CMTR1_RAT
ID CMTR1_RAT Reviewed; 837 AA.
AC Q5U2Z5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1;
DE EC=2.1.1.57 {ECO:0000250|UniProtKB:Q8N1G2};
DE AltName: Full=Cap methyltransferase 1;
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1;
DE Short=MTr1;
DE AltName: Full=FtsJ methyltransferase domain-containing protein 2;
GN Name=Cmtr1; Synonyms=Ftsjd2;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Kidney;
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 [2]
RP IDENTIFICATION BY 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: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-
CC capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1).
CC Displays a preference for cap0 transcripts. Cap1 modification is linked
CC to higher levels of translation. May be involved in the interferon
CC response pathway. {ECO:0000250|UniProtKB:Q8N1G2}.
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(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000250|UniProtKB:Q8N1G2};
CC -!- SUBUNIT: Interacts with POLR2A (via C-terminus).
CC {ECO:0000250|UniProtKB:Q8N1G2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N1G2}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC085799; AAH85799.1; -; mRNA.
DR RefSeq; NP_001014053.1; NM_001014031.1.
DR AlphaFoldDB; Q5U2Z5; -.
DR SMR; Q5U2Z5; -.
DR STRING; 10116.ENSRNOP00000000640; -.
DR iPTMnet; Q5U2Z5; -.
DR PhosphoSitePlus; Q5U2Z5; -.
DR jPOST; Q5U2Z5; -.
DR PaxDb; Q5U2Z5; -.
DR PRIDE; Q5U2Z5; -.
DR Ensembl; ENSRNOT00000000640; ENSRNOP00000000640; ENSRNOG00000000532.
DR GeneID; 309656; -.
DR KEGG; rno:309656; -.
DR UCSC; RGD:1307801; rat.
DR CTD; 23070; -.
DR RGD; 1307801; Cmtr1.
DR eggNOG; KOG3673; Eukaryota.
DR GeneTree; ENSGT00940000157172; -.
DR HOGENOM; CLU_011097_0_0_1; -.
DR InParanoid; Q5U2Z5; -.
DR OrthoDB; 1336442at2759; -.
DR PRO; PR:Q5U2Z5; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000532; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q5U2Z5; baseline and differential.
DR Genevisible; Q5U2Z5; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
DR GO; GO:0097309; P:cap1 mRNA methylation; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR InterPro; IPR030376; Cap_mRNA_MeTrfase_1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR025816; RrmJ-type_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001202; WW_dom.
DR PANTHER; PTHR16121:SF0; PTHR16121:SF0; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS51613; SAM_MT_RRMJ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..837
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1"
FT /id="PRO_0000251242"
FT DOMAIN 86..132
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 230..449
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT DOMAIN 751..785
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..834
FT /note="Interaction with POLR2A"
FT /evidence="ECO:0000250"
FT MOTIF 2..18
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT ACT_SITE 363
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT ACT_SITE 403
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 202..206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 276..282
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 334..335
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 373..375
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC3"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC3"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT MOD_RES 107
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
SQ SEQUENCE 837 AA; 95619 MW; 443BFE2882E687CA CRC64;
MKRRTDPECT APLKKQKRIG ELARHLSSTS DDEPLSSVSH AAKASTTSLS GSDSETEGKQ
PCSDGFKDAF KADSLVEGTS SRYSMYNSVS QKLMAKMGFR EGEGLGKYSQ GRKDIVETSN
QKGRRGLGLT LQGFDQELNV DWRDEPEPNA CEQVSWFPEC TTEIPDSREM SDWMVVGKRK
MVIEDETEFC GEELLHSMLK CKSVFDILDG EEMRRARTRA NPYEMIRGVF FLNRAAMKMA
NMDFVFDRMF TNPLDSSGKP LLKESDIDLL YFADVCAGPG GFSEYVLWRR KWHAKGFGMT
LKGPNDFKLE DFYSASSELF EPYYGEGGVD GDGDITRPEN INAFRNFVLD NTDRKGVHFV
MADGGFSVEG QENLQEILSK QLLLCQFLMA LSVVRTGGHF VCKTFDLFTP FSVGLIYLLY
CCFERVCLFK PVTSRPANSE RYVVCKGLKV GIDDVREYLF SVNIQLNQLR NTDSDVNLVV
PLSVIKGDHE FNDYMIRSNE SYCSLQIKAL AKIHAFVQDT TLSEPRQAEI RKECLQLWEI
PDRARVAPSP SDPKFKFFEL IKDTDINIFS YKPTLLTAKT LEKIRPVLEY RCMVSGSEQK
FLLGLGKSQI YTWDGRQSDR WVKLDLKTEL PRDTLLCVEI VHELKGEGKA QRKISAIHIL
DVLVLNGSDV REQHFNQRIQ LAEKFVKAVS KPSRPDMNPI RVKEVYRLEE MEKIFVRLEM
KLIKGSGGTP KLSYTGRDDR HFVPTGVYIV RTVTEPWTMA FSKGWKKKFF YNKKTGESFF
TLPPESIAPF HTCYYTRLFW EWGDGFHMRD SQKPQDPDKL SKEDVLSFIQ SHNPLGP
