TGS1_RAT
ID TGS1_RAT Reviewed; 850 AA.
AC P85107;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Trimethylguanosine synthase;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q96RS0};
DE AltName: Full=Nuclear receptor coactivator 6-interacting protein;
DE AltName: Full=PRIP-interacting protein with methyltransferase motif;
DE Short=PIMT;
DE Short=PIPMT;
GN Name=Tgs1 {ECO:0000250|UniProtKB:Q96RS0};
GN Synonyms=Ncoa6ip {ECO:0000312|RGD:1309953},
GN Pimt {ECO:0000250|UniProtKB:Q96RS0};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=12943661; DOI=10.1016/s0006-291x(03)01514-6;
RA Enuenlue I., Papai G., Cserpan I., Udvardy A., Jeang K.-T., Boros I.;
RT "Different isoforms of PRIP-interacting protein with methyltransferase
RT domain/trimethylguanosine synthase localize to the cytoplasm and nucleus.";
RL Biochem. Biophys. Res. Commun. 309:44-51(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the 2 serial methylation steps for the conversion
CC of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a
CC 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is
CC specific for guanine, and N7 methylation must precede N2 methylation.
CC Hypermethylation of the m7G cap of U snRNAs leads to their
CC concentration in nuclear foci, their colocalization with coilin and the
CC formation of canonical Cajal bodies (CBs). Plays a role in
CC transcriptional regulation (By similarity).
CC {ECO:0000250|UniProtKB:Q96RS0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(7)-dimethyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67620, Rhea:RHEA-COMP:17167, Rhea:RHEA-
CC COMP:17315, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156461, ChEBI:CHEBI:172880;
CC Evidence={ECO:0000250|UniProtKB:Q96RS0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67621;
CC Evidence={ECO:0000250|UniProtKB:Q96RS0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-
CC ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end
CC (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-(ribonucleoside) in
CC mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67624,
CC Rhea:RHEA-COMP:17171, Rhea:RHEA-COMP:17315, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:167623,
CC ChEBI:CHEBI:172880; Evidence={ECO:0000250|UniProtKB:Q96RS0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67625;
CC Evidence={ECO:0000250|UniProtKB:Q96RS0};
CC -!- SUBUNIT: May form homooligomers. Interacts with CREBBP/CBP, EED/WAIT1,
CC EP300/P300, NCOA6/PRIP, PPARBP/PBP and SMN (By similarity).
CC {ECO:0000250|UniProtKB:Q96RS0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96RS0}.
CC Nucleus, Cajal body {ECO:0000250|UniProtKB:Q96RS0}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q96RS0}.
CC -!- TISSUE SPECIFICITY: A 55 kDa isoform is widely expressed while a 90 kDa
CC isoform is detected exclusively in brain and testis (at protein level).
CC {ECO:0000269|PubMed:12943661}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC Trimethylguanosine synthase family. {ECO:0000255}.
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DR EMBL; AABR03040398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001101374.1; NM_001107904.1.
DR AlphaFoldDB; P85107; -.
DR SMR; P85107; -.
DR STRING; 10116.ENSRNOP00000010783; -.
DR iPTMnet; P85107; -.
DR PhosphoSitePlus; P85107; -.
DR PaxDb; P85107; -.
DR Ensembl; ENSRNOT00000010783; ENSRNOP00000010783; ENSRNOG00000008156.
DR GeneID; 312947; -.
DR KEGG; rno:312947; -.
DR UCSC; RGD:1309953; rat.
DR CTD; 96764; -.
DR RGD; 1309953; Tgs1.
DR eggNOG; KOG2730; Eukaryota.
DR GeneTree; ENSGT00390000018056; -.
DR HOGENOM; CLU_016892_0_0_1; -.
DR InParanoid; P85107; -.
DR OMA; VNKPMDE; -.
DR OrthoDB; 176302at2759; -.
DR PhylomeDB; P85107; -.
DR TreeFam; TF313065; -.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR PRO; PR:P85107; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008156; Expressed in thymus and 19 other tissues.
DR Genevisible; P85107; RN.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0071164; F:RNA trimethylguanosine synthase activity; ISO:RGD.
DR GO; GO:0036261; P:7-methylguanosine cap hypermethylation; ISO:RGD.
DR GO; GO:0009452; P:7-methylguanosine RNA capping; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019012; RNA_cap_Gua-N2-MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF09445; Methyltransf_15; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..850
FT /note="Trimethylguanosine synthase"
FT /id="PRO_0000283727"
FT REGION 54..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 713
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12052"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RS0"
SQ SEQUENCE 850 AA; 96045 MW; 1C47E614F90382DD CRC64;
MCCEKWSHVA EMLLFIEDRE EEYKILCLCS RAFVEDRKLY NLGLKGYYVK SSGNNAGDRV
TEEEEDDHSS GTTESHSADE GDLDPEAKLM RSMGLPVRFG RMSTHGSFEV SMNARNKAKV
RQKRRKHRKQ YLDEIVREDW RNDCEEDDLV VSDDPSSVEH CENNSACEIQ SKTDAEAENL
PVENTLAPKL EVTENWEKYW NEYGEGLLWQ SWQEKYPDQT LSSEPWNLPD TKEEWEQHYS
QLYWYYLEQF QYWEAQGWTF VASQNCDKDV CTSHTQVDQN AESSLKADGT TLSSSPNTAE
DESLGSNDND HNEIIAGINK ITLSAEEVEQ SQLDSSEHCD KPLSEVTGKE CPASGGSDSC
HGTPKESDIS ENRSSDQPAQ ELQESSGTNT SKHRPHHNGT DGNESEDDPP DHKPSKMKRS
HELDIDENPD SEVDDNGFHL GFKHGSGQKY GGIPNFSRRQ VRYLEKNVKY KSKYLDMRKR
MTVKNKHIVF SEESGKPFIR KSKVRSKVEK FLKWVNEPVD EEISQEPLSH NKMQDTCTSS
DSEEQDMSME KTDGLMETRD PEPENCQTIS SASELEAEKS EGGSLVAAVP ENCSTEGVAN
SPRAEAEVEI KKKKKKKKKN KNKKINGLPP EIASVPELAK YWAQRYRLFS RFDDGIKLDK
EGWFSVTPEK IAEHIAGRVS QSFNCDIIVD AFCGVGGNTI QFALTGKRVI AIDIDPVKID
LARNNAEVYG VADKIEFICG DFLLLAPCLK ADVVFLSPPW GGPDYATAET FDIRTMMSPD
GFEIFRLSQK ITNNIVYFLP RNADVDQVAS LAGPGGQVEI EQNFLNNKLK TITAYFGDLI
RRPALRSAEA
