RTCA_HUMAN
ID RTCA_HUMAN Reviewed; 366 AA.
AC O00442; Q5VVL5; Q5VVL6; Q96E99;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=RNA 3'-terminal phosphate cyclase;
DE Short=RNA cyclase;
DE Short=RNA-3'-phosphate cyclase;
DE EC=6.5.1.4 {ECO:0000269|PubMed:9184239};
DE AltName: Full=RNA terminal phosphate cyclase domain-containing protein 1;
DE Short=RTC domain-containing protein 1;
GN Name=RTCA; Synonyms=RPC, RPC1, RTC1, RTCD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), PARTIAL PROTEIN
RP SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Blood;
RX PubMed=9184239; DOI=10.1093/emboj/16.10.2955;
RA Genschik P., Billy E., Swianiewicz M., Filipowicz W.;
RT "The human RNA 3'-terminal phosphate cyclase is a member of a new family of
RT proteins conserved in Eucarya, Bacteria and Archaea.";
RL EMBO J. 16:2955-2967(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CHARACTERIZATION.
RX PubMed=2199762; DOI=10.1016/0076-6879(90)81147-m;
RA Filipowicz W., Vincente O.;
RT "RNA 3'-terminal phosphate cyclase from HeLa cells.";
RL Methods Enzymol. 181:499-510(1990).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic
CC phosphodiester at the end of RNA. The mechanism of action of the enzyme
CC occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer
CC of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of
CC the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to
CC produce the cyclic end product. The biological role of this enzyme is
CC unknown but it is likely to function in some aspects of cellular RNA
CC processing. {ECO:0000269|PubMed:9184239}.
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:0000269|PubMed:9184239};
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC O00442-2; P32243-2: OTX2; NbExp=3; IntAct=EBI-12886464, EBI-9087860;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:9184239}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00442-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00442-2; Sequence=VSP_005915;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; Y11651; CAA72364.1; -; mRNA.
DR EMBL; Y11652; CAA72365.1; -; Genomic_DNA.
DR EMBL; AL445928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL663111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW72961.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72962.1; -; Genomic_DNA.
DR EMBL; BC012604; AAH12604.1; -; mRNA.
DR CCDS; CCDS44178.1; -. [O00442-2]
DR CCDS; CCDS768.1; -. [O00442-1]
DR PIR; T48844; T48844.
DR RefSeq; NP_001124313.1; NM_001130841.1. [O00442-2]
DR RefSeq; NP_003720.1; NM_003729.3. [O00442-1]
DR AlphaFoldDB; O00442; -.
DR SMR; O00442; -.
DR BioGRID; 114187; 127.
DR IntAct; O00442; 15.
DR MINT; O00442; -.
DR STRING; 9606.ENSP00000260563; -.
DR iPTMnet; O00442; -.
DR MetOSite; O00442; -.
DR PhosphoSitePlus; O00442; -.
DR BioMuta; RTCA; -.
DR EPD; O00442; -.
DR jPOST; O00442; -.
DR MassIVE; O00442; -.
DR MaxQB; O00442; -.
DR PaxDb; O00442; -.
DR PeptideAtlas; O00442; -.
DR PRIDE; O00442; -.
DR ProteomicsDB; 47890; -. [O00442-1]
DR ProteomicsDB; 47891; -. [O00442-2]
DR Antibodypedia; 33694; 147 antibodies from 26 providers.
DR DNASU; 8634; -.
DR Ensembl; ENST00000260563.4; ENSP00000260563.4; ENSG00000137996.13. [O00442-2]
DR Ensembl; ENST00000370128.9; ENSP00000359146.4; ENSG00000137996.13. [O00442-1]
DR GeneID; 8634; -.
DR KEGG; hsa:8634; -.
DR MANE-Select; ENST00000370128.9; ENSP00000359146.4; NM_003729.4; NP_003720.1.
DR UCSC; uc001dtc.4; human. [O00442-1]
DR CTD; 8634; -.
DR DisGeNET; 8634; -.
DR GeneCards; RTCA; -.
DR HGNC; HGNC:17981; RTCA.
DR HPA; ENSG00000137996; Low tissue specificity.
DR MIM; 611286; gene.
DR neXtProt; NX_O00442; -.
DR OpenTargets; ENSG00000137996; -.
DR PharmGKB; PA34877; -.
DR VEuPathDB; HostDB:ENSG00000137996; -.
DR eggNOG; KOG3980; Eukaryota.
DR GeneTree; ENSGT00530000063404; -.
DR HOGENOM; CLU_027882_0_1_1; -.
DR OMA; PKPGLSH; -.
DR OrthoDB; 1151685at2759; -.
DR PhylomeDB; O00442; -.
DR TreeFam; TF300831; -.
DR BRENDA; 6.5.1.4; 2681.
DR PathwayCommons; O00442; -.
DR SignaLink; O00442; -.
DR BioGRID-ORCS; 8634; 6 hits in 1084 CRISPR screens.
DR ChiTaRS; RTCA; human.
DR GenomeRNAi; 8634; -.
DR Pharos; O00442; Tbio.
DR PRO; PR:O00442; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00442; protein.
DR Bgee; ENSG00000137996; Expressed in jejunal mucosa and 205 other tissues.
DR ExpressionAtlas; O00442; baseline and differential.
DR Genevisible; O00442; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003963; F:RNA-3'-phosphate cyclase activity; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.30.360.20; -; 1.
DR Gene3D; 3.65.10.20; -; 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 PANTHER; PTHR11096; PTHR11096; 1.
DR PANTHER; PTHR11096:SF0; PTHR11096:SF0; 1.
DR Pfam; PF01137; RTC; 1.
DR Pfam; PF05189; RTC_insert; 1.
DR PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1.
DR SUPFAM; SSF52913; SSF52913; 1.
DR SUPFAM; SSF55205; SSF55205; 2.
DR TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR PROSITE; PS01287; RTC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..366
FT /note="RNA 3'-terminal phosphate cyclase"
FT /id="PRO_0000156410"
FT ACT_SITE 320
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 294..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 48
FT /note="L -> LSSGGWKSKIKVLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005915"
FT CONFLICT 34
FT /note="L -> S (in Ref. 4; AAH12604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 39337 MW; D129E680FF08BAD1 CRC64;
MAGPRVEVDG SIMEGGGQIL RVSTALSCLL GLPLRVQKIR AGRSTPGLRP QHLSGLEMIR
DLCDGQLEGA EIGSTEITFT PEKIKGGIHT ADTKTAGSVC LLMQVSMPCV LFAASPSELH
LKGGTNAEMA PQIDYTVMVF KPIVEKFGFI FNCDIKTRGY YPKGGGEVIV RMSPVKQLNP
INLTERGCVT KIYGRAFVAG VLPFKVAKDM AAAAVRCIRK EIRDLYVNIQ PVQEPKDQAF
GNGNGIIIIA ETSTGCLFAG SSLGKRGVNA DKVGIEAAEM LLANLRHGGT VDEYLQDQLI
VFMALANGVS RIKTGPVTLH TQTAIHFAEQ IAKAKFIVKK SEDEEDAAKD TYIIECQGIG
MTNPNL
