ID MRM3_HUMAN Reviewed; 420 AA.
AC Q9HC36; Q53GN1; Q86VC3; Q96F76; Q9NVQ5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 30-NOV-2016, entry version 122.
DE RecName: Full=rRNA methyltransferase 3, mitochondrial {ECO:0000303|PubMed:25009282};
DE EC=2.1.1.- {ECO:0000305|PubMed:24036117, ECO:0000305|PubMed:25074936};
DE AltName: Full=16S rRNA (guanosine(1370)-2'-O)-methyltransferase {ECO:0000303|PubMed:25074936};
DE AltName: Full=16S rRNA [Gm1370] 2'-O-methyltransferase {ECO:0000303|PubMed:25074936};
DE AltName: Full=RNA methyltransferase-like protein 1 {ECO:0000303|PubMed:12296377};
DE Flags: Precursor;
GN Name=MRM3 {ECO:0000303|PubMed:25009282, ECO:0000312|HGNC:HGNC:18485};
GN Synonyms=RNMTL1 {ECO:0000303|PubMed:12296377}; ORFNames=HC90;
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 [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Gu J.R., Zhao X.T., Wan D.F., Jiang H.Q., Huang Y., He Y.H., Qin W.X.,
RA Han L.W., Zhang P.P., Qiu X.K., He L.P.;
RT "Homo sapiens P579 chromosome 17p DNA sequence fragment.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-8 AND
RP VAL-185.
RC TISSUE=Brain, and Skin;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12296377; DOI=10.1038/sj.cr.7290124;
RA Xu J., De Zhu J., Ni M., Wan F., Gu J.R.;
RT "The ATF/CREB site is the key element for transcription of the human
RT RNA methyltransferase like 1(RNMTL1) gene, a newly discovered 17p13.3
RT gene.";
RL Cell Res. 12:177-197(2002).
RN [7]
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).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24036117; DOI=10.1074/jbc.M113.515692;
RA Lee K.W., Okot-Kotber C., LaComb J.F., Bogenhagen D.F.;
RT "Mitochondrial ribosomal RNA (rRNA) methyltransferase family members
RT are positioned to modify nascent rRNA in foci near the mitochondrial
RT DNA nucleoid.";
RL J. Biol. Chem. 288:31386-31399(2013).
RN [9]
RP FUNCTION.
RX PubMed=25074936; DOI=10.1074/jbc.C114.581868;
RA Lee K.W., Bogenhagen D.F.;
RT "Assignment of 2'-O-methyltransferases to modification sites on the
RT mammalian mitochondrial large subunit 16S rRNA.";
RL J. Biol. Chem. 289:24936-24942(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25009282; DOI=10.1091/mbc.E14-01-0014;
RA Rorbach J., Boesch P., Gammage P.A., Nicholls T.J., Pearce S.F.,
RA Patel D., Hauser A., Perocchi F., Minczuk M.;
RT "MRM2 and MRM3 are involved in biogenesis of the large subunit of the
RT mitochondrial ribosome.";
RL Mol. Biol. Cell 25:2542-2555(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC methyltransferase that catalyzes the formation of 2'-O-
CC methylguanosine at position 1370 (Gm1370) in the 16S mitochondrial
CC large subunit ribosomal RNA (mtLSU rRNA), a conserved modification
CC in the peptidyl transferase domain of the mtLSU rRNA.
CC {ECO:0000269|PubMed:24036117, ECO:0000269|PubMed:25009282,
CC ECO:0000269|PubMed:25074936}.
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanosine(1370) in
CC 16S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine(1370)
CC in 16S rRNA. {ECO:0000305|PubMed:24036117,
CC ECO:0000305|PubMed:25074936}.
CC -!- INTERACTION:
CC Q13643:FHL3; NbExp=5; IntAct=EBI-1045440, EBI-741101;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24036117,
CC ECO:0000269|PubMed:25009282}.
CC -!- TISSUE SPECIFICITY: Expressed at same level in normal liver and
CC hepatocarcinoma. {ECO:0000269|PubMed:12296377}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding
CC methyltransferase superfamily. RNA methyltransferase TrmH family.
CC {ECO:0000305}.
DR EMBL; AK001443; BAA91694.1; -; mRNA.
DR EMBL; AK222900; BAD96620.1; -; mRNA.
DR EMBL; AF177344; AAG17988.2; -; mRNA.
DR EMBL; CH471108; EAW90642.1; -; Genomic_DNA.
DR EMBL; BC011550; AAH11550.1; -; mRNA.
DR EMBL; BC050614; AAH50614.1; -; mRNA.
DR CCDS; CCDS10997.1; -.
DR RefSeq; NP_001304876.1; NM_001317947.1.
DR RefSeq; NP_060616.1; NM_018146.3.
DR UniGene; Hs.182729; -.
DR ProteinModelPortal; Q9HC36; -.
DR SMR; Q9HC36; -.
DR BioGrid; 120477; 51.
DR IntAct; Q9HC36; 7.
DR MINT; MINT-8052394; -.
DR STRING; 9606.ENSP00000306080; -.
DR iPTMnet; Q9HC36; -.
DR PhosphoSitePlus; Q9HC36; -.
DR BioMuta; RNMTL1; -.
DR DMDM; 74734265; -.
DR EPD; Q9HC36; -.
DR MaxQB; Q9HC36; -.
DR PaxDb; Q9HC36; -.
DR PeptideAtlas; Q9HC36; -.
DR PRIDE; Q9HC36; -.
DR DNASU; 55178; -.
DR Ensembl; ENST00000304478; ENSP00000306080; ENSG00000171861.
DR GeneID; 55178; -.
DR KEGG; hsa:55178; -.
DR UCSC; uc002frw.4; human.
DR CTD; 55178; -.
DR GeneCards; RNMTL1; -.
DR HGNC; HGNC:18485; MRM3.
DR HPA; HPA022534; -.
DR HPA; HPA023031; -.
DR HPA; HPA023292; -.
DR MIM; 612600; gene.
DR neXtProt; NX_Q9HC36; -.
DR OpenTargets; ENSG00000171861; -.
DR PharmGKB; PA38341; -.
DR eggNOG; KOG2506; Eukaryota.
DR eggNOG; COG0566; LUCA.
DR GeneTree; ENSGT00390000017317; -.
DR HOGENOM; HOG000154151; -.
DR HOVERGEN; HBG108411; -.
DR InParanoid; Q9HC36; -.
DR KO; K20095; -.
DR OMA; RYDKAFP; -.
DR OrthoDB; EOG091G0OPI; -.
DR PhylomeDB; Q9HC36; -.
DR TreeFam; TF323420; -.
DR BioCyc; ZFISH:ENSG00000171861-MONOMER; -.
DR Reactome; R-HSA-6793080; rRNA modification in the mitochondrion.
DR ChiTaRS; RNMTL1; human.
DR GeneWiki; RNMTL1; -.
DR GenomeRNAi; 55178; -.
DR PRO; PR:Q9HC36; -.
DR Proteomes; UP000005640; Chromosome 17.
DR Bgee; ENSG00000171861; -.
DR CleanEx; HS_RNMTL1; -.
DR ExpressionAtlas; Q9HC36; baseline and differential.
DR Genevisible; Q9HC36; HS.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.40.1280.10; -; 2.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR013123; SpoU_subst-bd.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SMART; SM00967; SpoU_sub_bind; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF75217; SSF75217; 2.
PE 1: Evidence at protein level;
KW Complete proteome; Methyltransferase; Mitochondrion; Polymorphism;
KW Reference proteome; rRNA processing; S-adenosyl-L-methionine;
KW Transferase; Transit peptide.
FT TRANSIT 1 40 Mitochondrion. {ECO:0000255}.
FT CHAIN 41 420 rRNA methyltransferase 3, mitochondrial.
FT /FTId=PRO_0000311301.
FT BINDING 356 356 S-adenosyl-L-methionine; via carbonyl
FT oxygen. {ECO:0000250}.
FT BINDING 380 380 S-adenosyl-L-methionine; via amide
FT nitrogen and carbonyl oxygen.
FT {ECO:0000250}.
FT BINDING 389 389 S-adenosyl-L-methionine; via amide
FT nitrogen. {ECO:0000250}.
FT VARIANT 8 8 A -> S (in dbSNP:rs2273454).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_037217.
FT VARIANT 45 45 G -> E (in dbSNP:rs2249542).
FT /FTId=VAR_037218.
FT VARIANT 185 185 I -> V (in dbSNP:rs17854653).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_037219.
FT VARIANT 326 326 E -> Q (in dbSNP:rs35780267).
FT /FTId=VAR_037220.
FT CONFLICT 247 247 A -> V (in Ref. 3; BAD96620).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 210 400 ipfam:SpoU_methylase [T]
FT MYHIT 124 195 ismart:SpoU_sub_bind [T]
SQ SEQUENCE 420 AA; 47020 MW; CC06C27489A89FC3 CRC64;
MAALVRPARF VVRPLLQVVQ AWDLDARRWV RALRRSPVKV VFPSGEVVEQ KRAPGKQPRK
APSEASAQEQ REKQPLEESA SRAPSTWEES GLRYDKAYPG DRRLSSVMTI VKSRPFREKQ
GKILLEGRRL ISDALKAGAV PKMFFFSRLE YLKELPVDKL KGVSLIKVKF EDIKDWSDLV
TPQGIMGIFA KPDHVKMTYP KTQLQHSLPL LLICDNLRDP GNLGTILRSA AGAGCSKVLL
TKGCVDAWEP KVLRAGMGAH FRMPIINNLE WETVPNYLPP DTRVYVADNC GLYAQAEMSN
KASDHGWVCD QRVMKFHKYE EEEDVETGAS QDWLPHVEVQ SYDSDWTEAP AAVVIGGETY
GVSLESLQLA ESTGGKRLLI PVVPGVDSLN SAMAASILLF EGKRQLRGRA EDLSRDRSYH
//
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