HENMT_MOUSE
ID HENMT_MOUSE Reviewed; 395 AA.
AC Q8CAE2; A2VCS5; Q8C3K8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Small RNA 2'-O-methyltransferase;
DE EC=2.1.1.n8 {ECO:0000269|PubMed:17652135, ECO:0000269|PubMed:18029764};
DE AltName: Full=HEN1 methyltransferase homolog 1;
DE Short=mHEN1;
GN Name=Henmt1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Kidney;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-355 (ISOFORM 2).
RC TISSUE=Oocyte;
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 FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=18029764; DOI=10.1093/nass/nrm209;
RA Kirino Y., Mourelatos Z.;
RT "2'-O-methyl modification in mouse piRNAs and its methylase.";
RL Nucleic Acids Symp. Ser. 51:417-418(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 54-ASP--GLY-58.
RX PubMed=17652135; DOI=10.1261/rna.659307;
RA Kirino Y., Mourelatos Z.;
RT "The mouse homolog of HEN1 is a potential methylase for Piwi-interacting
RT RNAs.";
RL RNA 13:1397-1401(2007).
CC -!- FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end
CC of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a
CC Dicer-independent mechanism and are primarily derived from transposons
CC and other repeated sequence elements. This probably protects the 3'-end
CC of piRNAs from uridylation activity and subsequent degradation.
CC Stabilization of piRNAs is essential for gametogenesis.
CC {ECO:0000269|PubMed:17652135, ECO:0000269|PubMed:18029764}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) +
CC S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide;
CC Xref=Rhea:RHEA:37887, Rhea:RHEA-COMP:10415, Rhea:RHEA-COMP:10416,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:74898; EC=2.1.1.n8;
CC Evidence={ECO:0000269|PubMed:17652135, ECO:0000269|PubMed:18029764};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9C5Q8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9C5Q8};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q568P9}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis. {ECO:0000250|UniProtKB:Q568P9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CAE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CAE2-2; Sequence=VSP_028012;
CC -!- TISSUE SPECIFICITY: Specifically expressed in testis.
CC {ECO:0000269|PubMed:17652135, ECO:0000269|PubMed:18029764}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39480.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK038994; BAC30196.1; -; mRNA.
DR EMBL; AK085587; BAC39480.1; ALT_FRAME; mRNA.
DR EMBL; AL671894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099408; AAH99408.1; -; mRNA.
DR EMBL; BC128494; AAI28495.1; -; mRNA.
DR EMBL; BC128495; AAI28496.1; -; mRNA.
DR CCDS; CCDS38602.1; -. [Q8CAE2-1]
DR RefSeq; NP_001072114.1; NM_001078646.1. [Q8CAE2-1]
DR RefSeq; NP_079999.2; NM_025723.2. [Q8CAE2-1]
DR RefSeq; XP_006501961.1; XM_006501898.2. [Q8CAE2-2]
DR AlphaFoldDB; Q8CAE2; -.
DR SMR; Q8CAE2; -.
DR STRING; 10090.ENSMUSP00000054829; -.
DR PhosphoSitePlus; Q8CAE2; -.
DR PaxDb; Q8CAE2; -.
DR PRIDE; Q8CAE2; -.
DR ProteomicsDB; 269591; -. [Q8CAE2-1]
DR ProteomicsDB; 269592; -. [Q8CAE2-2]
DR Antibodypedia; 33732; 50 antibodies from 15 providers.
DR Ensembl; ENSMUST00000059946; ENSMUSP00000054829; ENSMUSG00000045662. [Q8CAE2-1]
DR Ensembl; ENSMUST00000106586; ENSMUSP00000102196; ENSMUSG00000045662. [Q8CAE2-1]
DR Ensembl; ENSMUST00000196533; ENSMUSP00000143574; ENSMUSG00000045662. [Q8CAE2-2]
DR GeneID; 66715; -.
DR KEGG; mmu:66715; -.
DR UCSC; uc008qzz.1; mouse. [Q8CAE2-1]
DR UCSC; uc008rab.1; mouse. [Q8CAE2-2]
DR CTD; 113802; -.
DR MGI; MGI:1913965; Henmt1.
DR VEuPathDB; HostDB:ENSMUSG00000045662; -.
DR eggNOG; KOG1045; Eukaryota.
DR GeneTree; ENSGT00390000004798; -.
DR HOGENOM; CLU_044646_0_0_1; -.
DR InParanoid; Q8CAE2; -.
DR OMA; QRHQFVV; -.
DR OrthoDB; 789470at2759; -.
DR PhylomeDB; Q8CAE2; -.
DR TreeFam; TF315178; -.
DR BioGRID-ORCS; 66715; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Henmt1; mouse.
DR PRO; PR:Q8CAE2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8CAE2; protein.
DR Bgee; ENSMUSG00000045662; Expressed in spermatocyte and 29 other tissues.
DR ExpressionAtlas; Q8CAE2; baseline and differential.
DR Genevisible; Q8CAE2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008173; F:RNA methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; ISO:MGI.
DR GO; GO:0034587; P:piRNA metabolic process; IDA:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IDA:UniProtKB.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026610; Hen1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR21404; PTHR21404; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Magnesium; Metal-binding;
KW Methyltransferase; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..395
FT /note="Small RNA 2'-O-methyltransferase"
FT /id="PRO_0000304141"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT VAR_SEQ 9..51
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028012"
FT MUTAGEN 54..58
FT /note="DLGCG->NAVAV: Abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:17652135"
FT CONFLICT 319
FT /note="F -> L (in Ref. 1; BAC39480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 44921 MW; BA648D0289C2EEBE CRC64;
MEMAESIPCN SVVGGNFKEV SPEKVIRFKP PLYKQRYQFV RDLVDRHEPK KVADLGCGDA
KLLKLLKIYP CIQLLVGVDI NEEKLHSNGH RLSPYLGEFV KPRDLDLTVT LYHGSVVERD
SRLLGFDLIT CIELIEHLDS DDLARFPDVV FGYLSPAMVV ISTPNAEFNP LFPTVTLRDA
DHKFEWSRME FQTWALHVAN CYNYRVEFTG VGTPPAGSEH VGYCTQIGVF TKNGGKLSKP
SVSQQCDQHV YKPVYTTSYP SLQQEKVLKF VLVGELLIQV DRLRLRYQRM LRDREKDRGP
KPGDMDSCPA PHLLLGAVFT EAEKARIESS PKPFCEGEKF YIPLQRLLTY PKLHRLCADE
DRVRSLIADS VCLSSDGSAV VVDLHNSWDY RPEEN
