MET14_BOVIN
ID MET14_BOVIN Reviewed; 456 AA.
AC A4IFD8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=N6-adenosine-methyltransferase non-catalytic subunit;
DE AltName: Full=Methyltransferase-like protein 14;
GN Name=METTL14;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) 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 (By similarity). M6A acts
CC as a key regulator of mRNA stability by promoting mRNA destabilization
CC and degradation (By similarity). In embryonic stem cells (ESCs), m6A
CC methylation of mRNAs encoding key naive pluripotency-promoting
CC transcripts results in transcript destabilization (By similarity). M6A
CC regulates spermatogonial differentiation and meiosis and is essential
CC for male fertility and spermatogenesis (By similarity). M6A also
CC regulates cortical neurogenesis: m6A methylation of transcripts related
CC to transcription factors, neural stem cells, the cell cycle and
CC neuronal differentiation during brain development promotes their
CC destabilization and decay, promoting differentiation of radial glial
CC cells (By similarity). {ECO:0000250|UniProtKB:Q3UIK4,
CC 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. The
CC MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and,
CC in some cases of RBM15 (RBM15 or RBM15B).
CC {ECO:0000250|UniProtKB:Q9HCE5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HCE5}.
CC -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000255|PROSITE-
CC ProRule:PRU00489}.
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DR EMBL; BC134533; AAI34534.1; -; mRNA.
DR RefSeq; NP_001077183.1; NM_001083714.1.
DR AlphaFoldDB; A4IFD8; -.
DR SMR; A4IFD8; -.
DR STRING; 9913.ENSBTAP00000018721; -.
DR PaxDb; A4IFD8; -.
DR PRIDE; A4IFD8; -.
DR GeneID; 531382; -.
DR KEGG; bta:531382; -.
DR CTD; 57721; -.
DR eggNOG; KOG2097; Eukaryota.
DR InParanoid; A4IFD8; -.
DR OrthoDB; 788192at2759; -.
DR Proteomes; UP000009136; Unplaced.
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 InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13107; PTHR13107; 1.
DR Pfam; PF05063; MT-A70; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51143; MT_A70; 1.
PE 2: Evidence at transcript level;
KW Differentiation; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Spermatogenesis.
FT CHAIN 1..456
FT /note="N6-adenosine-methyltransferase non-catalytic
FT subunit"
FT /id="PRO_0000325789"
FT REGION 45..76
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 393..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
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"
FT SITE 399
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
SQ SEQUENCE 456 AA; 52193 MW; 1925B5113227E934 CRC64;
MDSRLQEIRE RQKLRRQLLA QQLGAESADS IGALLNSKDE QREIAETRET CRASYDTSAP
NAKRKYQDEG ETDEDKMEEY KDELEMQQEE ENLPYEEEIY KDSSTFLKGT QSLNPHNDYC
QHFVDTGHRP QNFIRDVGLA DRFEEYPKLR ELIRLKDELI AKSNTPPMYL QADIEAFDIR
ELTPKFDVIL LEPPLEEYYR ETGITANEKC WTWDDIMKLE IDEIAAPRSF IFLWCGSGEG
LDLGRVCLRK WGYRRCEDIC WIKTNKNNPG KTKTLDPKAV FQRTKEHCLM GIKGTVKRST
DGDFIHANVD IDLIITEEPE IGNIEKPVEI FHIIEHFCLG RRRLHLFGRD STIRPGWLTV
GPTLTNSNYN AETYASYFSA PNSYLTGCTE EIERLRPKSP PPKSKSDRGG GAPRGGGRGG
TSAGRGRERN RSNFRGERGG FRGGRGGAHR GGFPPR
