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Small RNA 2'-O-methyltransferase (EC 2.1.1.n8) (HEN1 methyltransferase homolog 1) (mHEN1)

 HENMT_MOUSE             Reviewed;         395 AA.
Q8CAE2; A2VCS5; Q8C3K8;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
22-NOV-2017, entry version 103.
RecName: Full=Small RNA 2'-O-methyltransferase;
EC=2.1.1.n8 {ECO:0000269|PubMed:17652135, ECO:0000269|PubMed:18029764};
AltName: Full=HEN1 methyltransferase homolog 1;
Short=mHEN1;
Name=Henmt1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-355 (ISOFORM 2).
TISSUE=Oocyte;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=18029764; DOI=10.1093/nass/nrm209;
Kirino Y., Mourelatos Z.;
"2'-O-methyl modification in mouse piRNAs and its methylase.";
Nucleic Acids Symp. Ser. 51:417-418(2007).
[5]
FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
54-ASP--GLY-58.
PubMed=17652135; DOI=10.1261/rna.659307;
Kirino Y., Mourelatos Z.;
"The mouse homolog of HEN1 is a potential methylase for Piwi-
interacting RNAs.";
RNA 13:1397-1401(2007).
-!- FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the
3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are
generated by a Dicer-independent mechanism and are primarily
derived from transposons and other repeated sequence elements.
This probably protects the 3'-end of piRNAs from uridylation
activity and subsequent degradation. Stabilization of piRNAs is
essential for gametogenesis. {ECO:0000269|PubMed:17652135,
ECO:0000269|PubMed:18029764}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + small RNA = S-
adenosyl-L-homocysteine + small RNA containing a 3'-terminal 2'-O-
methylnucleotide. {ECO:0000269|PubMed:17652135,
ECO:0000269|PubMed:18029764}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9C5Q8};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:Q9C5Q8};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q568P9}.
Note=Component of the meiotic nuage, also named P granule, a germ-
cell-specific organelle required to repress transposon activity
during meiosis. {ECO:0000250|UniProtKB:Q568P9}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8CAE2-1; Sequence=Displayed;
Name=2;
IsoId=Q8CAE2-2; Sequence=VSP_028012;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Specifically expressed in testis.
{ECO:0000269|PubMed:17652135, ECO:0000269|PubMed:18029764}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC39480.1; Type=Frameshift; Positions=270; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK038994; BAC30196.1; -; mRNA.
EMBL; AK085587; BAC39480.1; ALT_FRAME; mRNA.
EMBL; AL671894; CAM20609.1; -; Genomic_DNA.
EMBL; BC099408; AAH99408.1; -; mRNA.
EMBL; BC128494; AAI28495.1; -; mRNA.
EMBL; BC128495; AAI28496.1; -; mRNA.
CCDS; CCDS38602.1; -. [Q8CAE2-1]
RefSeq; NP_001072114.1; NM_001078646.1. [Q8CAE2-1]
RefSeq; NP_079999.2; NM_025723.2. [Q8CAE2-1]
RefSeq; XP_006501961.1; XM_006501898.2. [Q8CAE2-2]
UniGene; Mm.158124; -.
ProteinModelPortal; Q8CAE2; -.
SMR; Q8CAE2; -.
STRING; 10090.ENSMUSP00000054829; -.
PhosphoSitePlus; Q8CAE2; -.
PaxDb; Q8CAE2; -.
PRIDE; Q8CAE2; -.
Ensembl; ENSMUST00000059946; ENSMUSP00000054829; ENSMUSG00000045662. [Q8CAE2-1]
Ensembl; ENSMUST00000106586; ENSMUSP00000102196; ENSMUSG00000045662. [Q8CAE2-1]
Ensembl; ENSMUST00000196533; ENSMUSP00000143574; ENSMUSG00000045662. [Q8CAE2-2]
GeneID; 66715; -.
KEGG; mmu:66715; -.
UCSC; uc008qzz.1; mouse. [Q8CAE2-1]
UCSC; uc008rab.1; mouse. [Q8CAE2-2]
CTD; 113802; -.
MGI; MGI:1913965; Henmt1.
eggNOG; KOG1045; Eukaryota.
eggNOG; ENOG410XSD6; LUCA.
GeneTree; ENSGT00390000004798; -.
HOVERGEN; HBG097349; -.
InParanoid; Q8CAE2; -.
KO; K20798; -.
OMA; NSEFNPL; -.
OrthoDB; EOG091G08Y9; -.
PhylomeDB; Q8CAE2; -.
TreeFam; TF315178; -.
PRO; PR:Q8CAE2; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000045662; -.
CleanEx; MM_4921515J06RIK; -.
ExpressionAtlas; Q8CAE2; baseline and differential.
Genevisible; Q8CAE2; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043186; C:P granule; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0008173; F:RNA methyltransferase activity; IDA:UniProtKB.
GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
GO; GO:0034587; P:piRNA metabolic process; IDA:UniProtKB.
GO; GO:0001510; P:RNA methylation; IDA:UniProtKB.
InterPro; IPR026610; Hen1.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR21404; PTHR21404; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Metal-binding;
Methyltransferase; Reference proteome; RNA-binding;
RNA-mediated gene silencing; S-adenosyl-L-methionine; Transferase.
CHAIN 1 395 Small RNA 2'-O-methyltransferase.
/FTId=PRO_0000304141.
METAL 133 133 Magnesium.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 136 136 Magnesium.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 137 137 Magnesium; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 182 182 Magnesium; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9C5Q8}.
BINDING 79 79 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q9C5Q8}.
BINDING 115 115 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q9C5Q8}.
VAR_SEQ 9 51 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028012.
MUTAGEN 54 58 DLGCG->NAVAV: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:17652135}.
CONFLICT 319 319 F -> L (in Ref. 1; BAC39480).
{ECO:0000305}.
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


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