HENMT_CAEEL
ID HENMT_CAEEL Reviewed; 442 AA.
AC P34283; Q8T3F9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Small RNA 2'-O-methyltransferase {ECO:0000305};
DE EC=2.1.1.n8 {ECO:0000269|PubMed:22829772, ECO:0000305|PubMed:22536158, ECO:0000305|PubMed:22548001};
DE AltName: Full=HEN1 methyltransferase homolog {ECO:0000305};
GN Name=henn-1 {ECO:0000303|PubMed:22536158, ECO:0000303|PubMed:22548001,
GN ECO:0000303|PubMed:22829772, ECO:0000312|WormBase:C02F5.6b};
GN ORFNames=C02F5.6 {ECO:0000312|WormBase:C02F5.6b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 347-LYS--LEU-442.
RX PubMed=22536158; DOI=10.1371/journal.pgen.1002616;
RA Montgomery T.A., Rim Y.S., Zhang C., Dowen R.H., Phillips C.M.,
RA Fischer S.E., Ruvkun G.;
RT "PIWI associated siRNAs and piRNAs specifically require the Caenorhabditis
RT elegans HEN1 ortholog henn-1.";
RL PLoS Genet. 8:E1002616-E1002616(2012).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=22548001; DOI=10.1371/journal.pgen.1002617;
RA Billi A.C., Alessi A.F., Khivansara V., Han T., Freeberg M., Mitani S.,
RA Kim J.K.;
RT "The Caenorhabditis elegans HEN1 ortholog, HENN-1, methylates and
RT stabilizes select subclasses of germline small RNAs.";
RL PLoS Genet. 8:E1002617-E1002617(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF ASP-151 AND 347-LYS--LEU-442.
RX PubMed=22829772; DOI=10.1371/journal.pgen.1002702;
RA Kamminga L.M., van Wolfswinkel J.C., Luteijn M.J., Kaaij L.J., Bagijn M.P.,
RA Sapetschnig A., Miska E.A., Berezikov E., Ketting R.F.;
RT "Differential impact of the HEN1 homolog HENN-1 on 21U and 26G RNAs in the
RT germline of Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002702-E1002702(2012).
CC -!- FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end
CC of PIWI-interacting RNAs (piRNAs) and small interfering RNAs (siRNAs)
CC which are classes of regulatory RNAs that are involved in gene
CC silencing in endogenous RNA interference (RNAi) pathways
CC (PubMed:22536158, PubMed:22548001, PubMed:22829772). Methylation
CC protects the 3'-end of small RNAs from tailing and trimming and could
CC constitute a recognition signal for appropriate argonaute machineries
CC (Probable). Methylates and stabilizes 26G-siRNAs (a class of 26
CC nucleotide siRNAs that possess a monophosphorylated guanine residue at
CC the 5'-end) when they are bound by argonaute protein ergo-1
CC (PubMed:22536158, PubMed:22548001, PubMed:22829772). This occurs in the
CC female germline and embryo, but not in the male germline
CC (PubMed:22548001). Does not methylate 26G-siRNAs bound by argonaute
CC proteins alg-3 or alg-4 (PubMed:22548001, PubMed:22829772). Methylates
CC and stabilizes 21U-piRNAs, which are a class of 21 nucleotide piRNAs
CC that possess a uracil residue at the 5'-end, in the male and female
CC germline (PubMed:22536158, PubMed:22548001, PubMed:22829772). In
CC addition, may play a role in exogenous RNAi (exoRNAi) pathways in the
CC germline (PubMed:22829772). {ECO:0000269|PubMed:22536158,
CC ECO:0000269|PubMed:22548001, ECO:0000269|PubMed:22829772, ECO:0000305}.
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:22829772, ECO:0000305|PubMed:22536158,
CC ECO:0000305|PubMed:22548001};
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:22548001,
CC ECO:0000269|PubMed:22829772}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:22548001}. Cytoplasmic granule
CC {ECO:0000269|PubMed:22829772}. Note=Nucleoplasm localization ceases
CC following fertilization (PubMed:22548001). In embryos, diffusely
CC localized in the cytoplasm (PubMed:22829772). In cells of the P-lineage
CC (germ cell progenitor cells) in embryos, localizes to granules and at
CC later postembryonic stages of development, localizes to perinuclear
CC granules in the germ cells (PubMed:22829772).
CC {ECO:0000269|PubMed:22548001, ECO:0000269|PubMed:22829772}.
CC -!- TISSUE SPECIFICITY: Broadly expressed in the germline and somatic
CC tissues in both hermaphrodites and males.
CC {ECO:0000269|PubMed:22548001}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the germline and soma throughout
CC development (at the protein level) (PubMed:22548001, PubMed:22829772).
CC Highly expressed in embryos (PubMed:22548001, PubMed:22829772).
CC Expression is lowest during the early larval stages and increases as
CC the germline proliferates, peaking at the adult stage
CC (PubMed:22548001). {ECO:0000269|PubMed:22548001,
CC ECO:0000269|PubMed:22829772}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown suppresses RNAi-mediated
CC silencing by siR-1, which are 22G-siRNAs (a class of secondary 22
CC nucleotide siRNAs that possess a triphosphorylated guanine residue at
CC the 5'-end and are formed from 21U-piRNAs and 26G-siRNAs).
CC {ECO:0000269|PubMed:22536158}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC {ECO:0000305}.
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DR EMBL; BX284603; CCD62631.1; -; Genomic_DNA.
DR PIR; S44608; S44608.
DR RefSeq; NP_001309472.1; NM_001322688.1.
DR AlphaFoldDB; P34283; -.
DR SMR; P34283; -.
DR BioGRID; 41364; 4.
DR STRING; 6239.C02F5.6b; -.
DR EPD; P34283; -.
DR PaxDb; P34283; -.
DR PeptideAtlas; P34283; -.
DR EnsemblMetazoa; C02F5.6b.1; C02F5.6b.1; WBGene00015349.
DR GeneID; 176159; -.
DR KEGG; cel:CELE_C02F5.6; -.
DR UCSC; C02F5.6b; c. elegans.
DR CTD; 176159; -.
DR WormBase; C02F5.6b; CE51509; WBGene00015349; henn-1.
DR eggNOG; KOG1045; Eukaryota.
DR GeneTree; ENSGT00390000004798; -.
DR InParanoid; P34283; -.
DR OrthoDB; 789470at2759; -.
DR PhylomeDB; P34283; -.
DR PRO; PR:P34283; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015349; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008173; F:RNA methyltransferase activity; IDA:WormBase.
DR GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IDA:WormBase.
DR GO; GO:0030422; P:siRNA processing; IMP: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; Magnesium; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..442
FT /note="Small RNA 2'-O-methyltransferase"
FT /id="PRO_0000065111"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5T8I9"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5T8I9"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT MUTAGEN 151
FT /note="D->N: In pk2452; viable with reduced brood size.
FT Reduces methyltransferase activity. Reduces methylation of
FT 26G-siRNAs and 21U-piRNAs."
FT /evidence="ECO:0000269|PubMed:22829772"
FT MUTAGEN 347..442
FT /note="Missing: In pk2295; viable with reduced brood size.
FT Reduces methyltransferase activity. Reduces methylation of
FT 26G-siRNAs and 21U-piRNAs. Reduces levels of 22G-siRNAs
FT (which are formed from 21U-piRNAs and 26G-siRNAs) in
FT embryos. Suppresses RNAi-mediated silencing by siR-1, which
FT are 22G-siRNAs. Reduces levels of 21U-piRNAs in embryos and
FT modestly reduces levels of 21U-piRNAs in adults, but 21U-
FT piRNAs levels are unaffected at the L4 larval stage. Mixed
FT exoRNAi defects with enhanced RNAi (Eri phenotype) in
FT somatic cells in a dpy-13 RNAi-mediated knockdown
FT background, and defective RNAi (Rde phenotype) in somatic
FT cells in a pos-1 RNAi-mediated knockdown background."
FT /evidence="ECO:0000269|PubMed:22536158,
FT ECO:0000269|PubMed:22829772"
SQ SEQUENCE 442 AA; 50853 MW; DA33E77743C751D6 CRC64;
MAHTSDGWGA PYDNQTYVEA YEQLEIALLE PLDRILETAN VEEFRPKFKN HQDPNDRKNK
KNNDEEWRDS IYNIATDESD TDDHEQRKNF FQPPLQVQRN SFVKNTLMEF KRSSQIDISR
LAVMGCGEMS LEKGICEYLG SFGTINVLSV DIDEPSLSIG QQLLGKHLER NAEILAVETG
LPVLMRSYVG DILEPDHRFA DVDAIVSMEV VEHIPLPNAK KFVENVLGTL MPRIFIFSTP
NHEYNAVFGM EPGEFRHGDH KFEMNRKEFS NWLEELSIRF PHYQIDPPHY IGMTRGYENL
SGASQAAVCR LQVDLNTTLP QEVTPYEMVG HLPCRLGSRL IAYNLVKEAF LDWLEKIELQ
EHEPRTDGYS PYWIFNVQNI LHHLKAPVSF ALTIDEKVAI KYIQGMTSRK VHAEYSHGFN
GIVILQMHSK EELIKTVQDN TL
