CMTR2_MOUSE
ID CMTR2_MOUSE Reviewed; 767 AA.
AC Q8BWQ4; Q3TYT6; Q8R3E7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2;
DE EC=2.1.1.296 {ECO:0000250|UniProtKB:Q8IYT2};
DE AltName: Full=Cap methyltransferase 2;
DE AltName: Full=Cap2 2'O-ribose methyltransferase 2;
DE Short=MTr2;
DE AltName: Full=FtsJ methyltransferase domain-containing protein 1;
GN Name=Cmtr2; Synonyms=Ftsjd1;
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=Inner ear, and Liver;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of
CC mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-
CC capped mRNA and small nuclear RNA (snRNA) (cap0) to produce
CC m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently
CC of its N(7) methylation status. Display cap2 methylation on both cap0
CC and cap1. Displays a preference for cap1 RNAs.
CC {ECO:0000250|UniProtKB:Q8IYT2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC ribonucleoside)-(ribonucleotide) in mRNA + S-adenosyl-L-methionine =
CC a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC ribonucleoside)-(2'-O-methyl-ribonucleotide) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67024, Rhea:RHEA-COMP:17169,
CC Rhea:RHEA-COMP:17170, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:167612, ChEBI:CHEBI:167614;
CC EC=2.1.1.296; Evidence={ECO:0000250|UniProtKB:Q8IYT2};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IYT2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8IYT2}.
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; AK050315; BAC34184.1; -; mRNA.
DR EMBL; AK158368; BAE34476.1; -; mRNA.
DR EMBL; BC025546; AAH25546.1; -; mRNA.
DR CCDS; CCDS22662.1; -.
DR RefSeq; NP_666327.2; NM_146215.4.
DR RefSeq; XP_006530979.1; XM_006530916.2.
DR RefSeq; XP_006530980.1; XM_006530917.2.
DR AlphaFoldDB; Q8BWQ4; -.
DR SMR; Q8BWQ4; -.
DR STRING; 10090.ENSMUSP00000060558; -.
DR iPTMnet; Q8BWQ4; -.
DR PhosphoSitePlus; Q8BWQ4; -.
DR EPD; Q8BWQ4; -.
DR MaxQB; Q8BWQ4; -.
DR PaxDb; Q8BWQ4; -.
DR PeptideAtlas; Q8BWQ4; -.
DR PRIDE; Q8BWQ4; -.
DR ProteomicsDB; 285504; -.
DR Antibodypedia; 44554; 81 antibodies from 18 providers.
DR DNASU; 234728; -.
DR Ensembl; ENSMUST00000056972; ENSMUSP00000060558; ENSMUSG00000046441.
DR GeneID; 234728; -.
DR KEGG; mmu:234728; -.
DR UCSC; uc009nkp.2; mouse.
DR CTD; 55783; -.
DR MGI; MGI:2384580; Cmtr2.
DR VEuPathDB; HostDB:ENSMUSG00000046441; -.
DR eggNOG; KOG3674; Eukaryota.
DR GeneTree; ENSGT00940000161773; -.
DR HOGENOM; CLU_019427_0_0_1; -.
DR InParanoid; Q8BWQ4; -.
DR OMA; VSPLHYC; -.
DR OrthoDB; 1327262at2759; -.
DR PhylomeDB; Q8BWQ4; -.
DR TreeFam; TF314897; -.
DR BioGRID-ORCS; 234728; 21 hits in 74 CRISPR screens.
DR PRO; PR:Q8BWQ4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BWQ4; protein.
DR Bgee; ENSMUSG00000046441; Expressed in animal zygote and 217 other tissues.
DR ExpressionAtlas; Q8BWQ4; baseline and differential.
DR Genevisible; Q8BWQ4; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
DR GO; GO:0097309; P:cap1 mRNA methylation; IBA:GO_Central.
DR GO; GO:0097310; P:cap2 mRNA methylation; ISS:UniProtKB.
DR InterPro; IPR025807; Adrift-typ_MeTrfase.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51614; SAM_MT_ADRIFT; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..767
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 2"
FT /id="PRO_0000326181"
FT DOMAIN 109..322
FT /note="Adrift-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT ACT_SITE 117
FT /evidence="ECO:0000250|UniProtKB:Q8IYT2"
FT ACT_SITE 235
FT /evidence="ECO:0000250|UniProtKB:Q8IYT2"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT CONFLICT 108
FT /note="A -> T (in Ref. 2; AAH25546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 767 AA; 87143 MW; DB08D0490B89F22B CRC64;
MSKRRKLPAR QPACLETFSP DVLNDVSELF AKSFSYRKPL DNEWQLPAPT ESFSCGHLEF
RALLDLKNSL NEVKNLLSDK KLDEWHRHTA FTNKAGKIIS HVKKAVNAEL CTQAWCKFQE
ILCSFPLIPQ EAFQSGRLNS LHLCEAPGAF IASLNHYLKS HRFPCEWSWV ANSLNPYHEA
NDNLRMITDD RLMANTLHCW YFGPDNTGDI MTLKYLTGLQ DFLSGMSPIH LVTADGSFDC
QGNPGEQEAL VSSLHYCEAV TALITLGDGG SFVLKMFTLF EHCSVNLMYL LNCSFDQVHV
FKPATSKAGN SEVYVVCLRY KGREAVQPLL SRMVLNFGTE MTRKALFPHH VIPKSFLERH
EECCTFFHRY QLETISENIR LFESMGTGEQ ERLNNLRDCA VQYFMQKFQL KPLSRNHWLV
KKSNIGCSMN TKWFGQRNKY FKTYNERKMM ETLSWKDKVA KGYFNSWAEE HTVYHPGQNS
LLEGTASSLE YQSWQVLEGK KLPKVKCSPF CDGEILKTLN EAIEKSLGEA LSVDAKVSSK
QQYRCCPVFS EESVLSELLR LTKCLPDEQG AEPSGPVKCL LVGSPAVCDL QMPAPLEIQL
VESVELTAFS CSLLHDGDPA YQHLFLDCLL HSLRRLHRGD VMVLPILSCF TRFMAGLTFV
LHGCFRFITF SCPTSLEPLR TCAVLLCIGY QNLPDAVFQF LQNVHDLLSK LLHPSAPRQI
LQFLPMEALL QGTLLDFLWD LNAAIAKRHL HLIIQGERDQ AIGSLEL
