ID   RTCA_MOUSE              Reviewed;         366 AA.
AC   Q9D7H3; Q3TVV2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=RNA 3'-terminal phosphate cyclase {ECO:0000303|PubMed:25961792};
DE            Short=RNA cyclase {ECO:0000303|PubMed:25961792};
DE            Short=RNA-3'-phosphate cyclase {ECO:0000303|PubMed:25961792};
DE            EC=6.5.1.4 {ECO:0000250|UniProtKB:O00442};
DE   AltName: Full=RNA terminal phosphate cyclase domain-containing protein 1 {ECO:0000303|PubMed:25961792};
GN   Name=RtcA {ECO:0000303|PubMed:25961792, ECO:0000312|MGI:MGI:1913618};
GN   Synonyms=Rpc1, Rtcd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Pancreas, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=25961792; DOI=10.1038/nn.4019;
RA   Song Y., Sretavan D., Salegio E.A., Berg J., Huang X., Cheng T., Xiong X.,
RA   Meltzer S., Han C., Nguyen T.T., Bresnahan J.C., Beattie M.S., Jan L.Y.,
RA   Jan Y.N.;
RT   "Regulation of axon regeneration by the RNA repair and splicing pathway.";
RL   Nat. Neurosci. 18:817-825(2015).
CC   -!- FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic
CC       phosphodiester at the end of RNA (By similarity). The mechanism of
CC       action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme
CC       by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-
CC       N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-
CC       phosphorus in the diester linkage to produce the cyclic end product (By
CC       similarity). Likely functions in some aspects of cellular RNA
CC       processing (PubMed:25961792). Function plays an important role in
CC       regulating axon regeneration by inhibiting central nervous system (CNS)
CC       axon regeneration following optic nerve injury (PubMed:25961792).
CC       {ECO:0000250|UniProtKB:O00442, ECO:0000269|PubMed:25961792}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-
CC         cyclophospho-ribonucleotide-RNA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23976, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:10464,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83062,
CC         ChEBI:CHEBI:83064, ChEBI:CHEBI:456215; EC=6.5.1.4;
CC         Evidence={ECO:0000250|UniProtKB:O00442};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:O00442}.
CC   -!- TISSUE SPECIFICITY: Detected in retinal ganglion cells (RGCs) (at
CC       protein level). {ECO:0000269|PubMed:25961792}.
CC   -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AK009245; BAB26164.1; -; mRNA.
DR   EMBL; AK152129; BAE30970.1; -; mRNA.
DR   EMBL; AK159961; BAE35516.1; -; mRNA.
DR   EMBL; CH466532; EDL12384.1; -; Genomic_DNA.
DR   CCDS; CCDS17786.1; -.
DR   RefSeq; NP_079793.2; NM_025517.3.
DR   AlphaFoldDB; Q9D7H3; -.
DR   SMR; Q9D7H3; -.
DR   BioGRID; 211419; 3.
DR   STRING; 10090.ENSMUSP00000000348; -.
DR   iPTMnet; Q9D7H3; -.
DR   PhosphoSitePlus; Q9D7H3; -.
DR   SwissPalm; Q9D7H3; -.
DR   REPRODUCTION-2DPAGE; Q9D7H3; -.
DR   EPD; Q9D7H3; -.
DR   jPOST; Q9D7H3; -.
DR   MaxQB; Q9D7H3; -.
DR   PaxDb; 10090-ENSMUSP00000000348; -.
DR   ProteomicsDB; 260944; -.
DR   Pumba; Q9D7H3; -.
DR   Antibodypedia; 33694; 168 antibodies from 26 providers.
DR   DNASU; 66368; -.
DR   Ensembl; ENSMUST00000000348.15; ENSMUSP00000000348.9; ENSMUSG00000000339.15.
DR   GeneID; 66368; -.
DR   KEGG; mmu:66368; -.
DR   UCSC; uc008rcd.2; mouse.
DR   AGR; MGI:1913618; -.
DR   CTD; 8634; -.
DR   MGI; MGI:1913618; Rtca.
DR   VEuPathDB; HostDB:ENSMUSG00000000339; -.
DR   eggNOG; KOG3980; Eukaryota.
DR   GeneTree; ENSGT00530000063404; -.
DR   HOGENOM; CLU_027882_0_1_1; -.
DR   InParanoid; Q9D7H3; -.
DR   OMA; WSPPIDY; -.
DR   OrthoDB; 315241at2759; -.
DR   PhylomeDB; Q9D7H3; -.
DR   TreeFam; TF300831; -.
DR   BioGRID-ORCS; 66368; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Rtca; mouse.
DR   PRO; PR:Q9D7H3; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9D7H3; Protein.
DR   Bgee; ENSMUSG00000000339; Expressed in ear vesicle and 255 other cell types or tissues.
DR   ExpressionAtlas; Q9D7H3; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003963; F:RNA-3'-phosphate cyclase activity; ISS:UniProtKB.
DR   GO; GO:1905592; P:negative regulation of optical nerve axon regeneration; IMP:UniProtKB.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd00874; RNA_Cyclase_Class_II; 1.
DR   Gene3D; 3.65.10.20; RNA 3'-terminal phosphate cyclase domain; 1.
DR   Gene3D; 3.30.360.20; RNA 3'-terminal phosphate cyclase, insert domain; 1.
DR   HAMAP; MF_00200; RTC; 1.
DR   InterPro; IPR013791; RNA3'-term_phos_cycl_insert.
DR   InterPro; IPR023797; RNA3'_phos_cyclase_dom.
DR   InterPro; IPR037136; RNA3'_phos_cyclase_dom_sf.
DR   InterPro; IPR000228; RNA3'_term_phos_cyc.
DR   InterPro; IPR017770; RNA3'_term_phos_cyc_type_1.
DR   InterPro; IPR020719; RNA3'_term_phos_cycl-like_CS.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR036553; RPTC_insert.
DR   NCBIfam; TIGR03399; RNA_3prim_cycl; 1.
DR   PANTHER; PTHR11096; RNA 3' TERMINAL PHOSPHATE CYCLASE; 1.
DR   PANTHER; PTHR11096:SF0; RNA 3'-TERMINAL PHOSPHATE CYCLASE; 1.
DR   Pfam; PF01137; RTC; 1.
DR   Pfam; PF05189; RTC_insert; 1.
DR   PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 2.
DR   SUPFAM; SSF52913; RNA 3'-terminal phosphate cyclase, RPTC, insert domain; 1.
DR   PROSITE; PS01287; RTC; 1.
DR   Genevisible; Q9D7H3; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..366
FT                   /note="RNA 3'-terminal phosphate cyclase"
FT                   /id="PRO_0000156411"
FT   ACT_SITE        320
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         294
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   CONFLICT        273
FT                   /note="V -> A (in Ref. 1; BAB26164)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   366 AA;  39254 MW;  28C7DADEBB86B9C5 CRC64;
     MEGQRVEVDG GIMEGGGQIL RVSTALSCLL GLPLRVQKIR AGRSTPGLRP QHLSGLEMVR
     DLCGGHLEGA EIGSTEITFT PEKIRGGVHT ADTKTAGSVC LLMQVSMPCV LFAASPSELR
     LKGGTNAEMA PQIDYTMMVF KPIAEKFGFT FNCDIKTRGY YPKGGGEVIV RVSPVKRLDP
     INLTDRGSVT KIYGRAFVAG VLPLKVAKDM AAAAVRCIRK EIRDLYVSIQ PVQEARDQAF
     GNGSGIIIVA ETSTGCLFAG SSLGKRGVNA DKVGIEAAEM LLANLRHGGT VDEYLQDQLI
     IFMALANGIS RIKTGSVTLH TQTAIHFAEQ LAKAKFTVKK SEEEEDATKD TYVIECEGIG
     MANPHL
//