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Reviewed, UniProtKB/Swiss-Prot Q9D7H3 (RTC1_MOUSE)

Last modified February 9, 2010. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    RNA 3'-terminal phosphate cyclase
      Short name=RNA-3'-phosphate cyclase
      Short name=RNA cyclase
    EC=6.5.1.4
Alternative name(s):
    RNA terminal phosphate cyclase domain-containing protein 1
Gene names
Name: Rtcd1
Synonyms: Rpc1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) the enzyme acts on RNA-N3'P to produce RNA-N3'PP5'A; (C) a non catalytic nucleophilic attack by the adjacent 2'hydroxyl on the phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing By similarity.

Catalytic activity

ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate.

Subunit structure

Monomer By similarity.

Subcellular location

Nucleusnucleoplasm By similarity.

Sequence similarities

Belongs to the RNA 3'-terminal cyclase family. Type 1 subfamily.

Ontologies

Keywords
   Cellular componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Gene Ontology (GO)
   Biological processRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-3'-phosphate cyclase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 366366RNA 3'-terminal phosphate cyclase
PRO_0000156411

Sites

Active site3201 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9D7H3-1 [UniParc].

Last modified April 27, 2001. Version 1.
Checksum: 6829D420AB90DED3

FASTA36639,226
        10         20         30         40         50         60 
MEGQRVEVDG GIMEGGGQIL RVSTALSCLL GLPLRVQKIR AGRSTPGLRP QHLSGLEMVR 

        70         80         90        100        110        120 
DLCGGHLEGA EIGSTEITFT PEKIRGGVHT ADTKTAGSVC LLMQVSMPCV LFAASPSELR 

       130        140        150        160        170        180 
LKGGTNAEMA PQIDYTMMVF KPIAEKFGFT FNCDIKTRGY YPKGGGEVIV RVSPVKRLDP 

       190        200        210        220        230        240 
INLTDRGSVT KIYGRAFVAG VLPLKVAKDM AAAAVRCIRK EIRDLYVSIQ PVQEARDQAF 

       250        260        270        280        290        300 
GNGSGIIIVA ETSTGCLFAG SSLGKRGVNA DKAGIEAAEM LLANLRHGGT VDEYLQDQLI 

       310        320        330        340        350        360 
IFMALANGIS RIKTGSVTLH TQTAIHFAEQ LAKAKFTVKK SEEEEDATKD TYVIECEGIG 


MANPHL 

« Hide

References

[1]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Tongue.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK009245 mRNA. Translation: BAB26164.1.
IPIIPI00110315.
UniGeneMm.251228

3D structure databases

SMRQ9D7H3. Positions 6-340.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9D7H3.

2-D gel databases

REPRODUCTION-2DPAGEQ9D7H3.

Proteomic databases

PRIDEQ9D7H3.

Genome annotation databases

EnsemblENSMUST00000000348; ENSMUSP00000000348; ENSMUSG00000000339; Mus musculus. [Genome view]
UCSCuc008rcd.1. mouse.

Organism-specific databases

MGIMGI:1913618. Rtcd1.

Phylogenomic databases

HOGENOMHBG683539.
HOVERGENQ9D7H3.
InParanoidQ9D7H3.
PhylomeDBQ9D7H3.

Enzyme and pathway databases

BRENDA6.5.1.4. 244.

Gene expression databases

ArrayExpressQ9D7H3.
BgeeQ9D7H3.
CleanExMM_RTCD1.
GenevestigatorQ9D7H3.
GermOnlineENSMUSG00000000339. Mus musculus.

Family and domain databases

InterProIPR013791. RNA3'-term_phos_cycl_insert.
IPR000228. RNA3'_term_phos_cycl-like.
IPR020719. RNA3'_term_phos_cycl-like_CS.
IPR016443. RNA3'_term_phos_cycl-like_euk.
IPR013796. RNA3'_term_phos_cycl_insert.
IPR017770. RNA3'_term_phos_cycl_sub.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]
Gene3DG3DSA:3.65.10.20. RNA3'_term_phos_cycl. 1 hit.
PANTHERPTHR11096. RNA3'_term_phos_cycl. 1 hit.
PfamPF01137. RTC. 1 hit.
PF05189. RTC_insert. 1 hit.
[Graphical view]
PIRSFPIRSF005378. RNA3'_term_phos_cycl_euk. 1 hit.
TIGRFAMsTIGR03399. RNA_3prim_cycl. 1 hit.
PROSITEPS01287. RTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio321465.
PMAP-CutDBQ9D7H3.
SOURCESearch...

Entry information

Entry nameRTC1_MOUSE
AccessionPrimary (citable) accession number: Q9D7H3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: February 9, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents