2; NM_182916.2. [Q96Q11-1]
DR RefSeq; XP_011532078.1; XM_011533776.2.
DR RefSeq; XP_011532079.1; XM_011533777.2.
DR RefSeq; XP_011532080.1; XM_011533778.2.
DR PDB; 1OU5; X-ray; 3.40 A; A/B=30-434.
DR PDB; 4X4W; X-ray; 1.90 A; A/B=28-434.
DR PDBsum; 1OU5; -.
DR PDBsum; 4X4W; -.
DR AlphaFoldDB; Q96Q11; -.
DR SMR; Q96Q11; -.
DR BioGRID; 119284; 46.
DR IntAct; Q96Q11; 7.
DR STRING; 9606.ENSP00000251607; -.
DR GlyGen; Q96Q11; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96Q11; -.
DR PhosphoSitePlus; Q96Q11; -.
DR BioMuta; TRNT1; -.
DR DMDM; 296452848; -.
DR EPD; Q96Q11; -.
DR jPOST; Q96Q11; -.
DR MassIVE; Q96Q11; -.
DR MaxQB; Q96Q11; -.
DR PaxDb; Q96Q11; -.
DR PeptideAtlas; Q96Q11; -.
DR PRIDE; Q96Q11; -.
DR ProteomicsDB; 77807; -. [Q96Q11-1]
DR ProteomicsDB; 77808; -. [Q96Q11-2]
DR ProteomicsDB; 77809; -. [Q96Q11-3]
DR Antibodypedia; 25074; 59 antibodies from 18 providers.
DR DNASU; 51095; -.
DR Ensembl; ENST00000251607.11; ENSP00000251607.6; ENSG00000072756.17. [Q96Q11-1]
DR Ensembl; ENST00000280591.10; ENSP00000280591.6; ENSG00000072756.17. [Q96Q11-2]
DR Ensembl; ENST00000339437.11; ENSP00000342985.6; ENSG00000072756.17. [Q96Q11-3]
DR Ensembl; ENST00000402675.5; ENSP00000385745.1; ENSG00000072756.17. [Q96Q11-3]
DR Ensembl; ENST00000420393.5; ENSP00000400394.1; ENSG00000072756.17. [Q96Q11-3]
DR Ensembl; ENST00000434583.5; ENSP00000415100.1; ENSG00000072756.17. [Q96Q11-1]
DR GeneID; 51095; -.
DR KEGG; hsa:51095; -.
DR MANE-Select; ENST00000251607.11; ENSP00000251607.6; NM_182916.3; NP_886552.3.
DR UCSC; uc003bpn.2; human. [Q96Q11-1]
DR CTD; 51095; -.
DR DisGeNET; 51095; -.
DR GeneCards; TRNT1; -.
DR HGNC; HGNC:17341; TRNT1.
DR HPA; ENSG00000072756; Low tissue specificity.
DR MalaCards; TRNT1; -.
DR MIM; 612907; gene.
DR MIM; 616084; phenotype.
DR MIM; 616959; phenotype.
DR neXtProt; NX_Q96Q11; -.
DR OpenTargets; ENSG00000072756; -.
DR Orphanet; 369861; Congenital sideroblastic anemia-B-cell immunodeficiency-periodic fever-developmental delay syndrome.
DR PharmGKB; PA38446; -.
DR VEuPathDB; HostDB:ENSG00000072756; -.
DR eggNOG; KOG2159; Eukaryota.
DR GeneTree; ENSGT00390000009678; -.
DR HOGENOM; CLU_206721_0_0_1; -.
DR InParanoid; Q96Q11; -.
DR OMA; YNYELRI; -.
DR OrthoDB; 730946at2759; -.
DR PhylomeDB; Q96Q11; -.
DR TreeFam; TF313253; -.
DR BRENDA; 2.7.7.72; 2681.
DR PathwayCommons; Q96Q11; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-6785470; tRNA processing in the mitochondrion.
DR SignaLink; Q96Q11; -.
DR BioGRID-ORCS; 51095; 734 hits in 1096 CRISPR screens.
DR ChiTaRS; TRNT1; human.
DR EvolutionaryTrace; Q96Q11; -.
DR GeneWiki; TRNT1; -.
DR GenomeRNAi; 51095; -.
DR Pharos; Q96Q11; Tbio.
DR PRO; PR:Q96Q11; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96Q11; protein.
DR Bgee; ENSG00000072756; Expressed in endothelial cell and 182 other tissues.
DR ExpressionAtlas; Q96Q11; baseline and differential.
DR Genevisible; Q96Q11; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0034062; F:5'-3' RNA polymerase activity; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; TAS:UniProtKB.
DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IDA: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; IDA:UniProtKB.
DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:1990180; P:mitochondrial tRNA 3'-end processing; IDA:UniProtKB.
DR GO; GO:0042780; P:tRNA 3'-end processing; TAS:Reactome.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IDA:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR DisProt; DP02803; -.
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 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Disease variant; Disulfide bond; Magnesium; Mitochondrion;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Reference proteome; Retinitis pigmentosa; RNA-binding; Transferase;
KW Transit peptide; 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_0000004782"
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:0007744|PubMed:20068231"
FT MOD_RES 402
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT DISULFID 373
FT /note="Interchain"
FT VAR_SEQ 50..57
FT /note="ELFVKENH -> GINAFHEN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008440"
FT VAR_SEQ 58..434
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008441"
FT VAR_SEQ 248..267
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008442"
FT VARIANT 23
FT /note="P -> L (in dbSNP:rs334773)"
FT /evidence="ECO:0000269|PubMed:10810093,
FT ECO:0000269|PubMed:11504732, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.6"
FT /id="VAR_048698"
FT VARIANT 43
FT /note="Missing (in RPEM)"
FT /evidence="ECO:0000269|PubMed:26494905"
FT /id="VAR_076924"
FT VARIANT 154
FT /note="T -> I (in SIFD; reduced activity;
FT dbSNP:rs606231290)"
FT /evidence="ECO:0000269|PubMed:25193871"
FT /id="VAR_072421"
FT VARIANT 158
FT /note="M -> V (in SIFD; loss of activity;
FT dbSNP:rs771781629)"
FT /evidence="ECO:0000269|PubMed:25193871"
FT /id="VAR_072422"
FT VARIANT 166
FT /note="L -> S (in SIFD; loss of activity;
FT dbSNP:rs606231289)"
FT /evidence="ECO:0000269|PubMed:25193871"
FT /id="VAR_072423"
FT VARIANT 190
FT /note="R -> I (in SIFD; loss of activity;
FT dbSNP:rs606231287)"
FT /evidence="ECO:0000269|PubMed:25193871"
FT /id="VAR_072424"
FT VARIANT 223
FT /note="I -> T (in SIFD; loss of activity;
FT dbSNP:rs370011798)"
FT /evidence="ECO:0000269|PubMed:25193871"
FT /id="VAR_072425"
FT VARIANT 326
FT /note="I -> T (in SIFD; loss of activity)"
FT /evidence="ECO:0000269|PubMed:25193871"
FT /id="VAR_072426"
FT VARIANT 416
FT /note="K -> E (in SIFD; dbSNP:rs199931785)"
FT /evidence="ECO:0000269|PubMed:25193871"
FT /id="VAR_072427"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1OU5"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:4X4W"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:4X4W"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 358..368
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 390..395
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 401..417
FT /evidence="ECO:0007829|PDB:4X4W"
FT HELIX 424..434
FT /evidence="ECO:0007829|PDB:4X4W"
SQ SEQUENCE 434 AA; 50128 MW; 60B7387E203A53D0 CRC64;
MLRCLYHWHR PVLNRRWSRL CLPKQYLFTM KLQSPEFQSL FTEGLKSLTE LFVKENHELR
IAGGAVRDLL NGVKPQDIDF ATTATPTQMK EMFQSAGIRM INNRGEKHGT ITARLHEENF
EITTLRIDVT TDGRHAEVEF TTDWQKDAER RDLTINSMFL GFDGTLFDYF NGYEDLKNKK
VRFVGHAKQR IQEDYLRILR YFRFYGRIVD KPGDHDPETL EAIAENAKGL AGISGERIWV
ELKKILVGNH VNHLIHLIYD LDVAPYIGLP ANASLEEFDK VSKNVDGFSP KPVTLLASLF
KVQDDVTKLD LRLKIAKEEK NLGLFIVKNR KDLIKATDSS DPLKPYQDFI IDSREPDATT
RVCELLKYQG EHCLLKEMQQ WSIPPFPVSG HDIRKVGISS GKEIGALLQQ LREQWKKSGY
QMEKDELLSY IKKT
