METL5_DANRE
ID METL5_DANRE Reviewed; 207 AA.
AC F1QVR8; Q5XJ53;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=rRNA N6-adenosine-methyltransferase METTL5 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9NRN9};
DE AltName: Full=Methyltransferase-like protein 5 {ECO:0000303|PubMed:31564433};
GN Name=mettl5 {ECO:0000303|PubMed:31564433,
GN ECO:0000312|ZFIN:ZDB-GENE-041010-21};
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].
RC TISSUE=Larva {ECO:0000312|EMBL:AAH83455.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=31564433; DOI=10.1016/j.ajhg.2019.09.007;
RA Richard E.M., Polla D.L., Assir M.Z., Contreras M., Shahzad M., Khan A.A.,
RA Razzaq A., Akram J., Tarar M.N., Blanpied T.A., Ahmed Z.M., Abou Jamra R.,
RA Wieczorek D., van Bokhoven H., Riazuddin S., Riazuddin S.;
RT "Bi-allelic variants in METTL5 cause autosomal-recessive intellectual
RT disability and microcephaly.";
RL Am. J. Hum. Genet. 105:869-878(2019).
CC -!- FUNCTION: Catalytic subunit of a heterodimer with TRMT112, which
CC specifically methylates the 6th position of adenine in position 1832 of
CC 18S rRNA (By similarity). N6-methylation of adenine(1832) in 18S rRNA
CC resides in the decoding center of 18S rRNA and is required for
CC translation and embryonic stem cells (ESCs) pluripotency and
CC differentiation (By similarity). {ECO:0000250|UniProtKB:Q8K1A0,
CC ECO:0000250|UniProtKB:Q9NRN9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(1832) in 18S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyladenosine(1832) in 18S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:62612, Rhea:RHEA-COMP:16144, Rhea:RHEA-COMP:16145,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449;
CC Evidence={ECO:0000250|UniProtKB:Q9NRN9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62613;
CC Evidence={ECO:0000250|UniProtKB:Q9NRN9};
CC -!- ACTIVITY REGULATION: rRNA N6-adenosine-methyltransferase activity is
CC inhibited by zinc. {ECO:0000250|UniProtKB:Q9NRN9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NRN9}.
CC Presynapse {ECO:0000250|UniProtKB:Q9NRN9}. Postsynapse
CC {ECO:0000250|UniProtKB:Q9NRN9}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 20 minutes after fertilization in
CC embryos. {ECO:0000269|PubMed:31564433}.
CC -!- DISRUPTION PHENOTYPE: Microcephaly and curved tails.
CC {ECO:0000269|PubMed:31564433}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000305}.
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DR EMBL; BX321905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC083455; AAH83455.1; -; mRNA.
DR RefSeq; NP_001005949.1; NM_001005949.1.
DR AlphaFoldDB; F1QVR8; -.
DR SMR; F1QVR8; -.
DR STRING; 7955.ENSDARP00000090567; -.
DR PaxDb; F1QVR8; -.
DR Ensembl; ENSDART00000099794; ENSDARP00000090567; ENSDARG00000068893.
DR Ensembl; ENSDART00000169733; ENSDARP00000138303; ENSDARG00000068893.
DR GeneID; 449776; -.
DR KEGG; dre:449776; -.
DR CTD; 29081; -.
DR ZFIN; ZDB-GENE-041010-21; mettl5.
DR eggNOG; KOG3420; Eukaryota.
DR GeneTree; ENSGT00390000000227; -.
DR HOGENOM; CLU_074702_1_1_1; -.
DR OMA; DVVYSIH; -.
DR OrthoDB; 1528520at2759; -.
DR TreeFam; TF314953; -.
DR PRO; PR:F1QVR8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000068893; Expressed in mature ovarian follicle and 27 other tissues.
DR ExpressionAtlas; F1QVR8; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008988; F:rRNA (adenine-N6-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Synapse; Transferase.
FT CHAIN 1..207
FT /note="rRNA N6-adenosine-methyltransferase METTL5"
FT /id="PRO_0000449609"
FT BINDING 25
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 28
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 105..106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT CONFLICT 148
FT /note="S -> T (in Ref. 2; AAH83455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 23146 MW; D3F15CE8541F970A CRC64;
MKLKELESCL QQVDGFEEPK ILLEQYPTSP HIAGCMLYTI HNTFDDIQNK LVADLGCGCG
VLSIGAAVLD AGLCVGFDID EDALDIFRGN VEEFELPNID VVQCDVCSIG SSYAKKFDTV
IMNPPFGTKH NQGIDMQFLQ TAISMATSAV YSLHKTSTRD HIQKKANDWK VKMEVIAELR
YDLPASYKFH KKKSVDIQVD FIRFTPT
