HENMT_DANRE
ID HENMT_DANRE Reviewed; 402 AA.
AC Q568P9; Q5RH79;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Small RNA 2'-O-methyltransferase;
DE EC=2.1.1.n8 {ECO:0000269|PubMed:20859253};
DE AltName: Full=HEN1 methyltransferase homolog 1;
GN Name=henmt1; ORFNames=si:ch211-199m3.6, zgc:110175;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=20859253; DOI=10.1038/emboj.2010.233;
RA Kamminga L.M., Luteijn M.J., den Broeder M.J., Redl S., Kaaij L.J.,
RA Roovers E.F., Ladurner P., Berezikov E., Ketting R.F.;
RT "Hen1 is required for oocyte development and piRNA stability in
RT zebrafish.";
RL EMBO J. 29:3688-3700(2010).
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 and adenylation activities and subsequent
CC degradation. Stabilization of piRNAs is essential for oocyte
CC development. {ECO:0000269|PubMed:20859253}.
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:20859253};
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:0000269|PubMed:20859253}.
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:0000269|PubMed:20859253}.
CC -!- TISSUE SPECIFICITY: Gonad-specific. {ECO:0000269|PubMed:20859253}.
CC -!- DEVELOPMENTAL STAGE: Expression in gonads starts around 3 weeks of age,
CC which corresponds to the start of sex determination. Expression remains
CC present in the adult gonads, both in males and females, although
CC expression is weaker in testis. {ECO:0000269|PubMed:20859253}.
CC -!- DISRUPTION PHENOTYPE: Defects in germ cell development due to reduced
CC piRNAs levels. {ECO:0000269|PubMed:20859253}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC {ECO:0000305}.
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DR EMBL; BX571790; CAI11740.1; -; Genomic_DNA.
DR EMBL; BC092772; AAH92772.1; -; mRNA.
DR RefSeq; NP_001017842.1; NM_001017842.2.
DR AlphaFoldDB; Q568P9; -.
DR SMR; Q568P9; -.
DR STRING; 7955.ENSDARP00000004251; -.
DR PaxDb; Q568P9; -.
DR Ensembl; ENSDART00000015000; ENSDARP00000004251; ENSDARG00000018871.
DR GeneID; 550540; -.
DR KEGG; dre:550540; -.
DR CTD; 113802; -.
DR ZFIN; ZDB-GENE-050417-387; henmt1.
DR eggNOG; KOG1045; Eukaryota.
DR GeneTree; ENSGT00390000004798; -.
DR HOGENOM; CLU_044646_0_0_1; -.
DR InParanoid; Q568P9; -.
DR OMA; QRHQFVV; -.
DR OrthoDB; 789470at2759; -.
DR PhylomeDB; Q568P9; -.
DR TreeFam; TF315178; -.
DR PRO; PR:Q568P9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000018871; Expressed in retina and 21 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:ZFIN.
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; IEA:RHEA.
DR GO; GO:0048599; P:oocyte development; IMP:ZFIN.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:ZFIN.
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 Cytoplasm; Differentiation; Magnesium; Metal-binding; Methyltransferase;
KW Oogenesis; Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..402
FT /note="Small RNA 2'-O-methyltransferase"
FT /id="PRO_0000304143"
FT REGION 348..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..374
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT CONFLICT 161
FT /note="D -> G (in Ref. 2; AAH92772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 46124 MW; 6EA54C594C320690 CRC64;
MTATPFSPPL YMQRYQFVID YVKTYRPRKV IDFGCAECCL LKKLKFHRNG IQLLVGVDIN
SVVLLKRMHS LAPLVSDYLQ PSDGPLTIEL YQGSVMEREP CTKGFDLVTC VELIEHLELE
EVERFSEVVF GYMAPGAVIV TTPNAEFNPL LPGLRGFRNY DHKFEWTRAE FQTWAHRVCR
EHGYSVQFTG VGEAAGHWRD VGFCTQIAVF QRNFDGVNRS MSNAEHLEPS VYRLLYRVVY
PSLCDNNIYQ KTLINEVLYE AQHLRQQWLI RENMNNNAHF YSPPLMEALH HGAEGNACEQ
QPVYQQGGII CVPLARVWSC PRVQALCGSL QRLREKLLED ERVRMSADGS ALNLPADDDD
DNVEEEEEEE EEENQQNVKA VSGAVNNMEE DWDRELGSYG DE
