MET14_DANRE
ID MET14_DANRE Reviewed; 455 AA.
AC Q6NZ22;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=N6-adenosine-methyltransferase non-catalytic subunit;
DE AltName: Full=Methyltransferase-like protein 14;
GN Name=mettl14; ORFNames=zgc:77296;
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 MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-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; BC066377; AAH66377.1; -; mRNA.
DR RefSeq; NP_996954.1; NM_207071.1.
DR AlphaFoldDB; Q6NZ22; -.
DR SMR; Q6NZ22; -.
DR STRING; 7955.ENSDARP00000093767; -.
DR PaxDb; Q6NZ22; -.
DR Ensembl; ENSDART00000102993; ENSDARP00000093767; ENSDARG00000070278.
DR Ensembl; ENSDART00000180272; ENSDARP00000155942; ENSDARG00000112383.
DR GeneID; 404603; -.
DR KEGG; dre:404603; -.
DR CTD; 57721; -.
DR ZFIN; ZDB-GENE-040426-2328; mettl14.
DR eggNOG; KOG2097; Eukaryota.
DR GeneTree; ENSGT00550000075003; -.
DR HOGENOM; CLU_046318_1_0_1; -.
DR InParanoid; Q6NZ22; -.
DR OMA; NINKPGH; -.
DR OrthoDB; 788192at2759; -.
DR PhylomeDB; Q6NZ22; -.
DR TreeFam; TF323641; -.
DR Reactome; R-DRE-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR PRO; PR:Q6NZ22; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000070278; Expressed in blastula and 21 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 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; Reference proteome; RNA-binding; Spermatogenesis.
FT CHAIN 1..455
FT /note="N6-adenosine-methyltransferase non-catalytic
FT subunit"
FT /id="PRO_0000325794"
FT REGION 21..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..135
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 236..237
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 244..253
FT /note="Positively charged region required for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 254..257
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 277..286
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 296..297
FT /note="Positively charged region required for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 307..311
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT REGION 392..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Basic and acidic residues"
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 145
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT SITE 241
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT SITE 244
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT SITE 297
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
FT SITE 398
FT /note="Interaction with METTL3"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE5"
SQ SEQUENCE 455 AA; 52179 MW; 63BE722EEA7067C5 CRC64;
MNSRLQEIRE RQKLRRQLLA QQLGAESPDS IGAVLNSKDE QKEIEETRET CRASFDISVP
GAKRKCLNEG EDPEEDVEEQ KEDVEPQHQE ESGPYEEVYK DSSTFLKGTQ SLNPHNDYCQ
HFVDTGHRPQ NFIRDGGLAD RFEEYPKQRE LIRLKDELIS ATNTPPMYLQ ADPDTFDLRE
LKCKFDVILI EPPLEEYYRE SGIIANERFW NWDDIMKLNI EEISSIRSFV FLWCGSGEGL
DLGRMCLRKW GFRRCEDICW IKTNKNNPGK TKTLDPKAVF QRTKEHCLMG IKGTVRRSTD
GDFIHANVDI DLIITEEPEM GNIEKPVEIF HIIEHFCLGR RRLHLFGRDS TIRPGWLTVG
PTLTNSNFNI EVYSTHFSEP NSYLSGCTEE IERLRPKSPP PKSMAERGGG APRGGRGGPA
AGRGDRGRER NRPNFRGDRG GFRGRGGPHR GFPPR
