CPLM-000075

Genbank Nucleotide ID

RNA 3'-terminal phosphate cyclase

Protein Synonyms/Alias

RNA cyclase; RNA-3'-phosphate cyclase; RNA terminal phosphate cyclase domain-containing protein 1; RTC domain-containing protein 1

RPC; RPC1; RTC1; RTCD1

Homo sapiens (Human)

Position	Peptide	Type	References
141	DYTVMVFKPIVEKFG	ubiquitination	[1, 2]
156	FIFNCDIKTRGYYPK	ubiquitination	[2, 3]
163	KTRGYYPKGGGEVIV	acetylation	[4, 5]
163	KTRGYYPKGGGEVIV	ubiquitination	[2, 5, 6]
176	IVRMSPVKQLNPINL	ubiquitination	[2, 6]
191	TERGCVTKIYGRAFV	ubiquitination	[2]
208	VLPFKVAKDMAAAAV	ubiquitination	[2]
272	KRGVNADKVGIEAAE	ubiquitination	[2]

[1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]

Functional Description

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.

NP_BIND 294 298 ATP (By similarity).
ACT_SITE 320 320 Tele-AMP-histidine intermediate (By
BINDING 104 104 ATP (By similarity).

Alternative splicing; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Nucleotide-binding; Nucleus; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005654; C:nucleoplasm; TAS:ProtInc.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0003723; F:RNA binding; TAS:ProtInc.
GO:0003963; F:RNA-3'-phosphate cyclase activity; TAS:ProtInc.
GO:0006396; P:RNA processing; IEA:InterPro.

IPR013791; 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.

PF01137; RTC
PF05189; RTC_insert