MET14_CHICK
ID MET14_CHICK Reviewed; 459 AA.
AC Q5ZK35;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=N6-adenosine-methyltransferase non-catalytic subunit;
DE AltName: Full=Methyltransferase-like protein 14;
GN Name=METTL14; ORFNames=RCJMB04_13h15;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720249; CAG31908.1; -; mRNA.
DR RefSeq; NP_001026319.1; NM_001031148.1.
DR RefSeq; XP_015131762.1; XM_015276276.1.
DR RefSeq; XP_015131763.1; XM_015276277.1.
DR AlphaFoldDB; Q5ZK35; -.
DR SMR; Q5ZK35; -.
DR STRING; 9031.ENSGALP00000041155; -.
DR PaxDb; Q5ZK35; -.
DR Ensembl; ENSGALT00000019584; ENSGALP00000019558; ENSGALG00000012000.
DR GeneID; 422684; -.
DR KEGG; gga:422684; -.
DR CTD; 57721; -.
DR VEuPathDB; HostDB:geneid_422684; -.
DR eggNOG; KOG2097; Eukaryota.
DR GeneTree; ENSGT00550000075003; -.
DR HOGENOM; CLU_046318_1_0_1; -.
DR InParanoid; Q5ZK35; -.
DR OMA; NINKPGH; -.
DR OrthoDB; 788192at2759; -.
DR PhylomeDB; Q5ZK35; -.
DR TreeFam; TF323641; -.
DR Reactome; R-GGA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR PRO; PR:Q5ZK35; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000012000; Expressed in spermatocyte 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 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..459
FT /note="N6-adenosine-methyltransferase non-catalytic
FT subunit"
FT /id="PRO_0000325793"
FT REGION 50..73
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 392..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..447
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"
SQ SEQUENCE 459 AA; 52521 MW; 97EA33EC814560C1 CRC64;
MNSRLQEIRE RQKLRRQLLA QQLGAENADS IGAVLNSKDD QREIAETRET CRASYDTSAP
NAKRKYPDEG EADEEEIEEY KDEVELQQDE ENLPYEEEIY KDSSTFLKGT QSLNPHNDYC
QHFVDTGHRP QNFIRDVGLA DRFEEYPKLR ELIRLKDELI SKSNTPPMYL QADLEAFDIR
ELKSKFDVIL LEPPLEEYYR ETGITANEKC WTWDDIMKLE IEEIAAPRSF VFLWCGSGEG
LDLGRVCLRK WGYRRCEDIC WIKTNKNNPG KTKTLDPKAV FQRTKEHCLM GIKGTVRRST
DGDFIHANVD IDLIITEEPE IGNIEKPVEI FHIIEHFCLG RRRLHLFGRD STIRPGWLTV
GPTLTNSNFN AETYSSYFTA PNSHLTGCTE EIERLRPKSP PPKSKSDRGG GAPRGGGRGG
TSAGRGERGR ERNRTNFRGE RGGFRGGRGG THRGGFPTR
