Full text data of RTCA
RTCA
(RPC, RPC1, RTC1, RTCD1)
[Confidence: low (only semi-automatic identification from reviews)]
RNA 3'-terminal phosphate cyclase; RNA cyclase; RNA-3'-phosphate cyclase; 6.5.1.4 (RNA terminal phosphate cyclase domain-containing protein 1; RTC domain-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
RNA 3'-terminal phosphate cyclase; RNA cyclase; RNA-3'-phosphate cyclase; 6.5.1.4 (RNA terminal phosphate cyclase domain-containing protein 1; RTC domain-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O00442
ID RTCA_HUMAN Reviewed; 366 AA.
AC O00442; Q5VVL5; Q5VVL6; Q96E99;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=RNA 3'-terminal phosphate cyclase;
DE Short=RNA cyclase;
DE Short=RNA-3'-phosphate cyclase;
DE EC=6.5.1.4;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND PARTIAL
RP PROTEIN SEQUENCE.
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
RT family of 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Buerckstuemmer T., 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'-
CC cyclic phosphodiester at the end of RNA. The mechanism of action
CC of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by
CC 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
CC product. The biological role of this enzyme is unknown but it is
CC likely to function in some aspects of cellular RNA processing.
CC -!- CATALYTIC ACTIVITY: ATP + RNA 3'-terminal-phosphate = AMP +
CC diphosphate + RNA terminal-2',3'-cyclic-phosphate.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Y11651; CAA72364.1; -; mRNA.
DR EMBL; Y11652; CAA72365.1; -; Genomic_DNA.
DR EMBL; AL445928; CAH72259.1; -; Genomic_DNA.
DR EMBL; AL663111; CAH72259.1; JOINED; Genomic_DNA.
DR EMBL; AL445928; CAH72260.1; -; Genomic_DNA.
DR EMBL; AL663111; CAH72260.1; JOINED; Genomic_DNA.
DR EMBL; AL663111; CAH73852.1; -; Genomic_DNA.
DR EMBL; AL445928; CAH73852.1; JOINED; Genomic_DNA.
DR EMBL; AL663111; CAH73853.1; -; Genomic_DNA.
DR EMBL; AL445928; CAH73853.1; JOINED; Genomic_DNA.
DR EMBL; CH471097; EAW72961.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72962.1; -; Genomic_DNA.
DR EMBL; BC012604; AAH12604.1; -; mRNA.
DR PIR; T48844; T48844.
DR RefSeq; NP_001124313.1; NM_001130841.1.
DR RefSeq; NP_003720.1; NM_003729.3.
DR UniGene; Hs.484222; -.
DR ProteinModelPortal; O00442; -.
DR SMR; O00442; 6-336.
DR IntAct; O00442; 1.
DR STRING; 9606.ENSP00000260563; -.
DR PhosphoSite; O00442; -.
DR PaxDb; O00442; -.
DR PRIDE; O00442; -.
DR DNASU; 8634; -.
DR Ensembl; ENST00000260563; ENSP00000260563; ENSG00000137996.
DR Ensembl; ENST00000370128; ENSP00000359146; ENSG00000137996.
DR GeneID; 8634; -.
DR KEGG; hsa:8634; -.
DR UCSC; uc001dtc.3; human.
DR CTD; 8634; -.
DR GeneCards; GC01P100732; -.
DR HGNC; HGNC:17981; RTCA.
DR HPA; HPA027982; -.
DR HPA; HPA028151; -.
DR MIM; 611286; gene.
DR neXtProt; NX_O00442; -.
DR PharmGKB; PA34877; -.
DR eggNOG; COG0430; -.
DR HOGENOM; HOG000015264; -.
DR HOVERGEN; HBG017761; -.
DR KO; K01974; -.
DR OMA; RRGHYPK; -.
DR OrthoDB; EOG780RMG; -.
DR ChiTaRS; RTCA; human.
DR GenomeRNAi; 8634; -.
DR NextBio; 32367; -.
DR PMAP-CutDB; O00442; -.
DR PRO; PR:O00442; -.
DR ArrayExpress; O00442; -.
DR Bgee; O00442; -.
DR CleanEx; HS_RTCD1; -.
DR Genevestigator; O00442; -.
DR GO; GO:0005654; C:nucleoplasm; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003963; F:RNA-3'-phosphate cyclase activity; TAS:ProtInc.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.30.360.20; -; 1.
DR Gene3D; 3.65.10.20; -; 2.
DR InterPro; IPR013791; RNA3'-term_phos_cycl_insert.
DR InterPro; IPR023797; RNA3'_phos_cyclase_dom.
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 PANTHER; PTHR11096; PTHR11096; 1.
DR Pfam; PF01137; RTC; 1.
DR Pfam; PF05189; RTC_insert; 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; Complete proteome;
KW Direct protein sequencing; Ligase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1 366 RNA 3'-terminal phosphate cyclase.
FT /FTId=PRO_0000156410.
FT NP_BIND 294 298 ATP (By similarity).
FT ACT_SITE 320 320 Tele-AMP-histidine intermediate (By
FT similarity).
FT BINDING 104 104 ATP (By similarity).
FT VAR_SEQ 48 48 L -> LSSGGWKSKIKVLT (in isoform 2).
FT /FTId=VSP_005915.
FT CONFLICT 34 34 L -> S (in Ref. 4; AAH12604).
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
//
ID RTCA_HUMAN Reviewed; 366 AA.
AC O00442; Q5VVL5; Q5VVL6; Q96E99;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=RNA 3'-terminal phosphate cyclase;
DE Short=RNA cyclase;
DE Short=RNA-3'-phosphate cyclase;
DE EC=6.5.1.4;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND PARTIAL
RP PROTEIN SEQUENCE.
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
RT family of 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Buerckstuemmer T., 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'-
CC cyclic phosphodiester at the end of RNA. The mechanism of action
CC of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by
CC 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
CC product. The biological role of this enzyme is unknown but it is
CC likely to function in some aspects of cellular RNA processing.
CC -!- CATALYTIC ACTIVITY: ATP + RNA 3'-terminal-phosphate = AMP +
CC diphosphate + RNA terminal-2',3'-cyclic-phosphate.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Y11651; CAA72364.1; -; mRNA.
DR EMBL; Y11652; CAA72365.1; -; Genomic_DNA.
DR EMBL; AL445928; CAH72259.1; -; Genomic_DNA.
DR EMBL; AL663111; CAH72259.1; JOINED; Genomic_DNA.
DR EMBL; AL445928; CAH72260.1; -; Genomic_DNA.
DR EMBL; AL663111; CAH72260.1; JOINED; Genomic_DNA.
DR EMBL; AL663111; CAH73852.1; -; Genomic_DNA.
DR EMBL; AL445928; CAH73852.1; JOINED; Genomic_DNA.
DR EMBL; AL663111; CAH73853.1; -; Genomic_DNA.
DR EMBL; AL445928; CAH73853.1; JOINED; Genomic_DNA.
DR EMBL; CH471097; EAW72961.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72962.1; -; Genomic_DNA.
DR EMBL; BC012604; AAH12604.1; -; mRNA.
DR PIR; T48844; T48844.
DR RefSeq; NP_001124313.1; NM_001130841.1.
DR RefSeq; NP_003720.1; NM_003729.3.
DR UniGene; Hs.484222; -.
DR ProteinModelPortal; O00442; -.
DR SMR; O00442; 6-336.
DR IntAct; O00442; 1.
DR STRING; 9606.ENSP00000260563; -.
DR PhosphoSite; O00442; -.
DR PaxDb; O00442; -.
DR PRIDE; O00442; -.
DR DNASU; 8634; -.
DR Ensembl; ENST00000260563; ENSP00000260563; ENSG00000137996.
DR Ensembl; ENST00000370128; ENSP00000359146; ENSG00000137996.
DR GeneID; 8634; -.
DR KEGG; hsa:8634; -.
DR UCSC; uc001dtc.3; human.
DR CTD; 8634; -.
DR GeneCards; GC01P100732; -.
DR HGNC; HGNC:17981; RTCA.
DR HPA; HPA027982; -.
DR HPA; HPA028151; -.
DR MIM; 611286; gene.
DR neXtProt; NX_O00442; -.
DR PharmGKB; PA34877; -.
DR eggNOG; COG0430; -.
DR HOGENOM; HOG000015264; -.
DR HOVERGEN; HBG017761; -.
DR KO; K01974; -.
DR OMA; RRGHYPK; -.
DR OrthoDB; EOG780RMG; -.
DR ChiTaRS; RTCA; human.
DR GenomeRNAi; 8634; -.
DR NextBio; 32367; -.
DR PMAP-CutDB; O00442; -.
DR PRO; PR:O00442; -.
DR ArrayExpress; O00442; -.
DR Bgee; O00442; -.
DR CleanEx; HS_RTCD1; -.
DR Genevestigator; O00442; -.
DR GO; GO:0005654; C:nucleoplasm; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003963; F:RNA-3'-phosphate cyclase activity; TAS:ProtInc.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.30.360.20; -; 1.
DR Gene3D; 3.65.10.20; -; 2.
DR InterPro; IPR013791; RNA3'-term_phos_cycl_insert.
DR InterPro; IPR023797; RNA3'_phos_cyclase_dom.
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 PANTHER; PTHR11096; PTHR11096; 1.
DR Pfam; PF01137; RTC; 1.
DR Pfam; PF05189; RTC_insert; 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; Complete proteome;
KW Direct protein sequencing; Ligase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1 366 RNA 3'-terminal phosphate cyclase.
FT /FTId=PRO_0000156410.
FT NP_BIND 294 298 ATP (By similarity).
FT ACT_SITE 320 320 Tele-AMP-histidine intermediate (By
FT similarity).
FT BINDING 104 104 ATP (By similarity).
FT VAR_SEQ 48 48 L -> LSSGGWKSKIKVLT (in isoform 2).
FT /FTId=VSP_005915.
FT CONFLICT 34 34 L -> S (in Ref. 4; AAH12604).
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
//
MIM
611286
*RECORD*
*FIELD* NO
611286
*FIELD* TI
*611286 RNA TERMINAL PHOSPHATE CYCLASE DOMAIN-CONTAINING PROTEIN 1; RTCD1
;;RTC DOMAIN-CONTAINING PROTEIN 1;;
read moreRNA 3-PRIME-TERMINAL PHOSPHATE CYCLASE: RPC
*FIELD* TX
DESCRIPTION
RNA 3-prime-terminal phosphate cyclase (RPC; EC 6.5.1.4) catalyzes the
ATP-dependent conversion of a 3-prime phosphate to a
2-prime,3-prime-cyclic phosphodiester at the end of RNA (Genschik et
al., 1997).
CLONING
Genschik et al. (1997) purified RPC from HeLa cells and obtained a
full-length RPC clone by PCR and screening a HeLa cell cDNA library. The
deduced 366-amino acid protein has a calculated molecular mass of 39.4
kD. Northern blot analysis detected ubiquitous expression of 1.8- and
3.0-kb transcripts in human tissues and cell lines, although the ratio
between the transcripts varied among tissues. Highest expression was in
skeletal muscle. Immunofluorescence analysis localized epitope-tagged
RPC primarily to the nucleus in HeLa cells and other mammalian cell
lines. RPC is conserved among eukaryotes, bacteria, and archaea.
GENE FUNCTION
Genschik et al. (1997) expressed recombinant human RPC in E. coli and
found that it underwent adenylation in the presence of radiolabeled ATP
and catalyzed cyclization of the 3-prime-terminal phosphate in different
RNA substrates. Comparison of RNA and DNA substrates with identical
sequences showed that the latter were 500-fold poorer substrates for
RPC. Genschik et al. (1997) stated that ATP is the best cofactor for
this reaction, but GTP, CTP, and UTP, but not dATP, can also act as
cofactors, although less efficiently.
GENE STRUCTURE
Genschik et al. (1997) determined that the upstream region of the RTCD1
gene is associated with a CpG island.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RTCD1
gene to chromosome 1 (TMAP SHGC-53265).
*FIELD* RF
1. Genschik, P.; Billy, E.; Swianiewicz, M.; Filipowicz, W.: The
human RNA 3-prime-terminal phosphate cyclase is a member of a new
family of proteins conserved in Eucarya, Bacteria, and Archaea. EMBO
J. 16: 2955-2967, 1997.
*FIELD* CD
Patricia A. Hartz: 8/2/2007
*FIELD* ED
mgross: 08/02/2007
*RECORD*
*FIELD* NO
611286
*FIELD* TI
*611286 RNA TERMINAL PHOSPHATE CYCLASE DOMAIN-CONTAINING PROTEIN 1; RTCD1
;;RTC DOMAIN-CONTAINING PROTEIN 1;;
read moreRNA 3-PRIME-TERMINAL PHOSPHATE CYCLASE: RPC
*FIELD* TX
DESCRIPTION
RNA 3-prime-terminal phosphate cyclase (RPC; EC 6.5.1.4) catalyzes the
ATP-dependent conversion of a 3-prime phosphate to a
2-prime,3-prime-cyclic phosphodiester at the end of RNA (Genschik et
al., 1997).
CLONING
Genschik et al. (1997) purified RPC from HeLa cells and obtained a
full-length RPC clone by PCR and screening a HeLa cell cDNA library. The
deduced 366-amino acid protein has a calculated molecular mass of 39.4
kD. Northern blot analysis detected ubiquitous expression of 1.8- and
3.0-kb transcripts in human tissues and cell lines, although the ratio
between the transcripts varied among tissues. Highest expression was in
skeletal muscle. Immunofluorescence analysis localized epitope-tagged
RPC primarily to the nucleus in HeLa cells and other mammalian cell
lines. RPC is conserved among eukaryotes, bacteria, and archaea.
GENE FUNCTION
Genschik et al. (1997) expressed recombinant human RPC in E. coli and
found that it underwent adenylation in the presence of radiolabeled ATP
and catalyzed cyclization of the 3-prime-terminal phosphate in different
RNA substrates. Comparison of RNA and DNA substrates with identical
sequences showed that the latter were 500-fold poorer substrates for
RPC. Genschik et al. (1997) stated that ATP is the best cofactor for
this reaction, but GTP, CTP, and UTP, but not dATP, can also act as
cofactors, although less efficiently.
GENE STRUCTURE
Genschik et al. (1997) determined that the upstream region of the RTCD1
gene is associated with a CpG island.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RTCD1
gene to chromosome 1 (TMAP SHGC-53265).
*FIELD* RF
1. Genschik, P.; Billy, E.; Swianiewicz, M.; Filipowicz, W.: The
human RNA 3-prime-terminal phosphate cyclase is a member of a new
family of proteins conserved in Eucarya, Bacteria, and Archaea. EMBO
J. 16: 2955-2967, 1997.
*FIELD* CD
Patricia A. Hartz: 8/2/2007
*FIELD* ED
mgross: 08/02/2007