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Q8K1J6 (TRNT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CCA tRNA nucleotidyltransferase 1, mitochondrial

EC=2.7.7.72
Alternative name(s):
mitochondrial tRNA nucleotidyl transferase, CCA-adding
Short name=mt CCA-adding enzyme
Short name=mt tRNA CCA-diphosphorylase
Short name=mt tRNA CCA-pyrophosphorylase
Short name=mt tRNA adenylyltransferase
Gene names
Name:Trnt1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates By similarity.

Catalytic activity

A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate.

Cofactor

Magnesium Probable.

Subunit structure

Monomer and homodimer By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandATP-binding
Magnesium
Nucleotide-binding
RNA-binding
   Molecular functionNucleotidyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA 3'-end processing

Inferred from sequence or structural similarity. Source: UniProtKB

tRNA 3'-terminal CCA addition

Inferred from electronic annotation. Source: UniProtKB-EC

tRNA processing

Inferred from sequence orthology Ref.1. Source: MGI

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

CTP:3'-cytidine-tRNA cytidylyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

CTP:tRNA cytidylyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

tRNA adenylyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

tRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

tRNA nucleotidyltransferase activity

Inferred from sequence orthology Ref.1. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K1J6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8K1J6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     204-215: FYGRIVDRPGDH → PGIVLGDLTTEK
     216-434: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4141Mitochondrion Potential
Chain42 – 434393CCA tRNA nucleotidyltransferase 1, mitochondrial
PRO_0000004783

Sites

Active site771 By similarity
Active site791 By similarity
Active site1211 By similarity

Amino acid modifications

Modified residue4001Phosphoserine By similarity
Modified residue4021N6-acetyllysine Ref.4

Natural variations

Alternative sequence204 – 21512FYGRI…RPGDH → PGIVLGDLTTEK in isoform 2.
VSP_018616
Alternative sequence216 – 434219Missing in isoform 2.
VSP_018617

Experimental info

Sequence conflict2021F → I in BAB70663. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 0578FB438165838B

FASTA43449,895
        10         20         30         40         50         60 
MQSVLYPWHR QVLRCSWSRL CLLKRYLFTM KLQSPEFQSL FTEGLKSLTE LFAKENHELR 

        70         80         90        100        110        120 
IAGGAVRDLL NGVKPQDVDF ATTATPTQMK EMFQSAGIRM INNKGEKHGT ITARLHEENF 

       130        140        150        160        170        180 
EVTTLRIDVT TDGRHAEVEF TTDWQKDAER RDLTINSMFL GFDGTLFDYF NGYADLKNKK 

       190        200        210        220        230        240 
VRFVGHAKQR IQEDYLRILR YFRFYGRIVD RPGDHDHETL EAIAENAKGL AGISGERIWV 

       250        260        270        280        290        300 
ELKKILTGDH VNHLIHLIYD LGVAPHIGLP ANANLEEFNK VSKNVEGFSP KPMTLLASLF 

       310        320        330        340        350        360 
KVQDDVTKLD LRLKISKEEK NLGLFIVKNR KDLIKATDSS EPLKPYQDFV IDSREPDATA 

       370        380        390        400        410        420 
RVCELLKYQG EHGLLKEMQQ WSVPPFPVSG HDIRKVGISS GKEIGALLQQ LREQWKKSGY 

       430 
RMEKDELLSY IKKT 

« Hide

Isoform 2 [UniParc].

Checksum: B0AEFBB90317372B
Show »

FASTA21525,018

References

« Hide 'large scale' references
[1]"Identification and characterization of mammalian mitochondrial tRNA nucleotidyltransferases."
Nagaike T., Suzuki T., Tomari Y., Takemoto-Hori C., Negayama F., Watanabe K., Ueda T.
J. Biol. Chem. 276:40041-40049(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Blastocyst, Bone marrow macrophage, Egg and Embryo.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary gland.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB063106 mRNA. Translation: BAB70663.1.
AK011764 mRNA. Translation: BAB27827.3.
AK135791 mRNA. Translation: BAE22664.1.
AK152739 mRNA. Translation: BAE31459.1.
AK166804 mRNA. Translation: BAE39032.1.
BC031764 mRNA. Translation: AAH31764.1.
CCDSCCDS20397.1. [Q8K1J6-1]
CCDS57443.1. [Q8K1J6-2]
RefSeqNP_001229287.1. NM_001242358.1. [Q8K1J6-1]
NP_001229289.1. NM_001242360.1. [Q8K1J6-2]
NP_081572.1. NM_027296.3. [Q8K1J6-1]
XP_006506643.1. XM_006506580.1. [Q8K1J6-1]
XP_006506644.1. XM_006506581.1. [Q8K1J6-1]
UniGeneMm.196332.

3D structure databases

ProteinModelPortalQ8K1J6.
SMRQ8K1J6. Positions 30-431.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000108874.

PTM databases

PhosphoSiteQ8K1J6.

Proteomic databases

MaxQBQ8K1J6.
PaxDbQ8K1J6.
PRIDEQ8K1J6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057578; ENSMUSP00000060900; ENSMUSG00000013736. [Q8K1J6-1]
ENSMUST00000113247; ENSMUSP00000108873; ENSMUSG00000013736. [Q8K1J6-2]
ENSMUST00000113248; ENSMUSP00000108874; ENSMUSG00000013736. [Q8K1J6-1]
ENSMUST00000113249; ENSMUSP00000108875; ENSMUSG00000013736. [Q8K1J6-1]
GeneID70047.
KEGGmmu:70047.
UCSCuc009dcy.2. mouse. [Q8K1J6-1]
uc029vxx.1. mouse. [Q8K1J6-2]

Organism-specific databases

CTD51095.
MGIMGI:1917297. Trnt1.

Phylogenomic databases

eggNOGCOG0617.
GeneTreeENSGT00390000009678.
HOGENOMHOG000253345.
HOVERGENHBG061403.
InParanoidQ8K1J6.
KOK00974.
OMAKGSCDID.
OrthoDBEOG7CCBR5.
PhylomeDBQ8K1J6.
TreeFamTF313253.

Gene expression databases

BgeeQ8K1J6.
CleanExMM_TRNT1.
GenevestigatorQ8K1J6.

Family and domain databases

InterProIPR002646. PolA_pol_head_dom.
[Graphical view]
PfamPF01743. PolyA_pol. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio330891.
PROQ8K1J6.
SOURCESearch...

Entry information

Entry nameTRNT1_MOUSE
AccessionPrimary (citable) accession number: Q8K1J6
Secondary accession number(s): Q3TKW1 expand/collapse secondary AC list , Q3UX99, Q920N6, Q9CSX0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot