MET14_XENTR
ID MET14_XENTR Reviewed; 456 AA.
AC Q66KJ9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=N6-adenosine-methyltransferase non-catalytic subunit;
DE AltName: Full=Methyltransferase-like protein 14;
GN Name=mettl14;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The METTL3-METTL14 heterodimer forms a N6-methyltransferase
CC complex that methylates adenosine residues at the N(6) position of some
CC mRNAs and regulates the circadian clock, differentiation of embryonic
CC stem cells and cortical neurogenesis. In the heterodimer formed with
CC mettl3, mettl14 constitutes the RNA-binding scaffold that recognizes
CC the substrate rather than the catalytic core. N6-methyladenosine (m6A),
CC which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs,
CC plays a role in mRNA stability and processing.
CC {ECO:0000250|UniProtKB:Q3UIK4, ECO:0000250|UniProtKB:Q9HCE5}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with mettl3 to form an
CC antiparallel heterodimer that constitutes an active methyltransferase.
CC Component of the WMM complex, a N6-methyltransferase complex composed
CC of a catalytic subcomplex, named MAC, and of an associated subcomplex,
CC named MACOM. The MAC subcomplex is composed of mettl3 and mettl14.
CC {ECO:0000250|UniProtKB:Q9HCE5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3UIK4}.
CC -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000255|PROSITE-
CC ProRule:PRU00489}.
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DR EMBL; BC080361; AAH80361.1; -; mRNA.
DR RefSeq; NP_001007920.1; NM_001007919.1.
DR AlphaFoldDB; Q66KJ9; -.
DR SMR; Q66KJ9; -.
DR STRING; 8364.ENSXETP00000008737; -.
DR PaxDb; Q66KJ9; -.
DR DNASU; 493301; -.
DR Ensembl; ENSXETT00000008737; ENSXETP00000008737; ENSXETG00000004037.
DR GeneID; 493301; -.
DR KEGG; xtr:493301; -.
DR CTD; 57721; -.
DR Xenbase; XB-GENE-5813560; mettl14.
DR eggNOG; KOG2097; Eukaryota.
DR HOGENOM; CLU_046318_1_0_1; -.
DR InParanoid; Q66KJ9; -.
DR OMA; CEEDKRF; -.
DR OrthoDB; 788192at2759; -.
DR PhylomeDB; Q66KJ9; -.
DR TreeFam; TF323641; -.
DR Reactome; R-XTR-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000004037; Expressed in early embryo and 13 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0016422; F:mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0021861; P:forebrain radial glial cell differentiation; ISS:UniProtKB.
DR GO; GO:0042063; P:gliogenesis; ISS:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
DR InterPro; IPR045123; METTL14-like.
DR InterPro; IPR007757; MT-A70-like.
DR PANTHER; PTHR13107; PTHR13107; 1.
DR Pfam; PF05063; MT-A70; 1.
DR PROSITE; PS51143; MT_A70; 1.
PE 2: Evidence at transcript level;
KW Differentiation; Nucleus; Reference proteome; RNA-binding; Spermatogenesis.
FT CHAIN 1..456
FT /note="N6-adenosine-methyltransferase non-catalytic
FT subunit"
FT /id="PRO_0000325796"
FT REGION 39..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..136
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 237..238
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 245..254
FT /note="Positively charged region required for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 255..258
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 278..287
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 297..298
FT /note="Positively charged region required for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 308..312
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 395..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 146
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT SITE 242
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT SITE 245
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT SITE 298
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
SQ SEQUENCE 456 AA; 52043 MW; 64391412EA790E25 CRC64;
MNSRLQEIRA RQTLRRKLLA QQLGAESADS IGAVLNSKDE QREIAETRET SRASYDTSAT
VSKRKMPEEG EADEEVIEEC KDAVEPQKEE ENLPYREEIY KDSSTFLKGT QSLNPHNDYC
QHFVDTGHRP QNFIRDVGLA DRFEEYPKLR ELIRLKDELI SKSNTPPMYL QADLESFDLR
ELKSEFDVIL LEPPLEEYFR ETGIAANEKW WTWEDIMKLD IEGIAGSRAF VFLWCGSGEG
LDFGRMCLRK WGFRRSEDIC WIKTNKDNPG KTKTLDPKAI FQRTKEHCLM GIKGTVHRST
DGDFIHANVD IDLIITEEPE IGNIEKPVEI FHIIEHFCLG RRRLHLFGRD STIRPGWLTV
GPTLTNSNFN SETYASYFNT PNSPLTGCTE EIERLRPKTP PPKSDRGFGA SRGGGRGGPS
AGRGERGRER NRGSFRGDRG NFRGRGGPHR GVFAPR
