ID A0A384BZU9_URSMA Unreviewed; 456 AA.
AC A0A384BZU9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:ENSUMAP00000004443,
GN ECO:0000313|RefSeq:XP_008687685.1};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008687685.1};
RN [1] {ECO:0000313|Ensembl:ENSUMAP00000004443}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008687685.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008687685.1};
RG RefSeq;
RL Submitted (NOV-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. M6A acts as a key
CC regulator of mRNA stability by promoting mRNA destabilization and
CC degradation. In embryonic stem cells (ESCs), m6A methylation of mRNAs
CC encoding key naive pluripotency-promoting transcripts results in
CC transcript destabilization. M6A regulates spermatogonial
CC differentiation and meiosis and is essential for male fertility and
CC spermatogenesis. M6A also regulates cortical neurogenesis: m6A
CC methylation of transcripts related to transcription factors, neural
CC stem cells, the cell cycle and neuronal differentiation during brain
CC development promotes their destabilization and decay, promoting
CC differentiation of radial glial cells. {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_008687685.1; XM_008689463.2.
DR STRING; 29073.ENSUMAP00000004443; -.
DR Ensembl; ENSUMAT00000005404.1; ENSUMAP00000004443.1; ENSUMAG00000003593.1.
DR GeneID; 103661775; -.
DR KEGG; umr:103661775; -.
DR CTD; 57721; -.
DR OMA; FNSELYQ; -.
DR OrthoDB; 179166at2759; -.
DR Proteomes; UP000261680; Unplaced.
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:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:Ensembl.
DR GO; GO:0061157; P:mRNA destabilization; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:UniProtKB-UniRule.
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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Differentiation {ECO:0000256|RuleBase:RU369092};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369092};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
KW RNA-binding {ECO:0000256|RuleBase:RU369092};
KW Spermatogenesis {ECO:0000256|RuleBase:RU369092}.
FT REGION 47..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 456 AA; 52179 MW; 028E1579AA232A1D CRC64;
MDSRLQEIRE RQKLRRQLLA QQLGAESADS IGAVLNSKDE 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
//
