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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)DescriptionActionsGraphical viewLength
Active sitei126For RNA 5'-triphosphatase activityBy similarity1
Active sitei294N6-GMP-lysine intermediate1
Binding sitei299GTP1
Binding sitei315GTPSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi343 – 345GTPSequence analysis3
Nucleotide bindingi458 – 460GTPSequence analysis3
Nucleotide bindingi528 – 533GTPSequence analysis6

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)DescriptionActionsGraphical viewLength
Mutagenesisi36D → A: No effect. 1 Publication1
Mutagenesisi66D → A: Decrease of >90% of TPase activity. 1 Publication1
Mutagenesisi110C → S: No effect. 1 Publication1
Mutagenesisi125H → A: Decrease of 55-60% of TPase activity. 1 Publication1
Mutagenesisi126C → S: Loss of TPase activity. 1 Publication1
Mutagenesisi132R → A: Loss of TPase activity. 1 Publication1
Mutagenesisi133T → A: Decrease of 55-60% of TPase activity. 1 Publication1
Mutagenesisi138C → S: No effect. 1 Publication1
Mutagenesisi168D → A: No effect. 1 Publication1
Mutagenesisi290K → A: No effect. 1 Publication1
Mutagenesisi294K → A: Loss of GTase activity. 1 Publication1
Mutagenesisi315R → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication1
Mutagenesisi315R → K: At least 60% of RNA-binding activity and loss of GTase activity. 1 Publication1
Mutagenesisi375C → R: Increases stimulation of GTase activity by POLR2A binding. 1 Publication1
Mutagenesisi530R → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication1
Mutagenesisi530R → K: Loss of GTase activity. 1 Publication1
Mutagenesisi533K → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication1
Mutagenesisi533K → R: At least 60% of RNA-binding activity and loss of GTase activity. 1 Publication1
Mutagenesisi537N → A: Almost complete loss of RNA-binding and loss of GTase activity. 1 Publication1
Mutagenesisi537N → Q: At least 60% of RNA binding activity and loss of GTase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002101091 – 597mRNA-capping enzymeAdd BLAST597

Proteomic databases

EPDiO55236.
PaxDbiO55236.
PeptideAtlasiO55236.
PRIDEiO55236.

PTM databases

iPTMnetiO55236.
PhosphoSitePlusiO55236.

Expressioni

Gene expression databases

BgeeiENSMUSG00000028274.
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

1597
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni21 – 23Combined sources3
Beta strandi24 – 27Combined sources4
Helixi33 – 35Combined sources3
Turni36 – 38Combined sources3
Helixi41 – 43Combined sources3
Helixi47 – 56Combined sources10
Beta strandi61 – 66Combined sources6
Beta strandi71 – 74Combined sources4
Helixi77 – 80Combined sources4
Turni81 – 83Combined sources3
Beta strandi85 – 88Combined sources4
Helixi100 – 110Combined sources11
Turni111 – 115Combined sources5
Beta strandi121 – 125Combined sources5
Beta strandi127 – 130Combined sources4
Helixi131 – 145Combined sources15
Helixi149 – 159Combined sources11
Helixi167 – 177Combined sources11
Helixi180 – 182Combined sources3
Helixi191 – 194Combined sources4
Beta strandi232 – 236Combined sources5
Beta strandi241 – 243Combined sources3
Helixi249 – 260Combined sources12
Beta strandi265 – 267Combined sources3
Beta strandi270 – 275Combined sources6
Helixi280 – 282Combined sources3
Helixi283 – 286Combined sources4
Beta strandi289 – 294Combined sources6
Beta strandi298 – 304Combined sources7
Beta strandi310 – 313Combined sources4
Beta strandi319 – 322Combined sources4
Beta strandi332 – 336Combined sources5
Beta strandi339 – 367Combined sources29
Helixi372 – 374Combined sources3
Helixi377 – 387Combined sources11
Helixi389 – 398Combined sources10
Turni403 – 405Combined sources3
Beta strandi406 – 412Combined sources7
Helixi418 – 420Combined sources3
Helixi421 – 424Combined sources4
Beta strandi439 – 446Combined sources8
Beta strandi451 – 459Combined sources9
Helixi539 – 550Combined sources12
Helixi555 – 565Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO55236.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 212TPaseAdd BLAST212
Regioni229 – 597GTaseAdd BLAST369
Regioni330 – 386Interaction with POLR2A1 PublicationAdd BLAST57

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi195 – 205Asp/Glu-richAdd BLAST11

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.
GeneTreeiENSGT00530000063473.
HOGENOMiHOG000264524.
HOVERGENiHBG006332.
InParanoidiO55236.
KOiK13917.
OMAiRFNERSP.
OrthoDBiEOG091G063D.
PhylomeDBiO55236.
TreeFamiTF314914.

Family and domain databases

Gene3Di3.90.190.10. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I9SX-ray1.65A1-210[»]
1I9TX-ray1.70A1-210[»]
3RTXX-ray2.81A/B226-567[»]
ProteinModelPortaliO55236.
SMRiO55236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61013N.
STRINGi10090.ENSMUSP00000103788.

PTM databases

iPTMnetiO55236.
PhosphoSitePlusiO55236.

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.
GeneTreeiENSGT00530000063473.
HOGENOMiHOG000264524.
HOVERGENiHBG006332.
InParanoidiO55236.
KOiK13917.
OMAiRFNERSP.
OrthoDBiEOG091G063D.
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

BgeeiENSMUSG00000028274.
CleanExiMM_RNGTT.
ExpressionAtlasiO55236. baseline and differential.
GenevisibleiO55236. MM.

Family and domain databases

Gene3Di3.90.190.10. 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...

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: November 2, 2016
This is version 150 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.