Polynucleotide 5'-triphosphatase
     (mRNA 5'-triphosphatase)
     (TPase)
     (EC 3.1.3.33)
mRNA guanylyltransferase
     (EC 2.7.7.50)
     (GTP--RNA guanylyltransferase)
     (GTase)

Gene name

	Name:	Rngtt
	Synonyms:	Cap1a

From

Mus musculus (Mouse)

[TaxID: 10090]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF LYS-294. DOI=10.1073/pnas.94.24.12898; PubMed=9371772 [NCBI, ExPASy, EBI, Israel, Japan] Yue Z., Maldonado E., Pillutla R., Cho H., Reinberg D., Shatkin A.J.; "Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II."; Proc. Natl. Acad. Sci. U.S.A. 94:12898-12903(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=9407024 [NCBI, ExPASy, EBI, Israel, Japan] McCracken S., Fong N., Rosonina E., Yankulov K., Brothers G., Siderovski D., Hessel A., Foster S., Shuman S., Bentley D.L.; "5'-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II."; Genes Dev. 11:3306-3318(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	CHARACTERIZATION, AND MUTAGENESIS. DOI=10.1073/pnas.95.21.12226; PubMed=9770468 [NCBI, ExPASy, EBI, Israel, Japan] Wen Y., Yue Z., Shatkin A.J.; "Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism."; Proc. Natl. Acad. Sci. U.S.A. 95:12226-12231(1998).
[5]	X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS). DOI=10.1093/emboj/20.10.2575; PubMed=11350947 [NCBI, ExPASy, EBI, Israel, Japan] Changela A., Ho C.K., Martins A., Shuman S., Mondragon A.; "Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme."; EMBO J. 20:2575-2586(2001).

Comments

FUNCTION: 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.
CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H₂O = a polynucleotide + phosphate.
CATALYTIC ACTIVITY: GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
ENZYME REGULATION: RNA triphosphatase activity is inhibited by vanadate, iodoacetate and magnesium.
SUBUNIT: Interacts with SUPT5H and RNMT (By similarity).
SUBCELLULAR LOCATION: Nucleus.
MISCELLANEOUS: Binds to the elongating phosphorylated form of RNA polymerase II. Can interact indirectly by binding to pol II C-terminal domain and directly by RNA binding. The GTase domain, rather than the TPase domain mediates these interactions.
SIMILARITY: In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family.
SIMILARITY: In the C-terminal section; belongs to the eukaryotic GTase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF025653; AAB91558.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF034568; AAB88903.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC043657; AAH43657.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_036014.1; -.

UniGene

Mm.240024

3D structure databases

PDB

1I9S; X-ray; 1.65 A; A=1-210.	[ExPASy / RCSB / EBI]
1I9T; X-ray; 1.70 A; A=1-210.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

1I9S; -.
1I9T; -.

PTM databases

O55236; -.

Organism-specific databases

MGI

MGI:1329041; Rngtt.

Gene expression databases

ArrayExpress

O55236; -.

CleanEx

MM_RNGTT; -.

GermOnline

ENSMUSG00000028274; Mus musculus.

Family and domain databases

InterPro

IPR017074; mRNA_cap_enz_bifunc.
IPR001339; mRNA_cap_enzyme.
IPR013846; mRNA_cap_enzyme_C.
IPR000387; Tyr_Pase.
IPR016130; Tyr_Pase_AS.
IPR000340; Tyr_Pase_dual_specific.
Graphical view of domain structure.

Pfam

PF00782; DSPc; 1.
PF03919; mRNA_cap_C; 1.
PF01331; mRNA_cap_enzyme; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036958; mRNA_capping_HCE; 1.

PROSITE

PS00383; TYR_PHOSPHATASE_1; 1.
PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

O55236.

Genome annotation databases

Ensembl

ENSMUSG00000028274; Mus musculus. [Contig view]

GeneID

24018; -.

KEGG

mmu:24018; -.

Phylogenomic databases

HOGENOM

O55236; -.

HOVERGEN

O55236; -.

Other

Rngtt; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotidyltransferase; Nucleus; Phosphoprotein; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 597`	`597`	`mRNA-capping enzyme.`	`PRO_0000210109`
`REGION`	`1 212`	`212`	`TPase.`
`REGION`	`229 597`	`369`	`GTase.`
`COMPBIAS`	`195 205`	`11`	`Asp/Glu-rich.`
`ACT_SITE`	`126 126`		`For RNA 5'-triphosphatase activity (By similarity).`
`ACT_SITE`	`294 294`		`N6-GMP-lysine intermediate.`
`MOD_RES`	`210 210`		`Phosphoserine (By similarity).`
`MUTAGEN`	`36 36`		`D->A: No effect.`
`MUTAGEN`	`66 66`		`D->A: Decrease of >90% of TPase activity.`
`MUTAGEN`	`110 110`		`C->S: No effect.`
`MUTAGEN`	`125 125`		`H->A: Decrease of 55-60% of TPase activity.`
`MUTAGEN`	`126 126`		`C->S: Loss of TPase activity.`
`MUTAGEN`	`132 132`		`R->A: Loss of TPase activity.`
`MUTAGEN`	`133 133`		`T->A: Decrease of 55-60% of TPase activity.`
`MUTAGEN`	`138 138`		`C->S: No effect.`
`MUTAGEN`	`168 168`		`D->A: No effect.`
`MUTAGEN`	`290 290`		`K->A: No effect.`
`MUTAGEN`	`294 294`		`K->A: Loss of GTase activity.`
`MUTAGEN`	`315 315`		`R->A: Almost complete loss of RNA-binding and loss of GTase activity.`
`MUTAGEN`	`315 315`		`R->K: At least 60% of RNA-binding activity and loss of GTase activity.`
`MUTAGEN`	`530 530`		`R->A: Almost complete loss of RNA-binding and loss of GTase activity.`
`MUTAGEN`	`530 530`		`R->K: Loss of GTase activity.`
`MUTAGEN`	`533 533`		`K->A: Almost complete loss of RNA-binding and loss of GTase activity.`
`MUTAGEN`	`533 533`		`K->R: At least 60% of RNA-binding activity and loss of GTase activity.`
`MUTAGEN`	`537 537`		`N->A: Almost complete loss of RNA-binding and loss of GTase activity.`
`MUTAGEN`	`537 537`		`N->Q: At least 60% of RNA binding activity and loss of GTase activity.`
`TURN`	`21 23`	`3`
`STRAND`	`24 27`	`4`
`HELIX`	`33 35`	`3`
`TURN`	`36 38`	`3`
`HELIX`	`41 43`	`3`
`HELIX`	`47 56`	`10`
`STRAND`	`61 66`	`6`
`STRAND`	`71 74`	`4`
`HELIX`	`77 80`	`4`
`TURN`	`81 83`	`3`
`STRAND`	`85 88`	`4`
`HELIX`	`100 110`	`11`
`STRAND`	`121 125`	`5`
`STRAND`	`127 130`	`4`
`HELIX`	`131 145`	`15`
`HELIX`	`149 159`	`11`
`HELIX`	`167 177`	`11`
`HELIX`	`180 182`	`3`
`HELIX`	`191 194`	`4`

Sequence information

Length: 597 AA [This is the length of the unprocessed precursor]

Molecular weight: 68684 Da [This is the MW of the unprocessed precursor]

CRC64: B2A9E711889D8EA7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAYNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK 

        70         80         90        100        110        120 
MSLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERSPPE 

       130        140        150        160        170        180 
LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI 

       190        200        210        220        230        240 
EEAPPPPVLP DWCFEDEDEE DEDEDGKKDS EPGSSASFSK RRKERLKLGA IFLEGITVKG 

       250        260        270        280        290        300 
VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IRLLEQKPYK VSWKADGTRY 

       310        320        330        340        350        360 
MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDK VNGQAVPRYL 

       370        380        390        400        410        420 
IYDIIKFNAQ PVGDCDFNIR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RPKQFFDINI 

       430        440        450        460        470        480 
SRKLLEGNFA KEVSHEMDGL IFQPIGKYKP GRCDDILKWK PPSLNSVDFR LKITRMGGEG 

       490        500        510        520        530        540 
LLPQNVGLLY VGGYERPFAQ IKVTKELKQY DNKIIECKFE NNSWVFMRQR IDKSFPNAYN 

       550        560        570        580        590 
TAMAVCNSIS NPVTKEMLFE FIDRCAAAAQ GQKRKYPLDP DTELMPPPPP KRLHRPT

O55236 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools