ID U3JHF7_FICAL Unreviewed; 459 AA.
AC U3JHF7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=N6-adenosine-methyltransferase non-catalytic subunit {ECO:0000256|ARBA:ARBA00026130, ECO:0000256|RuleBase:RU369092};
DE AltName: Full=Methyltransferase-like protein 14 {ECO:0000256|ARBA:ARBA00032942, ECO:0000256|RuleBase:RU369092};
GN Name=METTL14 {ECO:0000313|Ensembl:ENSFALP00000002211.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000002211.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000002211.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000002211.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|RuleBase:RU369092}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with mettl3 to form an
CC antiparallel heterodimer that constitutes an active methyltransferase.
CC {ECO:0000256|RuleBase:RU369092}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369092}.
CC -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000256|PROSITE-
CC ProRule:PRU00489, ECO:0000256|RuleBase:RU369092}.
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DR RefSeq; XP_016153297.1; XM_016297811.1.
DR AlphaFoldDB; U3JHF7; -.
DR SMR; U3JHF7; -.
DR STRING; 59894.ENSFALP00000002211; -.
DR Ensembl; ENSFALT00000002223.2; ENSFALP00000002211.2; ENSFALG00000002126.2.
DR GeneID; 101812238; -.
DR KEGG; fab:101812238; -.
DR CTD; 57721; -.
DR eggNOG; KOG2097; Eukaryota.
DR GeneTree; ENSGT00550000075003; -.
DR HOGENOM; CLU_046318_1_0_1; -.
DR Proteomes; UP000016665; Chromosome 4.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0021861; P:forebrain radial glial cell differentiation; IEA:Ensembl.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:Ensembl.
DR GO; GO:0061157; P:mRNA destabilization; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:1901533; P:negative regulation of hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0045664; P:regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR InterPro; IPR045123; METTL14-like.
DR InterPro; IPR007757; MT-A70-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13107; N6-ADENOSINE-METHYLTRANSFERASE NON-CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR13107:SF0; N6-ADENOSINE-METHYLTRANSFERASE NON-CATALYTIC SUBUNIT; 1.
DR Pfam; PF05063; MT-A70; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51143; MT_A70; 1.
DR PROSITE; PS51592; SAM_MTA70L_2; 1.
PE 3: Inferred from homology;
KW Differentiation {ECO:0000256|RuleBase:RU369092};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369092};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW RNA-binding {ECO:0000256|RuleBase:RU369092}.
FT REGION 53..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 459 AA; 52519 MW; 0D9717D1FAF63975 CRC64;
MNSRLQEIRE RQKLRRQLLA QQLGAENADS IGAVLNSKDE QREIAETRET CRAAYDTSAP
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
//
