BN3D2_MOUSE
ID BN3D2_MOUSE Reviewed; 285 AA.
AC Q91YP1; Q9D4U5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=RNA 5'-monophosphate methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q7Z5W3};
DE AltName: Full=BCDIN3 domain-containing protein;
GN Name=Bcdin3d {ECO:0000312|MGI:MGI:1922534};
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=Testis;
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: O-methyltransferase that specifically monomethylates 5'-
CC monophosphate of cytoplasmic histidyl tRNA (tRNA(His)), acting as a
CC capping enzyme by protecting tRNA(His) from cleavage by DICER1. Also
CC able, with less efficiently, to methylate the 5' monophosphate of a
CC subset of pre-miRNAs, acting as a negative regulator of miRNA
CC processing. The 5' monophosphate of pre-miRNAs is recognized by DICER1
CC and is required for pre-miRNAs processing: methylation at this position
CC reduces the processing of pre-miRNAs by DICER1. Was also reported to
CC mediate dimethylation of pre-miR-145; however dimethylation cannot be
CC reproduced by another group which observes a monomethylation of pre-
CC miR-145. {ECO:0000250|UniProtKB:Q7Z5W3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-phospho)-ribonucleoside-RNA + S-adenosyl-L-
CC methionine = a 5'-end (5'-methylphospho)-ribonucleoside-RNA + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:58656, Rhea:RHEA-COMP:15179,
CC Rhea:RHEA-COMP:15181, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:142776;
CC Evidence={ECO:0000250|UniProtKB:Q7Z5W3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-phospho)-ribonucleoside-RNA + 2 S-adenosyl-L-
CC methionine = a 5'-end (5'-bismethylphospho)-ribonucleoside-RNA + 2 S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:58640, Rhea:RHEA-COMP:15179,
CC Rhea:RHEA-COMP:15182, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:142777;
CC Evidence={ECO:0000250|UniProtKB:Q7Z5W3};
CC -!- SUBUNIT: Interacts with DICER1; the interaction may be mediated by RNA.
CC {ECO:0000250|UniProtKB:Q7Z5W3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7Z5W3}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AK016154; BAB30128.1; -; mRNA.
DR EMBL; BC016225; AAH16225.1; -; mRNA.
DR CCDS; CCDS37202.1; -.
DR RefSeq; NP_083512.2; NM_029236.2.
DR AlphaFoldDB; Q91YP1; -.
DR SMR; Q91YP1; -.
DR STRING; 10090.ENSMUSP00000041809; -.
DR PhosphoSitePlus; Q91YP1; -.
DR EPD; Q91YP1; -.
DR MaxQB; Q91YP1; -.
DR PaxDb; Q91YP1; -.
DR PRIDE; Q91YP1; -.
DR ProteomicsDB; 265449; -.
DR Antibodypedia; 49296; 48 antibodies from 14 providers.
DR DNASU; 75284; -.
DR Ensembl; ENSMUST00000040313; ENSMUSP00000041809; ENSMUSG00000037525.
DR GeneID; 75284; -.
DR KEGG; mmu:75284; -.
DR UCSC; uc007xpo.2; mouse.
DR CTD; 144233; -.
DR MGI; MGI:1922534; Bcdin3d.
DR VEuPathDB; HostDB:ENSMUSG00000037525; -.
DR eggNOG; KOG2899; Eukaryota.
DR GeneTree; ENSGT00940000153993; -.
DR HOGENOM; CLU_082749_0_0_1; -.
DR InParanoid; Q91YP1; -.
DR OMA; GNFMNYY; -.
DR OrthoDB; 1185441at2759; -.
DR PhylomeDB; Q91YP1; -.
DR TreeFam; TF324061; -.
DR BioGRID-ORCS; 75284; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Bcdin3d; mouse.
DR PRO; PR:Q91YP1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91YP1; protein.
DR Bgee; ENSMUSG00000037525; Expressed in ear vesicle and 160 other tissues.
DR Genevisible; Q91YP1; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008171; F:O-methyltransferase activity; ISO:MGI.
DR GO; GO:0070883; F:pre-miRNA binding; IEA:Ensembl.
DR GO; GO:0008173; F:RNA methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008175; F:tRNA methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; ISO:MGI.
DR GO; GO:2000632; P:negative regulation of pre-miRNA processing; ISS:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; IEA:Ensembl.
DR GO; GO:0001510; P:RNA methylation; ISO:MGI.
DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR039772; Bin3-like.
DR InterPro; IPR010675; Bin3_C.
DR InterPro; IPR024160; BIN3_SAM-bd_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12315; PTHR12315; 1.
DR Pfam; PF06859; Bin3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51515; BIN3_SAM; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..285
FT /note="RNA 5'-monophosphate methyltransferase"
FT /id="PRO_0000289266"
FT DOMAIN 53..275
FT /note="Bin3-type SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00848"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT BINDING 136..137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT CONFLICT 154
FT /note="F -> Y (in Ref. 1; BAB30128)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="S -> V (in Ref. 1; BAB30128)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="A -> G (in Ref. 1; BAB30128)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="E -> K (in Ref. 1; BAB30128)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="A -> P (in Ref. 1; BAB30128)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="I -> F (in Ref. 1; BAB30128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 32035 MW; C58CF217213A7E91 CRC64;
MAADGTLSRG GVGEAVEEEH PGALEPGAAP FGNFPHYSRF HPPEQRLRLL PPELLRQLFP
PEGPEKRPIL GLDVGCNSGD LSVALYKHFL SPRDGETCSG ASRELRILCC DIDPVLVERA
ERDCPFPEAL TFITLDIMDQ ESRKVPLSSF LSQFGRSVFD MVFCMSVTMW IHLNHGDRGL
CEFLAHVSSL CSYLLVEPQP WKCYRAAARR LRKLGLHSFD HFRSLAIRGD MAKQIVRILT
QDHGMELACC FGNTSWDRSL LLFRAKHTHE TQAIPESSTK ETRTD
