METL9_MOUSE
ID METL9_MOUSE Reviewed; 318 AA.
AC Q9EPL4; A0JG25; Q3TDX0; Q641L4; Q8R567; Q9EPL3; Q9JJ88;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein-L-histidine N-pros-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H1A3};
DE AltName: Full=DORA reverse strand protein {ECO:0000303|PubMed:11132146};
DE Short=DREV {ECO:0000303|PubMed:11132146};
DE AltName: Full=Methyltransferase-like protein 9 {ECO:0000303|PubMed:33563959};
DE Short=mMETTL9 {ECO:0000303|PubMed:33563959};
DE Flags: Precursor;
GN Name=Mettl9 {ECO:0000303|PubMed:33563959, ECO:0000312|MGI:MGI:1914862};
GN Synonyms=drev {ECO:0000303|PubMed:11132146};
GN ORFNames=MNCb-5680 {ECO:0000303|Ref.2};
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 [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-318,
RP AND TISSUE SPECIFICITY.
RC STRAIN=129/Ola;
RX PubMed=11132146; DOI=10.1007/s002510000259;
RA Bates E.E.M., Kissenpfennig A., Peronne C., Mattei M.-G., Fossiez F.,
RA Malissen B., Lebecque S.;
RT "The mouse and human IGSF6 (DORA) genes map to the inflammatory bowel
RT disease 1 locus and are embedded in an intron of a gene of unknown
RT function.";
RL Immunogenetics 52:112-120(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 74-318.
RC STRAIN=NOD;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION.
RX PubMed=33563959; DOI=10.1038/s41467-020-20670-7;
RA Davydova E., Shimazu T., Schuhmacher M.K., Jakobsson M.E.,
RA Willemen H.L.D.M., Liu T., Moen A., Ho A.Y.Y., Malecki J., Schroer L.,
RA Pinto R., Suzuki T., Groensberg I.A., Sohtome Y., Akakabe M., Weirich S.,
RA Kikuchi M., Olsen J.V., Dohmae N., Umehara T., Sodeoka M., Siino V.,
RA McDonough M.A., Eijkelkamp N., Schofield C.J., Jeltsch A., Shinkai Y.,
RA Falnes P.O.;
RT "The methyltransferase METTL9 mediates pervasive 1-methylhistidine
RT modification in mammalian proteomes.";
RL Nat. Commun. 12:891-891(2021).
CC -!- FUNCTION: Protein-histidine N-methyltransferase that specifically
CC catalyzes 1-methylhistidine (pros-methylhistidine) methylation of
CC target proteins (PubMed:33563959). Mediates methylation of proteins
CC with a His-x-His (HxH) motif (where 'x' is preferably a small amino
CC acid) (PubMed:33563959). Catalyzes methylation of target proteins such
CC as S100A9, NDUFB3, SLC39A5, SLC39A7, ARMC6 and DNAJB12; 1-
CC methylhistidine modification may affect the binding of zinc and other
CC metals to its target proteins (PubMed:33563959). Constitutes the main
CC methyltransferase for the 1-methylhistidine modification in cell
CC (PubMed:33563959). {ECO:0000269|PubMed:33563959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(pros)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:67076, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:17184,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29979, ChEBI:CHEBI:43903,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC Evidence={ECO:0000250|UniProtKB:Q9H1A3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67077;
CC Evidence={ECO:0000250|UniProtKB:Q9H1A3};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9H1A3}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9H1A3}. Note=Colocalizes with membranous
CC compartments such as the endoplasmic reticulum and mitochondria.
CC {ECO:0000250|UniProtKB:Q9H1A3}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, colon, small intestine, skin,
CC kidney and to a lesser extent in spleen, lung, thymus and stomach. Not
CC detected in fibroblast and endothelial cells.
CC {ECO:0000269|PubMed:11132146}.
CC -!- SIMILARITY: Belongs to the METTL9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA95109.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ278574; CAC20695.1; -; Genomic_DNA.
DR EMBL; AJ278579; CAC21450.1; -; Genomic_DNA.
DR EMBL; AJ278580; CAC21450.1; JOINED; Genomic_DNA.
DR EMBL; AJ278576; CAC20698.1; -; mRNA.
DR EMBL; AB041664; BAA95109.1; ALT_FRAME; mRNA.
DR EMBL; BC023188; AAH23188.1; ALT_INIT; mRNA.
DR EMBL; BC068124; AAH68124.1; -; mRNA.
DR EMBL; BC082317; AAH82317.1; -; mRNA.
DR EMBL; AK169951; BAE41478.1; -; mRNA.
DR CCDS; CCDS21800.1; -.
DR RefSeq; NP_067529.2; NM_021554.2.
DR AlphaFoldDB; Q9EPL4; -.
DR SMR; Q9EPL4; -.
DR BioGRID; 208515; 2.
DR IntAct; Q9EPL4; 1.
DR STRING; 10090.ENSMUSP00000033163; -.
DR GlyGen; Q9EPL4; 1 site.
DR iPTMnet; Q9EPL4; -.
DR PhosphoSitePlus; Q9EPL4; -.
DR EPD; Q9EPL4; -.
DR MaxQB; Q9EPL4; -.
DR PaxDb; Q9EPL4; -.
DR PeptideAtlas; Q9EPL4; -.
DR PRIDE; Q9EPL4; -.
DR ProteomicsDB; 292223; -.
DR Antibodypedia; 25721; 26 antibodies from 12 providers.
DR DNASU; 59052; -.
DR Ensembl; ENSMUST00000033163; ENSMUSP00000033163; ENSMUSG00000030876.
DR GeneID; 59052; -.
DR KEGG; mmu:59052; -.
DR UCSC; uc009jnk.1; mouse.
DR CTD; 51108; -.
DR MGI; MGI:1914862; Mettl9.
DR VEuPathDB; HostDB:ENSMUSG00000030876; -.
DR eggNOG; KOG3987; Eukaryota.
DR GeneTree; ENSGT00390000013648; -.
DR HOGENOM; CLU_056100_0_0_1; -.
DR InParanoid; Q9EPL4; -.
DR OMA; PYMHYVE; -.
DR OrthoDB; 899076at2759; -.
DR PhylomeDB; Q9EPL4; -.
DR TreeFam; TF314187; -.
DR BioGRID-ORCS; 59052; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Mettl9; mouse.
DR PRO; PR:Q9EPL4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9EPL4; protein.
DR Bgee; ENSMUSG00000030876; Expressed in gastrula and 255 other tissues.
DR ExpressionAtlas; Q9EPL4; baseline and differential.
DR Genevisible; Q9EPL4; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0106370; F:protein-L-histidine N-pros-methyltransferase activity; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR007884; METL9.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12890; PTHR12890; 1.
DR Pfam; PF05219; DREV; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Methyltransferase; Mitochondrion;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..318
FT /note="Protein-L-histidine N-pros-methyltransferase"
FT /id="PRO_0000317491"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 102
FT /note="S -> F (in Ref. 4; BAE41478)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="F -> S (in Ref. 2; BAA95109)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="K -> R (in Ref. 2; BAA95109)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="K -> E (in Ref. 2; BAA95109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36426 MW; 640AC36FEFE48BF5 CRC64;
MRLLAGWLCL SLASVWLARR MWTLRSPLSR SLYVNMTSGP GGPAAAAGGG KDTHQWYVCN
REKLCESLQS VFVQSYLDQG TQIFLNNSIE KSGWLFIQLY HSFVSSVFSL FMSRTSINGL
LGRGSMFVFS PDQFQRLLRI NPDWKTHRLL DLGAGDGEVT KIMSPHFEEI YATELSETMI
WQLQKKKYRV LGINEWQNTG FQYDVISCLN LLDRCDQPLT LLKDIRSVLE PTQGRVILAL
VLPFHPYVEN VGGKWEKPSE ILEIKGQNWE EQVNSLPEVF RKAGFVVEAF TRLPYLCEGD
MYNDYYVLDD AVFVLRPV
