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Protein

mRNA-capping enzyme

Gene

Rngtt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus.2 Publications

Catalytic activityi

A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.1 Publication
GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.1 Publication

Enzyme regulationi

RNA triphosphatase activity is inhibited by vanadate, iodoacetate and magnesium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei126 – 1261For RNA 5'-triphosphatase activityBy similarity
Active sitei294 – 2941N6-GMP-lysine intermediate
Binding sitei299 – 2991GTP
Binding sitei315 – 3151GTPSequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi343 – 3453GTPSequence analysis
Nucleotide bindingi458 – 4603GTPSequence analysis
Nucleotide bindingi528 – 5336GTPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.7.50. 3474.
ReactomeiR-MMU-72086. mRNA Capping.
R-MMU-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-capping enzyme
Alternative name(s):
HCE
MCE1
Including the following 2 domains:
Polynucleotide 5'-triphosphatase (EC:3.1.3.33)
Short name:
TPase
Short name:
mRNA 5'-triphosphatase
mRNA guanylyltransferase (EC:2.7.7.50)
Alternative name(s):
GTP--RNA guanylyltransferase
Short name:
GTase
Gene namesi
Name:Rngtt
Synonyms:Cap1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1329041. Rngtt.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361D → A: No effect. 1 Publication
Mutagenesisi66 – 661D → A: Decrease of >90% of TPase activity. 1 Publication
Mutagenesisi110 – 1101C → S: No effect. 1 Publication
Mutagenesisi125 – 1251H → A: Decrease of 55-60% of TPase activity. 1 Publication
Mutagenesisi126 – 1261C → S: Loss of TPase activity. 1 Publication
Mutagenesisi132 – 1321R → A: Loss of TPase activity. 1 Publication
Mutagenesisi133 – 1331T → A: Decrease of 55-60% of TPase activity. 1 Publication
Mutagenesisi138 – 1381C → S: No effect. 1 Publication
Mutagenesisi168 – 1681D → A: No effect. 1 Publication
Mutagenesisi290 – 2901K → A: No effect. 1 Publication
Mutagenesisi294 – 2941K → A: Loss of GTase activity. 1 Publication
Mutagenesisi315 – 3151R → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication
Mutagenesisi315 – 3151R → K: At least 60% of RNA-binding activity and loss of GTase activity. 1 Publication
Mutagenesisi375 – 3751C → R: Increases stimulation of GTase activity by POLR2A binding. 1 Publication
Mutagenesisi530 – 5301R → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication
Mutagenesisi530 – 5301R → K: Loss of GTase activity. 1 Publication
Mutagenesisi533 – 5331K → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication
Mutagenesisi533 – 5331K → R: At least 60% of RNA-binding activity and loss of GTase activity. 1 Publication
Mutagenesisi537 – 5371N → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication
Mutagenesisi537 – 5371N → Q: At least 60% of RNA binding activity and loss of GTase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 597597mRNA-capping enzymePRO_0000210109Add
BLAST

Proteomic databases

EPDiO55236.
PaxDbiO55236.
PeptideAtlasiO55236.
PRIDEiO55236.

PTM databases

iPTMnetiO55236.
PhosphoSiteiO55236.

Expressioni

Gene expression databases

BgeeiO55236.
CleanExiMM_RNGTT.
ExpressionAtlasiO55236. baseline and differential.
GenevisibleiO55236. MM.

Interactioni

Subunit structurei

Interacts with SUPT5H and RNMT (By similarity). Interacts with POLR2A (via C-terminus); this enhances guanylyltransferase activity. Binds (via GTase domain) to the elongating phosphorylated form of RNA polymerase II; can form direct interactions with the phosphorylated POLR2A C-terminal domain and indirect interactions via bound RNA.By similarity3 Publications

Protein-protein interaction databases

DIPiDIP-61013N.
STRINGi10090.ENSMUSP00000103788.

Structurei

Secondary structure

1
597
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni21 – 233Combined sources
Beta strandi24 – 274Combined sources
Helixi33 – 353Combined sources
Turni36 – 383Combined sources
Helixi41 – 433Combined sources
Helixi47 – 5610Combined sources
Beta strandi61 – 666Combined sources
Beta strandi71 – 744Combined sources
Helixi77 – 804Combined sources
Turni81 – 833Combined sources
Beta strandi85 – 884Combined sources
Helixi100 – 11011Combined sources
Turni111 – 1155Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi127 – 1304Combined sources
Helixi131 – 14515Combined sources
Helixi149 – 15911Combined sources
Helixi167 – 17711Combined sources
Helixi180 – 1823Combined sources
Helixi191 – 1944Combined sources
Beta strandi232 – 2365Combined sources
Beta strandi241 – 2433Combined sources
Helixi249 – 26012Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi270 – 2756Combined sources
Helixi280 – 2823Combined sources
Helixi283 – 2864Combined sources
Beta strandi289 – 2946Combined sources
Beta strandi298 – 3047Combined sources
Beta strandi310 – 3134Combined sources
Beta strandi319 – 3224Combined sources
Beta strandi332 – 3365Combined sources
Beta strandi339 – 36729Combined sources
Helixi372 – 3743Combined sources
Helixi377 – 38711Combined sources
Helixi389 – 39810Combined sources
Turni403 – 4053Combined sources
Beta strandi406 – 4127Combined sources
Helixi418 – 4203Combined sources
Helixi421 – 4244Combined sources
Beta strandi439 – 4468Combined sources
Beta strandi451 – 4599Combined sources
Helixi539 – 55012Combined sources
Helixi555 – 56511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I9SX-ray1.65A1-210[»]
1I9TX-ray1.70A1-210[»]
3RTXX-ray2.81A/B226-567[»]
ProteinModelPortaliO55236.
SMRiO55236. Positions 5-194, 226-565.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO55236.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 212212TPaseAdd
BLAST
Regioni229 – 597369GTaseAdd
BLAST
Regioni330 – 38657Interaction with POLR2AAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi195 – 20511Asp/Glu-richAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family.Curated
In the C-terminal section; belongs to the eukaryotic GTase family.Curated

Phylogenomic databases

eggNOGiKOG2386. Eukaryota.
COG5226. LUCA.
HOGENOMiHOG000264524.
HOVERGENiHBG006332.
InParanoidiO55236.
KOiK13917.
OMAiRFNERSP.
OrthoDBiEOG7HB592.
PhylomeDBiO55236.
TreeFamiTF314914.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR017074. mRNA_cap_enz_bifunc.
IPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
IPR012340. NA-bd_OB-fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
PF03919. mRNA_cap_C. 1 hit.
PF01331. mRNA_cap_enzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF036958. mRNA_capping_HCE. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O55236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML
60 70 80 90 100
SNYLKSLKVK MSLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT
110 120 130 140 150
ENTETFIRLC ERFNERSPPE LIGVHCTHGF NRTGFLICAF LVEKMDWSIE
160 170 180 190 200
AAVATFAQAR PPGIYKGDYL KELFRRYGDI EEAPPPPVLP DWCFEDEDEE
210 220 230 240 250
DEDEDGKKDS EPGSSASFSK RRKERLKLGA IFLEGITVKG VTQVTTQPKL
260 270 280 290 300
GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IRLLEQKPYK VSWKADGTRY
310 320 330 340 350
MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDK
360 370 380 390 400
VNGQAVPRYL IYDIIKFNAQ PVGDCDFNIR LQCIEREIIS PRHEKMKTGL
410 420 430 440 450
IDKTQEPFSV RPKQFFDINI SRKLLEGNFA KEVSHEMDGL IFQPIGKYKP
460 470 480 490 500
GRCDDILKWK PPSLNSVDFR LKITRMGGEG LLPQNVGLLY VGGYERPFAQ
510 520 530 540 550
IKVTKELKQY DNKIIECKFE NNSWVFMRQR IDKSFPNAYN TAMAVCNSIS
560 570 580 590
NPVTKEMLFE FIDRCAAAAQ GQKRKYPLDP DTELMPPPPP KRLHRPT
Length:597
Mass (Da):68,684
Last modified:June 1, 1998 - v1
Checksum:iB2A9E711889D8EA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025653 mRNA. Translation: AAB91558.1.
AF034568 mRNA. Translation: AAB88903.1.
BC043657 mRNA. Translation: AAH43657.1.
CCDSiCCDS38705.1.
RefSeqiNP_036014.1. NM_011884.3.
UniGeneiMm.240024.
Mm.464346.

Genome annotation databases

EnsembliENSMUST00000108153; ENSMUSP00000103788; ENSMUSG00000028274.
GeneIDi24018.
KEGGimmu:24018.
UCSCiuc008sfv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025653 mRNA. Translation: AAB91558.1.
AF034568 mRNA. Translation: AAB88903.1.
BC043657 mRNA. Translation: AAH43657.1.
CCDSiCCDS38705.1.
RefSeqiNP_036014.1. NM_011884.3.
UniGeneiMm.240024.
Mm.464346.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I9SX-ray1.65A1-210[»]
1I9TX-ray1.70A1-210[»]
3RTXX-ray2.81A/B226-567[»]
ProteinModelPortaliO55236.
SMRiO55236. Positions 5-194, 226-565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61013N.
STRINGi10090.ENSMUSP00000103788.

PTM databases

iPTMnetiO55236.
PhosphoSiteiO55236.

Proteomic databases

EPDiO55236.
PaxDbiO55236.
PeptideAtlasiO55236.
PRIDEiO55236.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108153; ENSMUSP00000103788; ENSMUSG00000028274.
GeneIDi24018.
KEGGimmu:24018.
UCSCiuc008sfv.2. mouse.

Organism-specific databases

CTDi8732.
MGIiMGI:1329041. Rngtt.

Phylogenomic databases

eggNOGiKOG2386. Eukaryota.
COG5226. LUCA.
HOGENOMiHOG000264524.
HOVERGENiHBG006332.
InParanoidiO55236.
KOiK13917.
OMAiRFNERSP.
OrthoDBiEOG7HB592.
PhylomeDBiO55236.
TreeFamiTF314914.

Enzyme and pathway databases

BRENDAi2.7.7.50. 3474.
ReactomeiR-MMU-72086. mRNA Capping.
R-MMU-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

EvolutionaryTraceiO55236.
PROiO55236.
SOURCEiSearch...

Gene expression databases

BgeeiO55236.
CleanExiMM_RNGTT.
ExpressionAtlasiO55236. baseline and differential.
GenevisibleiO55236. MM.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR017074. mRNA_cap_enz_bifunc.
IPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
IPR012340. NA-bd_OB-fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
PF03919. mRNA_cap_C. 1 hit.
PF01331. mRNA_cap_enzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF036958. mRNA_capping_HCE. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II."
    Yue Z., Maldonado E., Pillutla R., Cho H., Reinberg D., Shatkin A.J.
    Proc. Natl. Acad. Sci. U.S.A. 94:12898-12903(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-294, FUNCTION, SUBUNIT.
  2. "5'-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II."
    McCracken S., Fong N., Rosonina E., Yankulov K., Brothers G., Siderovski D., Hessel A., Foster S., Shuman S., Bentley D.L.
    Genes Dev. 11:3306-3318(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
  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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. "Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism."
    Wen Y., Yue Z., Shatkin A.J.
    Proc. Natl. Acad. Sci. U.S.A. 95:12226-12231(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Spleen and Testis.
  6. "Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme."
    Changela A., Ho C.K., Martins A., Shuman S., Mondragon A.
    EMBO J. 20:2575-2586(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
  7. "Structural insights to how mammalian capping enzyme reads the CTD code."
    Ghosh A., Shuman S., Lima C.D.
    Mol. Cell 43:299-310(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 226-567 IN COMPLEX WITH GUANINE AND POLR2A PEPTIDE, INTERACTION WITH POLR2A, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF CYS-375.

Entry informationi

Entry nameiMCE1_MOUSE
AccessioniPrimary (citable) accession number: O55236
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.