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O00442 (RTCA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
RNA 3'-terminal phosphate cyclase

Short name=RNA cyclase
Short name=RNA-3'-phosphate cyclase
EC=6.5.1.4
Alternative name(s):
RNA terminal phosphate cyclase domain-containing protein 1
Short name=RTC domain-containing protein 1
Gene names
Name:RTCA
Synonyms:RPC, RPC1, RTC1, RTCD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-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.

Catalytic activity

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

Subunit structure

Monomer.

Subcellular location

Nucleusnucleoplasm.

Tissue specificity

Ubiquitous.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleoplasm

Traceable author statement Ref.1. Source: ProtInc

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Traceable author statement Ref.1. Source: ProtInc

RNA-3'-phosphate cyclase activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00442-1)

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: O00442-2)

The sequence of this isoform differs from the canonical sequence as follows:
     48-48: L → LSSGGWKSKIKVLT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 366366RNA 3'-terminal phosphate cyclase
PRO_0000156410

Regions

Nucleotide binding294 – 2985ATP By similarity

Sites

Active site3201Tele-AMP-histidine intermediate By similarity
Binding site1041ATP By similarity

Natural variations

Alternative sequence481L → LSSGGWKSKIKVLT in isoform 2.
VSP_005915

Experimental info

Sequence conflict341L → S in AAH12604. Ref.4

Sequences

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

Last modified July 1, 1997. Version 1.
Checksum: D129E680FF08BAD1

FASTA36639,337
        10         20         30         40         50         60 
MAGPRVEVDG SIMEGGGQIL RVSTALSCLL GLPLRVQKIR AGRSTPGLRP QHLSGLEMIR 

        70         80         90        100        110        120 
DLCDGQLEGA EIGSTEITFT PEKIKGGIHT ADTKTAGSVC LLMQVSMPCV LFAASPSELH 

       130        140        150        160        170        180 
LKGGTNAEMA PQIDYTVMVF KPIVEKFGFI FNCDIKTRGY YPKGGGEVIV RMSPVKQLNP 

       190        200        210        220        230        240 
INLTERGCVT KIYGRAFVAG VLPFKVAKDM AAAAVRCIRK EIRDLYVNIQ PVQEPKDQAF 

       250        260        270        280        290        300 
GNGNGIIIIA ETSTGCLFAG SSLGKRGVNA DKVGIEAAEM LLANLRHGGT VDEYLQDQLI 

       310        320        330        340        350        360 
VFMALANGVS RIKTGPVTLH TQTAIHFAEQ IAKAKFIVKK SEDEEDAAKD TYIIECQGIG 


MTNPNL 

« Hide

Isoform 2 [UniParc].

Checksum: 1AD20D4CDDF4D0E6
Show »

FASTA37940,709

References

« Hide 'large scale' references
[1]"The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea."
Genschik P., Billy E., Swianiewicz M., Filipowicz W.
EMBO J. 16:2955-2967(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
Tissue: Blood.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 2).
Tissue: Brain.
[5]"RNA 3'-terminal phosphate cyclase from HeLa cells."
Filipowicz W., Vincente O.
Methods Enzymol. 181:499-510(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11651 mRNA. Translation: CAA72364.1.
Y11652 Genomic DNA. Translation: CAA72365.1.
AL445928, AL663111 Genomic DNA. Translation: CAH72259.1.
AL445928, AL663111 Genomic DNA. Translation: CAH72260.1.
AL663111, AL445928 Genomic DNA. Translation: CAH73852.1.
AL663111, AL445928 Genomic DNA. Translation: CAH73853.1.
CH471097 Genomic DNA. Translation: EAW72961.1.
CH471097 Genomic DNA. Translation: EAW72962.1.
BC012604 mRNA. Translation: AAH12604.1.
CCDSCCDS44178.1. [O00442-2]
CCDS768.1. [O00442-1]
PIRT48844.
RefSeqNP_001124313.1. NM_001130841.1. [O00442-2]
NP_003720.1. NM_003729.3. [O00442-1]
UniGeneHs.484222.

3D structure databases

ProteinModelPortalO00442.
SMRO00442. Positions 6-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114187. 11 interactions.
IntActO00442. 1 interaction.
STRING9606.ENSP00000260563.

PTM databases

PhosphoSiteO00442.

Proteomic databases

MaxQBO00442.
PaxDbO00442.
PRIDEO00442.

Protocols and materials databases

DNASU8634.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260563; ENSP00000260563; ENSG00000137996. [O00442-2]
ENST00000370128; ENSP00000359146; ENSG00000137996. [O00442-1]
GeneID8634.
KEGGhsa:8634.
UCSCuc001dtc.3. human. [O00442-1]
uc001dtd.3. human. [O00442-2]

Organism-specific databases

CTD8634.
GeneCardsGC01P100732.
HGNCHGNC:17981. RTCA.
HPAHPA027982.
HPA028151.
MIM611286. gene.
neXtProtNX_O00442.
PharmGKBPA34877.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0430.
HOGENOMHOG000015264.
HOVERGENHBG017761.
KOK01974.
OMAAEMLLRN.
OrthoDBEOG780RMG.
PhylomeDBO00442.
TreeFamTF300831.

Gene expression databases

ArrayExpressO00442.
BgeeO00442.
CleanExHS_RTCD1.
GenevestigatorO00442.

Family and domain databases

Gene3D3.30.360.20. 1 hit.
3.65.10.20. 2 hits.
InterProIPR013791. RNA3'-term_phos_cycl_insert.
IPR023797. RNA3'_phos_cyclase_dom.
IPR000228. RNA3'_term_phos_cyc.
IPR017770. RNA3'_term_phos_cyc_type_1.
IPR020719. RNA3'_term_phos_cycl-like_CS.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]
PANTHERPTHR11096. PTHR11096. 1 hit.
PfamPF01137. RTC. 1 hit.
PF05189. RTC_insert. 1 hit.
[Graphical view]
SUPFAMSSF52913. SSF52913. 1 hit.
SSF55205. SSF55205. 2 hits.
TIGRFAMsTIGR03399. RNA_3prim_cycl. 1 hit.
PROSITEPS01287. RTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRTCA. human.
GenomeRNAi8634.
NextBio32367.
PMAP-CutDBO00442.
PROO00442.
SOURCESearch...

Entry information

Entry nameRTCA_HUMAN
AccessionPrimary (citable) accession number: O00442
Secondary accession number(s): Q5VVL5, Q5VVL6, Q96E99
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM