Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

tRNA methyltransferase 10 homolog C

Gene

TRMT10C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial tRNA N1-methyltransferase involved in mitochondrial tRNA maturation (PubMed:18984158, PubMed:21593607, PubMed:23042678, PubMed:27132592). Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP3, which cleaves tRNA molecules in their 5'-ends (PubMed:18984158). Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity (PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of N1-methylguanine and N1-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting as the catalytic N1-methyltransferase subunit (PubMed:23042678). The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme (PubMed:29040705). In addition to tRNA N1-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA N1-methyltransferase by mediating methylation of adenosine residues at the N1 position of MT-ND5 mRNA (PubMed:29072297).6 Publications

Catalytic activityi

S-adenosyl-L-methionine + adenine9 in tRNA = S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA.1 Publication
S-adenosyl-L-methionine + guanine9 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA.1 Publication
S-adenosyl-L-methionine + adenine in mRNA = S-adenosyl-L-homocysteine + N1-methyladenine in mRNA.1 Publication

GO - Molecular functioni

  • mRNA (adenine-N1-)-methyltransferase activity Source: UniProtKB
  • RNA binding Source: UniProtKB
  • tRNA (adenine-N1-)-methyltransferase activity Source: CAFA
  • tRNA (guanine(9)-N(1))-methyltransferase activity Source: UniProtKB-EC
  • tRNA (guanine-N1-)-methyltransferase activity Source: CAFA
  • tRNA binding Source: UniProtKB

GO - Biological processi

  • mitochondrial RNA 5'-end processing Source: UniProtKB
  • mitochondrial tRNA 3'-end processing Source: UniProtKB
  • mitochondrial tRNA 5'-end processing Source: UniProtKB
  • mitochondrial tRNA methylation Source: Reactome
  • mitochondrial tRNA processing Source: UniProtKB
  • mRNA methylation Source: UniProtKB
  • positive regulation of mitochondrial translation Source: UniProtKB

Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processtRNA processing
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-HSA-6785470. tRNA processing in the mitochondrion.
R-HSA-6787450. tRNA modification in the mitochondrion.
R-HSA-8868766. rRNA processing in the mitochondrion.

Protein family/group databases

MoonProtiQ7L0Y3.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA methyltransferase 10 homolog CCurated
Alternative name(s):
HBV pre-S2 trans-regulated protein 21 Publication
Mitochondrial ribonuclease P protein 11 Publication
Short name:
Mitochondrial RNase P protein 11 Publication
RNA (guanine-9-)-methyltransferase domain-containing protein 1
Renal carcinoma antigen NY-REN-491 Publication
mRNA methyladenosine-N(1)-methyltransferase1 Publication (EC:2.1.1.-1 Publication)
tRNA (adenine(9)-N(1))-methyltransferase (EC:2.1.1.2181 Publication)
tRNA (guanine(9)-N(1))-methyltransferase (EC:2.1.1.2211 Publication)
Gene namesi
Name:TRMT10CImported
Synonyms:MRPP11 Publication, RG9MTD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000174173.6.
HGNCiHGNC:26022. TRMT10C.
MIMi615423. gene.
neXtProtiNX_Q7L0Y3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion, Mitochondrion nucleoid

Pathology & Biotechi

Involvement in diseasei

Combined oxidative phosphorylation deficiency 30 (COXPD30)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive, severe mitochondrial disease characterized by lactic acidosis, hypotonia, feeding difficulties, deafness, and respiratory failure with fatal issue. Patient skeletal muscle cells show decreased activities of mitochondrial complexes I, III and IV.
See also OMIM:616974
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076993181R → L in COXPD30; decreased protein abundance; impaired mitochondrial tRNA processing; has no effect on steady-state mitochondrial-mRNA and mitochondrial-tRNA levels but indirectly impairs mitochondrial translation. 1 PublicationCorresponds to variant dbSNP:rs199730889Ensembl.1
Natural variantiVAR_076994272T → A in COXPD30; decreased protein abundance; impaired mitochondrial tRNA processing; has no effect on steady-state mitochondrial-mRNA and mitochondrial-tRNA levels but indirectly impairs mitochondrial translation. 1 PublicationCorresponds to variant dbSNP:rs875989831Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi314D → N: Abolished mitochondrial tRNA methylation. Does not affect mitochondrial tRNA 5'-end processing. 1 Publication1

Keywords - Diseasei

Disease mutation, Primary mitochondrial disease

Organism-specific databases

DisGeNETi54931.
MalaCardsiTRMT10C.
MIMi616974. phenotype.
OpenTargetsiENSG00000174173.
PharmGKBiPA134988378.

Polymorphism and mutation databases

DMDMi221222465.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 39MitochondrionSequence analysisAdd BLAST39
ChainiPRO_000031130940 – 403tRNA methyltransferase 10 homolog CAdd BLAST364

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei84PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7L0Y3.
MaxQBiQ7L0Y3.
PaxDbiQ7L0Y3.
PeptideAtlasiQ7L0Y3.
PRIDEiQ7L0Y3.
TopDownProteomicsiQ7L0Y3.

PTM databases

iPTMnetiQ7L0Y3.
PhosphoSitePlusiQ7L0Y3.

Expressioni

Gene expression databases

BgeeiENSG00000174173.
CleanExiHS_RG9MTD1.
ExpressionAtlasiQ7L0Y3. baseline and differential.
GenevisibleiQ7L0Y3. HS.

Organism-specific databases

HPAiHPA036671.

Interactioni

Subunit structurei

Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31.(PubMed:18984158). Interacts with HSD17B10/MRPP2; forming the MRPP1-MRPP2 subcomplex of the mitochondrial ribonuclease P complex (PubMed:23042678, PubMed:29040705). Interacts with GRSF1 (PubMed:23473034).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSD17B10Q997144EBI-2107046,EBI-79964

Protein-protein interaction databases

BioGridi120271. 31 interactors.
IntActiQ7L0Y3. 29 interactors.
MINTiMINT-4992496.
STRINGi9606.ENSP00000312356.

Structurei

3D structure databases

ProteinModelPortaliQ7L0Y3.
SMRiQ7L0Y3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini191 – 383SAM-dependent MTase TRM10-typePROSITE-ProRule annotationAdd BLAST193

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili138 – 169Sequence analysisAdd BLAST32

Sequence similaritiesi

Belongs to the class IV-like SAM-binding methyltransferase superfamily. TRM10 family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

eggNOGiKOG2967. Eukaryota.
ENOG4111JE4. LUCA.
GeneTreeiENSGT00530000063169.
HOGENOMiHOG000088648.
HOVERGENiHBG108146.
InParanoidiQ7L0Y3.
KOiK17654.
OMAiKTLMECV.
OrthoDBiEOG091G09AL.
PhylomeDBiQ7L0Y3.
TreeFamiTF319795.

Family and domain databases

InterProiView protein in InterPro
IPR025812. MRPP1.
IPR028564. MT_TRM10-typ.
IPR007356. tRNA_m1G_MeTrfase_euk.
IPR016009. tRNA_MeTrfase_TRMD/TRM10.
PANTHERiPTHR13563. PTHR13563. 1 hit.
PTHR13563:SF5. PTHR13563:SF5. 1 hit.
PfamiView protein in Pfam
PF01746. tRNA_m1G_MT. 1 hit.
PROSITEiView protein in PROSITE
PS51675. SAM_MT_TRM10. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7L0Y3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAFLKMSVS VNFFRPFTRF LVPFTLHRKR NNLTILQRYM SSKIPAVTYP
60 70 80 90 100
KNESTPPSEE LELDKWKTTM KSSVQEECVS TISSSKDEDP LAATREFIEM
110 120 130 140 150
WRLLGREVPE HITEEELKTL MECVSNTAKK KYLKYLYTKE KVKKARQIKK
160 170 180 190 200
EMKAAAREEA KNIKLLETTE EDKQKNFLFL RLWDRNMDIA MGWKGAQAMQ
210 220 230 240 250
FGQPLVFDMA YENYMKRKEL QNTVSQLLES EGWNRRNVDP FHIYFCNLKI
260 270 280 290 300
DGALHRELVK RYQEKWDKLL LTSTEKSHVD LFPKDSIIYL TADSPNVMTT
310 320 330 340 350
FRHDKVYVIG SFVDKSMQPG TSLAKAKRLN LATECLPLDK YLQWEIGNKN
360 370 380 390 400
LTLDQMIRIL LCLKNNGNWQ EALQFVPKRK HTGFLEISQH SQEFINRLKK

AKT
Length:403
Mass (Da):47,347
Last modified:January 20, 2009 - v2
Checksum:i28CBD97B4114819F
GO

Sequence cautioni

The sequence AAD42877 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH35967 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA91166 differs from that shown. Reason: Frameshift at position 128.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05735556P → R1 PublicationCorresponds to variant dbSNP:rs3762735Ensembl.1
Natural variantiVAR_057356164K → N. Corresponds to variant dbSNP:rs16844031Ensembl.1
Natural variantiVAR_076993181R → L in COXPD30; decreased protein abundance; impaired mitochondrial tRNA processing; has no effect on steady-state mitochondrial-mRNA and mitochondrial-tRNA levels but indirectly impairs mitochondrial translation. 1 PublicationCorresponds to variant dbSNP:rs199730889Ensembl.1
Natural variantiVAR_076994272T → A in COXPD30; decreased protein abundance; impaired mitochondrial tRNA processing; has no effect on steady-state mitochondrial-mRNA and mitochondrial-tRNA levels but indirectly impairs mitochondrial translation. 1 PublicationCorresponds to variant dbSNP:rs875989831Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226052 mRNA. Translation: AAF86952.1.
AK000439 mRNA. Translation: BAA91166.1. Frameshift.
CH471052 Genomic DNA. Translation: EAW79795.1.
BC035967 mRNA. Translation: AAH35967.2. Different initiation.
AF155111 mRNA. Translation: AAD42877.1. Different initiation.
AY561707 mRNA. Translation: AAS66980.1.
CCDSiCCDS43122.1.
RefSeqiNP_060289.2. NM_017819.3.
UniGeneiHs.594839.
Hs.740864.
Hs.744223.

Genome annotation databases

EnsembliENST00000309922; ENSP00000312356; ENSG00000174173.
GeneIDi54931.
KEGGihsa:54931.
UCSCiuc003duz.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTM10C_HUMAN
AccessioniPrimary (citable) accession number: Q7L0Y3
Secondary accession number(s): Q9NRG5, Q9NX54, Q9Y596
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: January 20, 2009
Last modified: January 31, 2018
This is version 125 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-7 is the initiator.Curated
The identity of the enzyme catalyzing mitochondrial mRNA N1-methyltransferase is unclear. According to a report, mitochondrial mRNA N1-methyltransferase activity is catalyzed by TRMT61B (AC Q9BVS5) (PubMed:29107537). According to a second report, it is mediated by TRMT10C (PubMed:29072297). As both reports only tested one protein (either TRMT61B or TRMT10C), it is possible that both proteins have this activity.2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families